PubMed:20855471 JSONTXT

{"project":"GlyCosmos15-Species","denotations":[{"id":"1","span":{"begin":40,"end":44},"obj":"Species"},{"id":"31","span":{"begin":439,"end":443},"obj":"Species"},{"id":"35","span":{"begin":853,"end":857},"obj":"Species"},{"id":"38","span":{"begin":1219,"end":1223},"obj":"Species"},{"id":"43","span":{"begin":1469,"end":1473},"obj":"Species"},{"id":"45","span":{"begin":1513,"end":1517},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"1","obj":"10090"},{"id":"A31","pred":"db_id","subj":"31","obj":"10090"},{"id":"A35","pred":"db_id","subj":"35","obj":"10090"},{"id":"A38","pred":"db_id","subj":"38","obj":"10090"},{"id":"A43","pred":"db_id","subj":"43","obj":"10090"},{"id":"A45","pred":"db_id","subj":"45","obj":"10090"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1304,"end":1310},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T2","span":{"begin":1581,"end":1587},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":58,"end":64},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":109,"end":115},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":310,"end":316},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":377,"end":383},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":581,"end":587},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1249,"end":1255},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1304,"end":1310},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1374,"end":1380},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1551,"end":1557},"obj":"Glycan_Motif"},{"id":"T10","span":{"begin":1581,"end":1587},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00037MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00033MO"},{"id":"A10","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1304,"end":1310},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T2","span":{"begin":1581,"end":1587},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":710,"end":725},"obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"T3","span":{"begin":716,"end":725},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T4","span":{"begin":727,"end":734},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T5","span":{"begin":736,"end":742},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T6","span":{"begin":744,"end":751},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"T7","span":{"begin":752,"end":759},"obj":"http://purl.obolibrary.org/obo/MAT_0000137"},{"id":"T8","span":{"begin":764,"end":770},"obj":"http://purl.obolibrary.org/obo/MAT_0000080"},{"id":"T9","span":{"begin":1311,"end":1319},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"T10","span":{"begin":1338,"end":1345},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T11","span":{"begin":1354,"end":1359},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T12","span":{"begin":1588,"end":1596},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"T13","span":{"begin":1778,"end":1785},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T14","span":{"begin":1889,"end":1894},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":744,"end":751},"obj":"http://purl.bioontology.org/ontology/ICD10/E06"},{"id":"T2","span":{"begin":744,"end":751},"obj":"http://purl.bioontology.org/ontology/ICD10/E06.9"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":400,"end":408},"obj":"FMAID:226027"},{"id":"_T2","span":{"begin":400,"end":408},"obj":"FMAID:226028"},{"id":"_T3","span":{"begin":527,"end":552},"obj":"FMAID:166102"},{"id":"_T4","span":{"begin":703,"end":708},"obj":"FMAID:14543"},{"id":"_T5","span":{"begin":703,"end":708},"obj":"FMAID:104231"},{"id":"_T6","span":{"begin":710,"end":725},"obj":"FMAID:204388"},{"id":"_T7","span":{"begin":710,"end":725},"obj":"FMAID:209219"},{"id":"_T8","span":{"begin":710,"end":725},"obj":"FMAID:104314"},{"id":"_T9","span":{"begin":710,"end":725},"obj":"FMAID:7200"},{"id":"_T10","span":{"begin":710,"end":725},"obj":"FMAID:93676"},{"id":"_T11","span":{"begin":716,"end":725},"obj":"FMAID:93674"},{"id":"_T12","span":{"begin":716,"end":725},"obj":"FMAID:226991"},{"id":"_T13","span":{"begin":716,"end":725},"obj":"FMAID:7199"},{"id":"_T14","span":{"begin":727,"end":734},"obj":"FMAID:7148"},{"id":"_T15","span":{"begin":727,"end":734},"obj":"FMAID:93576"},{"id":"_T16","span":{"begin":736,"end":742},"obj":"FMAID:93681"},{"id":"_T17","span":{"begin":736,"end":742},"obj":"FMAID:7203"},{"id":"_T18","span":{"begin":744,"end":751},"obj":"FMAID:13344"},{"id":"_T19","span":{"begin":744,"end":751},"obj":"FMAID:102701"},{"id":"_T20","span":{"begin":752,"end":759},"obj":"FMAID:7394"},{"id":"_T21","span":{"begin":752,"end":759},"obj":"FMAID:94012"},{"id":"_T22","span":{"begin":764,"end":770},"obj":"FMAID:9607"},{"id":"_T23","span":{"begin