PubMed:12244074 JSONTXT

Annnotations TAB JSON ListView MergeView

    Glycan-Motif

    {"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":77,"end":97},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":726,"end":737},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T3","span":{"begin":987,"end":998},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T4","span":{"begin":1114,"end":1134},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T5","span":{"begin":1144,"end":1151},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T6","span":{"begin":1144,"end":1151},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T7","span":{"begin":1248,"end":1262},"obj":"https://glytoucan.org/Structures/Glycans/G13157WZ"},{"id":"T8","span":{"begin":1263,"end":1270},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T9","span":{"begin":1263,"end":1270},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T10","span":{"begin":1627,"end":1647},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos6-Glycan-Motif-Image

    {"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":77,"end":97},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":726,"end":737},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":987,"end":998},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1114,"end":1134},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1144,"end":1151},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1248,"end":1262},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1263,"end":1270},"obj":"Glycan_Motif"},{"id":"T10","span":{"begin":1627,"end":1647},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G01187XC"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00051MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G13157WZ"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G01187XC"},{"id":"A9","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00051MO"},{"id":"A10","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1546,"end":1705},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"T13","span":{"begin":1546,"end":1705},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"T13","span":{"begin":1546,"end":1705},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos6-Glycan-Motif-Structure

    {"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":77,"end":97},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":726,"end":737},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T3","span":{"begin":987,"end":998},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T4","span":{"begin":1114,"end":1134},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T5","span":{"begin":1144,"end":1151},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T6","span":{"begin":1144,"end":1151},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T7","span":{"begin":1248,"end":1262},"obj":"https://glytoucan.org/Structures/Glycans/G13157WZ"},{"id":"T8","span":{"begin":1263,"end":1270},"obj":"https://glytoucan.org/Structures/Glycans/G00051MO"},{"id":"T9","span":{"begin":1263,"end":1270},"obj":"https://glytoucan.org/Structures/Glycans/G01187XC"},{"id":"T10","span":{"begin":1627,"end":1647},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    Glycosmos6-GlycoEpitope

    {"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":726,"end":737},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":987,"end":998},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T3","span":{"begin":1144,"end":1151},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"T4","span":{"begin":1248,"end":1262},"obj":"http://www.glycoepitope.jp/epitopes/EP0141"},{"id":"T5","span":{"begin":1263,"end":1270},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    Glycan-GlyCosmos

    {"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":726,"end":737},"obj":"Glycan"},{"id":"T2","span":{"begin":987,"end":998},"obj":"Glycan"},{"id":"T3","span":{"begin":1136,"end":1142},"obj":"Glycan"},{"id":"T4","span":{"begin":1144,"end":1151},"obj":"Glycan"},{"id":"T5","span":{"begin":1248,"end":1262},"obj":"Glycan"},{"id":"T6","span":{"begin":1263,"end":1270},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A7","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A8","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G66213AR"},{"id":"A9","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66213AR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A10","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G13157WZ"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G13157WZ"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlycoBiology-FMA