":764,"end":770},"obj":"FMAID:97496"},{"id":"_T24","span":{"begin":1068,"end":1077},"obj":"FMAID:226027"},{"id":"_T25","span":{"begin":1068,"end":1077},"obj":"FMAID:226028"},{"id":"_T26","span":{"begin":1190,"end":1197},"obj":"FMAID:256050"},{"id":"_T27","span":{"begin":1292,"end":1300},"obj":"FMAID:226028"},{"id":"_T28","span":{"begin":1292,"end":1300},"obj":"FMAID:226027"},{"id":"_T29","span":{"begin":1338,"end":1345},"obj":"FMAID:93576"},{"id":"_T30","span":{"begin":1338,"end":1345},"obj":"FMAID:7148"},{"id":"_T31","span":{"begin":1354,"end":1359},"obj":"FMAID:104231"},{"id":"_T32","span":{"begin":1354,"end":1359},"obj":"FMAID:14543"},{"id":"_T33","span":{"begin":1438,"end":1445},"obj":"FMAID:256050"},{"id":"_T34","span":{"begin":1572,"end":1580},"obj":"FMAID:226028"},{"id":"_T35","span":{"begin":1572,"end":1580},"obj":"FMAID:226027"},{"id":"_T36","span":{"begin":1778,"end":1785},"obj":"FMAID:93576"},{"id":"_T37","span":{"begin":1778,"end":1785},"obj":"FMAID:7148"},{"id":"_T38","span":{"begin":1889,"end":1894},"obj":"FMAID:104231"},{"id":"_T39","span":{"begin":1889,"end":1894},"obj":"FMAID:14543"},{"id":"_T40","span":{"begin":1895,"end":1902},"obj":"FMAID:256050"},{"id":"_T41","span":{"begin":1943,"end":1954},"obj":"FMAID:82780"},{"id":"_T42","span":{"begin":1943,"end":1954},"obj":"FMAID:196773"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":75,"end":107},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T2","span":{"begin":121,"end":152},"obj":"http://www.uniprot.org/uniprot/Q06430"},{"id":"T3","span":{"begin":75,"end":107},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T4","span":{"begin":121,"end":152},"obj":"http://www.uniprot.org/uniprot/Q8N0V5"},{"id":"T5","span":{"begin":75,"end":107},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T6","span":{"begin":121,"end":152},"obj":"http://www.uniprot.org/uniprot/Q8NFS9"},{"id":"T7","span":{"begin":213,"end":219},"obj":"http://www.uniprot.org/uniprot/Q9P109"},{"id":"T8","span":{"begin":796,"end":802},"obj":"http://www.uniprot.org/uniprot/Q9P109"},{"id":"T9","span":{"begin":1453,"end":1459},"obj":"http://www.uniprot.org/uniprot/Q9P109"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":75,"end":107},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T2","span":{"begin":121,"end":152},"obj":"http://www.uniprot.org/uniprot/P97402"},{"id":"T3","span":{"begin":213,"end":219},"obj":"http://www.uniprot.org/uniprot/E9Q649"},{"id":"T4","span":{"begin":796,"end":802},"obj":"http://www.uniprot.org/uniprot/E9Q649"},{"id":"T5","span":{"begin":1453,"end":1459},"obj":"http://www.uniprot.org/uniprot/E9Q649"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":66,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":66,"end":70},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T3","span":{"begin":752,"end":759},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/988164"},{"id":"T4","span":{"begin":764,"end":770},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/49990"},{"id":"T5","span":{"begin":1190,"end":1197},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T6","span":{"begin":1311,"end":1319},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/293542"},{"id":"T7","span":{"begin":1438,"end":1445},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T8","span":{"begin":1588,"end":1596},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/293542"},{"id":"T9","span":{"begin":1895,"end":1902},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":5,"end":16},"obj":"http://purl.obolibrary.org/obo/GO_0046960"},{"id":"T2","span":{"begin":361,"end":373},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":667,"end":677},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":1721,"end":1729},"obj":"http://purl.obolibrary.org/obo/GO_0097502"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":58,"end":62},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T2","span":{"begin":310,"end":314},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T3","span":{"begin":377,"end":381},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T4","span":{"begin":581,"end":585},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T5","span":{"begin":1062,"end":1066},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T6","span":{"begin":1249,"end":1253},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T7","span":{"begin":1304,"end":1308},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T8","span":{"begin":1374,"end":1378},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T9","span":{"begin":1551,"end":1555},"obj":"http://purl.obolibrary.org/obo/GO_0019013"},{"id":"T10","span":{"begin":109,"end":113},"obj":"http://purl.obolibrary.org/obo/GO_0019013"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Allie