    {"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":24,"end":36},"obj":"FMAID:82737"},{"id":"_T2","span":{"begin":24,"end":36},"obj":"FMAID:197276"},{"id":"_T3","span":{"begin":77,"end":97},"obj":"FMAID:82786"},{"id":"_T4","span":{"begin":77,"end":97},"obj":"FMAID:196780"},{"id":"_T5","span":{"begin":86,"end":97},"obj":"FMAID:82792"},{"id":"_T6","span":{"begin":86,"end":97},"obj":"FMAID:196787"},{"id":"_T7","span":{"begin":174,"end":183},"obj":"FMAID:167148"},{"id":"_T8","span":{"begin":174,"end":183},"obj":"FMAID:62852"},{"id":"_T9","span":{"begin":197,"end":206},"obj":"FMAID:167164"},{"id":"_T10","span":{"begin":197,"end":206},"obj":"FMAID:62864"},{"id":"_T11","span":{"begin":225,"end":233},"obj":"FMAID:84050"},{"id":"_T12","span":{"begin":225,"end":233},"obj":"FMAID:197972"},{"id":"_T13","span":{"begin":460,"end":469},"obj":"FMAID:197972"},{"id":"_T14","span":{"begin":460,"end":469},"obj":"FMAID:84050"},{"id":"_T15","span":{"begin":512,"end":524},"obj":"FMAID:197276"},{"id":"_T16","span":{"begin":512,"end":524},"obj":"FMAID:82737"},{"id":"_T17","span":{"begin":585,"end":597},"obj":"FMAID:212684"},{"id":"_T18","span":{"begin":585,"end":597},"obj":"FMAID:200942"},{"id":"_T19","span":{"begin":590,"end":597},"obj":"FMAID:146300"},{"id":"_T20","span":{"begin":590,"end":597},"obj":"FMAID:50594"},{"id":"_T21","span":{"begin":598,"end":605},"obj":"FMAID:67257"},{"id":"_T22","span":{"begin":598,"end":605},"obj":"FMAID:165447"},{"id":"_T23","span":{"begin":609,"end":622},"obj":"FMAID:171182"},{"id":"_T24","span":{"begin":609,"end":622},"obj":"FMAID:199064"},{"id":"_T25","span":{"begin":609,"end":622},"obj":"FMAID:70339"},{"id":"_T26","span":{"begin":617,"end":622},"obj":"FMAID:169002"},{"id":"_T27","span":{"begin":617,"end":622},"obj":"FMAID:68646"},{"id":"_T28","span":{"begin":636,"end":648},"obj":"FMAID:171182"},{"id":"_T29","span":{"begin":636,"end":648},"obj":"FMAID:70339"},{"id":"_T30","span":{"begin":636,"end":648},"obj":"FMAID:199064"},{"id":"_T31","span":{"begin":708,"end":725},"obj":"FMAID:63011"},{"id":"_T32","span":{"begin":708,"end":725},"obj":"FMAID:167395"},{"id":"_T33","span":{"begin":726,"end":745},"obj":"FMAID:196838"},{"id":"_T34","span":{"begin":726,"end":745},"obj":"FMAID:82837"},{"id":"_T35","span":{"begin":987,"end":1006},"obj":"FMAID:196838"},{"id":"_T36","span":{"begin":987,"end":1006},"obj":"FMAID:82837"},{"id":"_T37","span":{"begin":1114,"end":1134},"obj":"FMAID:82786"},{"id":"_T38","span":{"begin":1114,"end":1134},"obj":"FMAID:196780"},{"id":"_T39","span":{"begin":1123,"end":1134},"obj":"FMAID:196787"},{"id":"_T40","span":{"begin":1123,"end":1134},"obj":"FMAID:82792"},{"id":"_T41","span":{"begin":1161,"end":1166},"obj":"FMAID:169002"},{"id":"_T42","span":{"begin":1161,"end":1166},"obj":"FMAID:68646"},{"id":"_T43","span":{"begin":1203,"end":1211},"obj":"FMAID:167180"},{"id":"_T44","span":{"begin":1417,"end":1430},"obj":"FMAID:197276"},{"id":"_T45","span":{"begin":1417,"end":1430},"obj":"FMAID:82737"},{"id":"_T46","span":{"begin":1434,"end":1447},"obj":"FMAID:199064"},{"id":"_T47","span":{"begin":1434,"end":1447},"obj":"FMAID:171182"},{"id":"_T48","span":{"begin":1434,"end":1447},"obj":"FMAID:70339"},{"id":"_T49","span":{"begin":1442,"end":1447},"obj":"FMAID:68646"},{"id":"_T50","span":{"begin":1442,"end":1447},"obj":"FMAID:169002"},{"id":"_T51","span":{"begin":1504,"end":1516},"obj":"FMAID:82737"},{"id":"_T52","span":{"begin":1504,"end":1516},"obj":"FMAID:197276"},{"id":"_T53","span":{"begin":1627,"end":1647},"obj":"FMAID:196781"},{"id":"_T54","span":{"begin":1627,"end":1647},"obj":"FMAID:82787"},{"id":"_T55","span":{"begin":1636,"end":1647},"obj":"FMAID:196792"},{"id":"_T56","span":{"begin":1636,"end":1647},"obj":"FMAID:82797"},{"id":"_T57","span":{"begin":1691,"end":1704},"obj":"FMAID:171182"},{"id":"_T58","span":{"begin":1691,"end":1704},"obj":"FMAID:199064"},{"id":"_T59","span":{"begin":1691,"end":1704},"obj":"FMAID:70339"},{"id":"_T60","span":{"begin":1699,"end":1704},"obj":"FMAID:68646"},{"id":"_T61","span":{"begin":1699,"end":1704},"obj":"FMAID:169002"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    uniprot-human