","denotations":[{"id":"SS1_20855471_1_0","span":{"begin":109,"end":152},"obj":"expanded"},{"id":"SS2_20855471_1_0","span":{"begin":154,"end":159},"obj":"abbr"}],"relations":[{"id":"AE1_20855471_1_0","pred":"abbreviatedTo","subj":"SS1_20855471_1_0","obj":"SS2_20855471_1_0"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T2","span":{"begin":710,"end":725},"obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"T3","span":{"begin":716,"end":725},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T4","span":{"begin":727,"end":734},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T5","span":{"begin":736,"end":742},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T6","span":{"begin":744,"end":751},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"T7","span":{"begin":752,"end":759},"obj":"http://purl.obolibrary.org/obo/MAT_0000137"},{"id":"T8","span":{"begin":764,"end":770},"obj":"http://purl.obolibrary.org/obo/MAT_0000080"},{"id":"T9","span":{"begin":1311,"end":1319},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"T10","span":{"begin":1338,"end":1345},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T11","span":{"begin":1354,"end":1359},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"T12","span":{"begin":1588,"end":1596},"obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"T13","span":{"begin":1778,"end":1785},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T14","span":{"begin":1889,"end":1894},"obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":108},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":109,"end":284},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":285,"end":409},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":410,"end":597},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":598,"end":858},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":859,"end":999},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1000,"end":1198},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1199,"end":1360},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1361,"end":1474},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1475,"end":1697},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1698,"end":1786},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1787,"end":1955},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":108},"obj":"Sentence"},{"id":"T2","span":{"begin":109,"end":284},"obj":"Sentence"},{"id":"T3","span":{"begin":285,"end":409},"obj":"Sentence"},{"id":"T4","span":{"begin":410,"end":597},"obj":"Sentence"},{"id":"T5","span":{"begin":598,"end":858},"obj":"Sentence"},{"id":"T6","span":{"begin":859,"end":1198},"obj":"Sentence"},{"id":"T7","span":{"begin":1199,"end":1360},"obj":"Sentence"},{"id":"T8","span":{"begin":1361,"end":1474},"obj":"Sentence"},{"id":"T9","span":{"begin":1475,"end":1697},"obj":"Sentence"},{"id":"T10","span":{"begin":1698,"end":1786},"obj":"Sentence"},{"id":"T11","span":{"begin":1787,"end":1955},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":108},"obj":"Sentence"},{"id":"T2","span":{"begin":109,"end":284},"obj":"Sentence"},{"id":"T3","span":{"begin":285,"end":409},"obj":"Sentence"},{"id":"T4","span":{"begin":410,"end":597},"obj":"Sentence"},{"id":"T5","span":{"begin":598,"end":858},"obj":"Sentence"},{"id":"T6","span":{"begin":859,"end":999},"obj":"Sentence"},{"id":"T7","span":{"begin":1000,"end":1198},"obj":"Sentence"},{"id":"T8","span":{"begin":1199,"end":1360},"obj":"Sentence"},{"id":"T9","span":{"begin":1361,"end":1474},"obj":"Sentence"},{"id":"T10","span":{"begin":1475,"end":1697},"obj":"Sentence"},{"id":"T11","span":{"begin":1698,"end":1786},"obj":"Sentence"},{"id":"T12","span":{"begin":1787,"end":1955},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1926,"end":1929},"obj":"http://www.glycoepitope.jp/epitopes/AN0279"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1190,"end":1197},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1438,"end":1445},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1895,"end":1902},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":703,"end":708},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":1354,"end":1359},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":1889,"end":1894},"obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":736,"end":742},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"PD-UBERON-AE-B_T8","span":{"begin":727,"end":734},"obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"PD-UBERON-AE-B_T9","span":{"begin":1338,"end":1345},"obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"PD-UBERON-AE-B_T10","span":{"begin":1778,"end":1785},"obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"PD-UBERON-AE-B_T11","span":{"begin":716,"end":725},"obj":"http://purl.obolibrary.org/obo/UBERON_0000160"},{"id":"PD-UBERON-AE-B_T12","span":{"begin":1311,"end":1319},"obj":"http://purl.obolibrary.org/obo/UBERON_0000972"},{"id":"PD-UBERON-AE-B_T13","span":{"begin":1588,"end":1596},"obj":"http://purl.obolibrary.org/obo/UBERON_0000972"},{"id":"PD-UBERON-AE-B_T14","span":{"begin":710,"end":725},"obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"PD-UBERON-AE-B_T15","span":{"begin":752,"end":759},"obj":"http://purl.obolibrary.org/obo/UBERON_0003126"},{"id":"PD-UBERON-AE-B_T16","span":{"begin":764,"end":770},"obj":"http://purl.obolibrary.org/obo/UBERON_0002370"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":58,"end":64},"obj":"Glycan"},{"id":"T2","span":{"begin":109,"end":115},"obj":"Glycan"},{"id":"T3","span":{"begin":310,"end":316},"obj":"Glycan"},{"id":"T4","span":{"begin":377,"end":383},"obj":"Glycan"},{"id":"T5","span":{"begin":581,"end":587},"obj":"Glycan"},{"id":"T6","span":{"begin":1249,"end":1255},"obj":"Glycan"},{"id":"T7","span":{"begin":1304,"end":1310},"obj":"Glycan"},{"id":"T8","span":{"begin":1374,"end":1380},"obj":"Glycan"},{"id":"T9","span":{"begin":1551,"end":1557},"obj":"Glycan"},{"id":"T10","span":{"begin":1581,"end":1587},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00037MO"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00037MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":58,"end":64},"obj":"Glycan"},{"id":"T2","span":{"begin":310,"end":316},"obj":"Glycan"},{"id":"T3","span":{"begin":377,"end":383},"obj":"Glycan"},{"id":"T4","span":{"begin":581,"end":587},"obj":"Glycan"},{"id":"T5","span":{"begin":1249,"end":1255},"obj":"Glycan"},{"id":"T6","span":{"begin":1304,"end":1310},"obj":"Glycan"},{"id":"T7","span":{"begin":1374,"end":1380},"obj":"Glycan"},{"id":"T8","span":{"begin":1551,"end":1557},"obj":"Glycan"},{"id":"T9","span":{"begin":1581,"end":1587},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A10","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A11","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00037MO"},{"id":"A12","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00037MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A13","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A14","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A15","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A16","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00033MO"},{"id":"A17","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00033MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A18","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":108},"obj":"Sentence"},{"id":"T2","span":{"begin":109,"end":284},"obj":"Sentence"},{"id":"T3","span":{"begin":285,"end":409},"obj":"Sentence"},{"id":"T4","span":{"begin":410,"end":597},"obj":"Sentence"},{"id":"T5","span":{"begin":598,"end":858},"obj":"Sentence"},{"id":"T6","span":{"begin":859,"end":1198},"obj":"Sentence"},{"id":"T7","span":{"begin":1199,"end":1360},"obj":"Sentence"},{"id":"T8","span":{"begin":1361,"end":1474},"obj":"Sentence"},{"id":"T9","span":{"begin":1475,"end":1697},"obj":"Sentence"},{"id":"T10","span":{"begin":1698,"end":1786},"obj":"Sentence"},{"id":"T11","span":{"begin":1787,"end":1955},"obj":"Sentence"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"Body_part"},{"id":"T2","span":{"begin":710,"end":725},"obj":"Body_part"},{"id":"T3","span":{"begin":727,"end":734},"obj":"Body_part"},{"id":"T4","span":{"begin":736,"end":742},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":751},"obj":"Body_part"},{"id":"T6","span":{"begin":752,"end":759},"obj":"Body_part"},{"id":"T9","span":{"begin":764,"end":770},"obj":"Body_part"},{"id":"T10","span":{"begin":1338,"end":1345},"obj":"Body_part"},{"id":"T11","span":{"begin":1354,"end":1359},"obj":"Body_part"},{"id":"T12","span":{"begin":1778,"end":1785},"obj":"Body_part"},{"id":"T13","span":{"begin":1889,"end":1894},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0003126"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0003127"},{"id":"A8","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_6005043"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0002370"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A13","pred":"uberon_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":40,"end":44},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":439,"end":443},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":764,"end":770},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":853,"end":857},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1219,"end":1223},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1469,"end":1473},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1513,"end":1517},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