    {"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T2","span":{"begin":263,"end":266},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T3","span":{"begin":490,"end":493},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T4","span":{"begin":756,"end":759},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T5","span":{"begin":915,"end":918},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T6","span":{"begin":1070,"end":1073},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T7","span":{"begin":1457,"end":1460},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T8","span":{"begin":0,"end":9},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T9","span":{"begin":263,"end":272},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T10","span":{"begin":490,"end":499},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T11","span":{"begin":756,"end":765},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T12","span":{"begin":915,"end":924},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T13","span":{"begin":1070,"end":1079},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T14","span":{"begin":1457,"end":1466},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T15","span":{"begin":234,"end":255},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T16","span":{"begin":50,"end":54},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T17","span":{"begin":126,"end":130},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T18","span":{"begin":285,"end":289},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T19","span":{"begin":343,"end":347},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T20","span":{"begin":422,"end":426},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T21","span":{"begin":538,"end":542},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T22","span":{"begin":544,"end":548},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T23","span":{"begin":671,"end":675},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T24","span":{"begin":788,"end":792},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T25","span":{"begin":898,"end":902},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T26","span":{"begin":965,"end":969},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T27","span":{"begin":1359,"end":1363},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T28","span":{"begin":1388,"end":1392},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T29","span":{"begin":1540,"end":1544},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T30","span":{"begin":1683,"end":1687},"obj":"http://www.uniprot.org/uniprot/Q9UCB0"},{"id":"T31","span":{"begin":234,"end":255},"obj":"http://www.uniprot.org/uniprot/Q06643"},{"id":"T32","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/P26022"},{"id":"T33","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/P26022"},{"id":"T34","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/P26022"},{"id":"T35","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/P98066"},{"id":"T36","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/P98066"},{"id":"T37","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/P98066"},{"id":"T38","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/P20827"},{"id":"T39","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/P20827"},{"id":"T40","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/P20827"},{"id":"T41","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/Q03169"},{"id":"T42","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/Q03169"},{"id":"T43","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/Q03169"},{"id":"T44","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/P21580"},{"id":"T45","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/P21580"},{"id":"T46","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/P21580"},{"id":"T47","span":{"begin":490,"end":507},"obj":"http://www.uniprot.org/uniprot/O95379"},{"id":"T48","span":{"begin":915,"end":932},"obj":"http://www.uniprot.org/uniprot/O95379"},{"id":"T49","span":{"begin":1070,"end":1087},"obj":"http://www.uniprot.org/uniprot/O95379"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    uniprot-mouse

    {"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T2","span":{"begin":263,"end":266},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T3","span":{"begin":490,"end":493},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T4","span":{"begin":756,"end":759},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T5","span":{"begin":915,"end":918},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T6","span":{"begin":1070,"end":1073},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T7","span":{"begin":1457,"end":1460},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T8","span":{"begin":0,"end":9},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T9","span":{"begin":263,"end":272},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T10","span":{"begin":490,"end":499},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T11","span":{"begin":756,"end":765},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T12","span":{"begin":915,"end":924},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T13","span":{"begin":1070,"end":1079},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T14","span":{"begin":1457,"end":1466},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T15","span":{"begin":234,"end":255},"obj":"http://www.uniprot.org/uniprot/P06804"},{"id":"T16","span":{"begin":50,"end":54},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T17","span":{"begin":126,"end":130},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T18","span":{"begin":285,"end":289},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T19","span":{"begin":343,"end":347},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T20","span":{"begin":422,"end":426},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T21","span":{"begin":538,"end":542},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T22","span":{"begin":544,"end":548},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T23","span":{"begin":671,"end":675},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T24","span":{"begin":788,"end":792},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T25","span":{"begin":898,"end":902},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T26","span":{"begin":965,"end":969},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T27","span":{"begin":1359,"end":1363},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T28","span":{"begin":1388,"end":1392},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T29","span":{"begin":1540,"end":1544},"obj":"http://www.uniprot.org/uniprot/Q62409"},{"id":"T30","span":{"begin":1683,"end":1687},"obj":"http://www.uniprot.org/uniprot/Q62409"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlycoBiology-NCBITAXON

    {"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":366,"end":372},"obj":"http://purl.bioontology.org/ontology/STY/T051"},{"id":"T2","span":{"begin":617,"end":622},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":1161,"end":1166},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1192,"end":1202},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T5","span":{"begin":1442,"end":1447},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T6","span":{"begin":1699,"end":1704},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GO-BP

    {"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T2","span":{"begin":135,"end":144},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T3","span":{"begin":290,"end":299},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T4","span":{"begin":409,"end":418},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T5","span":{"begin":525,"end":534},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":676,"end":685},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":793,"end":802},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T8","span":{"begin":858,"end":867},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T9","span":{"begin":970,"end":979},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T10","span":{"begin":1046,"end":1055},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T11","span":{"begin":576,"end":584},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T12","span":{"begin":738,"end":745},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T13","span":{"begin":999,"end":1006},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T14","span":{"begin":174,"end":192},"obj":"http://purl.obolibrary.org/obo/GO_0007159"},{"id":"T15","span":{"begin":240,"end":248},"obj":"http://purl.obolibrary.org/obo/GO_0001906"},{"id":"T16","span":{"begin":240,"end":248},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T17","span":{"begin":240,"end":248},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T18","span":{"begin":240,"end":248},"obj":"http://purl.obolibrary.org/obo/GO_0070265"},{"id":"T19","span":{"begin":585,"end":605},"obj":"http://purl.obolibrary.org/obo/GO_0034394"},{"id":"T20","span":{"begin":585,"end":605},"obj":"http://purl.obolibrary.org/obo/GO_0033575"},{"id":"T21","span":{"begin":585,"end":605},"obj":"http://purl.obolibrary.org/obo/GO_0033580"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GO-MF

    {"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":1203,"end":1211},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GO-CC

    {"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":585,"end":589},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":617,"end":622},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":1161,"end":1166},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1442,"end":1447},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1699,"end":1704},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":585,"end":597},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    EDAM-topics

    {"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":24,"end":36},"obj":"http://edamontology.org/topic_0152"},{"id":"T2","span":{"begin":512,"end":524},"obj":"http://edamontology.org/topic_0152"},{"id":"T3","span":{"begin":598,"end":605},"obj":"http://edamontology.org/topic_0078"},{"id":"T4","span":{"begin":1417,"end":1430},"obj":"http://edamontology.org/topic_0152"},{"id":"T5","span":{"begin":1504,"end":1516},"obj":"http://edamontology.org/topic_0152"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    EDAM-DFO

    {"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":310,"end":320},"obj":"http://edamontology.org/operation_3465"},{"id":"T2","span":{"begin":598,"end":605},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":598,"end":605},"obj":"http://edamontology.org/data_1467"},{"id":"T4","span":{"begin":1178,"end":1186},"obj":"http://edamontology.org/operation_2423"},{"id":"T5","span":{"begin":1370,"end":1382},"obj":"http://edamontology.org/operation_2246"},{"id":"T6","span":{"begin":1562,"end":1574},"obj":"http://edamontology.org/operation_2246"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlycoBiology-Motifs

    {"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":86,"end":97},"obj":"http://rdf.glycoinfo.org/glycan/G00055MO"},{"id":"T2","span":{"begin":1123,"end":1134},"obj":"http://rdf.glycoinfo.org/glycan/G00055MO"},{"id":"T3","span":{"begin":726,"end":737},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T4","span":{"begin":987,"end":998},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T5","span":{"begin":726,"end":745},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T6","span":{"begin":987,"end":1006},"obj":"http://rdf.glycoinfo.org/glycan/G00018MO"},{"id":"T7","span":{"begin":1144,"end":1149},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T8","span":{"begin":1263,"end":1268},"obj":"http://rdf.glycoinfo.org/glycan/G00047MO"},{"id":"T9","span":{"begin":1144,"end":1151},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"},{"id":"T10","span":{"begin":1263,"end":1270},"obj":"http://rdf.glycoinfo.org/glycan/G00051MO"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlycoBiology-Epitope

    {"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1144,"end":1151},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":1263,"end":1270},"obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":726,"end":737},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":987,"end":998},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":1248,"end":1262},"obj":"http://www.glycoepitope.jp/epitopes/EP0141"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    mondo_disease

    {"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":234,"end":239},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    HP-phenotype

    {"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":234,"end":239},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos-GlycoEpitope

    {"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":726,"end":737},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":987,"end":998},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1144,"end":1151},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1248,"end":1262},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1263,"end":1270},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0141"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0011"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-HP

    {"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":234,"end":239},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-UBERON

    {"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":174,"end":183},"obj":"Body_part"},{"id":"T2","span":{"begin":197,"end":206},"obj":"Body_part"},{"id":"T4","span":{"begin":609,"end":622},"obj":"Body_part"},{"id":"T5","span":{"begin":636,"end":648},"obj":"Body_part"},{"id":"T6","span":{"begin":1434,"end":1447},"obj":"Body_part"},{"id":"T7","span":{"begin":1691,"end":1704},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000576"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0001054"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000763"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-MONDO

    {"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":234,"end":239},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-CL

    {"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":174,"end":183},"obj":"Cell"},{"id":"T2","span":{"begin":197,"end":206},"obj":"Cell"},{"id":"T4","span":{"begin":609,"end":622},"obj":"Cell"},{"id":"T5","span":{"begin":636,"end":648},"obj":"Cell"},{"id":"T6","span":{"begin":1434,"end":1447},"obj":"Cell"},{"id":"T7","span":{"begin":1691,"end":1704},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A3","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000763"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1546,"end":1705},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"T13","span":{"begin":1546,"end":1705},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"T13","span":{"begin":1546,"end":1705},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-Sentences

    {"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":193},"obj":"Sentence"},{"id":"T3","span":{"begin":194,"end":373},"obj":"Sentence"},{"id":"T4","span":{"begin":374,"end":470},"obj":"Sentence"},{"id":"T5","span":{"begin":471,"end":543},"obj":"Sentence"},{"id":"T6","span":{"begin":544,"end":623},"obj":"Sentence"},{"id":"T7","span":{"begin":624,"end":746},"obj":"Sentence"},{"id":"T8","span":{"begin":747,"end":903},"obj":"Sentence"},{"id":"T9","span":{"begin":904,"end":1056},"obj":"Sentence"},{"id":"T10","span":{"begin":1057,"end":1242},"obj":"Sentence"},{"id":"T11","span":{"begin":1243,"end":1364},"obj":"Sentence"},{"id":"T12","span":{"begin":1365,"end":1545},"obj":"Sentence"},{"id":"T13","span":{"begin":1546,"end":1705},"obj":"Sentence"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-Glycan

    {"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":726,"end":737},"obj":"Glycan"},{"id":"T2","span":{"begin":987,"end":998},"obj":"Glycan"},{"id":"T3","span":{"begin":1136,"end":1142},"obj":"Glycan"},{"id":"T4","span":{"begin":1144,"end":1151},"obj":"Glycan"},{"id":"T5","span":{"begin":1248,"end":1262},"obj":"Glycan"},{"id":"T6","span":{"begin":1263,"end":1270},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A7","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A8","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G66213AR"},{"id":"A9","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66213AR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A10","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G13157WZ"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G13157WZ"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00051MO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00051MO"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    GlyCosmos15-GlycoEpitope

    {"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":726,"end":737},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":987,"end":998},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1144,"end":1151},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1248,"end":1262},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1263,"end":1270},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0011"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0141"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0011"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    Anatomy-UBERON

    {"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":174,"end":183},"obj":"Body_part"},{"id":"T2","span":{"begin":197,"end":206},"obj":"Body_part"},{"id":"T4","span":{"begin":609,"end":622},"obj":"Body_part"},{"id":"T5","span":{"begin":636,"end":648},"obj":"Body_part"},{"id":"T6","span":{"begin":1434,"end":1447},"obj":"Body_part"},{"id":"T7","span":{"begin":1691,"end":1704},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000576"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0001054"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000763"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000763"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}

    CL-cell

    {"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":174,"end":183},"obj":"Cell"},{"id":"T2","span":{"begin":197,"end":206},"obj":"Cell"},{"id":"T4","span":{"begin":609,"end":622},"obj":"Cell"},{"id":"T5","span":{"begin":636,"end":648},"obj":"Cell"},{"id":"T6","span":{"begin":1434,"end":1447},"obj":"Cell"},{"id":"T7","span":{"begin":1691,"end":1704},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000738"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A3","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000763"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000763"}],"text":"TNF-alpha increases the carbohydrate sulfation of CD44: induction of 6-sulfo N-acetyl lactosamine on N- and O-linked glycans.\nCD44 and sulfation have both been implicated in leukocyte adhesion. In monocytes, the inflammatory cytokine tumor necrosis factor alpha (TNF-alpha) stimulates CD44 sulfation, and this correlates with the induction of CD44-mediated adhesion events. However, little is known about the sulfation of CD44 or its induction by inflammatory cytokines. We determined that TNF-alpha induces the carbohydrate sulfation of CD44. CD44 was established as a major sulfated cell surface protein on myeloid cells. In the SR91 myeloid cell line, the majority of CD44 sulfation was attributed to the glycosaminoglycan chondroitin sulfate. However, TNF-alpha stimulation increased CD44 sulfation two- to threefold, largely attributed to the increased sulfation of N- and O-linked glycans on CD44. Therefore, TNF-alpha induced a decrease in the percentage of CD44 sulfation due to chondroitin sulfate and an increase due to N- and O-linked sulfation. Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. This 6-sulfo LacNAc/Lewis x epitope was induced on N-linked and (to a lesser extent) on O-linked glycans present on CD44. This demonstrates that CD44 is modified by sulfated carbohydrates in myeloid cells and that TNF-alpha modifies both the type and amount of carbohydrate sulfation occurring on CD44. In addition, it demonstrates that TNF-alpha can induce the expression of 6-sulfo N-acetyl glucosamine on both N- and O-linked glycans of CD44 in myeloid cells."}