T3","obj":"49990"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10088"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10088"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10088"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10088"}],"namespaces":[{"prefix":"_base","uri":"https://glycosmos.org/organisms/"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":527,"end":552},"obj":"Body_part"},{"id":"T2","span":{"begin":703,"end":708},"obj":"Body_part"},{"id":"T3","span":{"begin":710,"end":725},"obj":"Body_part"},{"id":"T4","span":{"begin":727,"end":734},"obj":"Body_part"},{"id":"T5","span":{"begin":736,"end":742},"obj":"Body_part"},{"id":"T6","span":{"begin":752,"end":759},"obj":"Body_part"},{"id":"T7","span":{"begin":764,"end":770},"obj":"Body_part"},{"id":"T8","span":{"begin":1190,"end":1197},"obj":"Body_part"},{"id":"T9","span":{"begin":1338,"end":1345},"obj":"Body_part"},{"id":"T10","span":{"begin":1354,"end":1359},"obj":"Body_part"},{"id":"T11","span":{"begin":1438,"end":1445},"obj":"Body_part"},{"id":"T12","span":{"begin":1778,"end":1785},"obj":"Body_part"},{"id":"T13","span":{"begin":1889,"end":1894},"obj":"Body_part"},{"id":"T14","span":{"begin":1895,"end":1902},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:305751"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:14543"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:7200"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:7148"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:7203"},{"id":"A6","pred":"db_id","subj":"T6","obj":"FMA:7394"},{"id":"A7","pred":"db_id","subj":"T7","obj":"FMA:9607"},{"id":"A8","pred":"db_id","subj":"T8","obj":"FMA:9637"},{"id":"A9","pred":"db_id","subj":"T9","obj":"FMA:7148"},{"id":"A10","pred":"db_id","subj":"T10","obj":"FMA:14543"},{"id":"A11","pred":"db_id","subj":"T11","obj":"FMA:9637"},{"id":"A12","pred":"db_id","subj":"T12","obj":"FMA:7148"},{"id":"A13","pred":"db_id","subj":"T13","obj":"FMA:14543"},{"id":"A14","pred":"db_id","subj":"T14","obj":"FMA:9637"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"Body_part"},{"id":"T2","span":{"begin":710,"end":725},"obj":"Body_part"},{"id":"T3","span":{"begin":727,"end":734},"obj":"Body_part"},{"id":"T4","span":{"begin":736,"end":742},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":751},"obj":"Body_part"},{"id":"T6","span":{"begin":752,"end":759},"obj":"Body_part"},{"id":"T7","span":{"begin":764,"end":770},"obj":"Body_part"},{"id":"T8","span":{"begin":1311,"end":1319},"obj":"Body_part"},{"id":"T9","span":{"begin":1338,"end":1345},"obj":"Body_part"},{"id":"T10","span":{"begin":1354,"end":1359},"obj":"Body_part"},{"id":"T11","span":{"begin":1588,"end":1596},"obj":"Body_part"},{"id":"T12","span":{"begin":1778,"end":1785},"obj":"Body_part"},{"id":"T13","span":{"begin":1889,"end":1894},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000137"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000080"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A10","pred":"mat_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A11","pred":"mat_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"A12","pred":"mat_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A13","pred":"mat_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":40,"end":44},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":439,"end":443},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":752,"end":759},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":764,"end":770},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":853,"end":857},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1219,"end":1223},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1469,"end":1473},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1513,"end":1517},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T3","obj":"988164"},{"id":"A4","pred":"db_id","subj":"T4","obj":"49990"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10088"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10088"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10088"},{"id":"A8","pred":"db_id","subj":"T8","obj":"10088"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"Body_part"},{"id":"T2","span":{"begin":710,"end":725},"obj":"Body_part"},{"id":"T3","span":{"begin":727,"end":734},"obj":"Body_part"},{"id":"T4","span":{"begin":736,"end":742},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":751},"obj":"Body_part"},{"id":"T6","span":{"begin":752,"end":759},"obj":"Body_part"},{"id":"T7","span":{"begin":764,"end":770},"obj":"Body_part"},{"id":"T8","span":{"begin":1311,"end":1319},"obj":"Body_part"},{"id":"T9","span":{"begin":1338,"end":1345},"obj":"Body_part"},{"id":"T10","span":{"begin":1354,"end":1359},"obj":"Body_part"},{"id":"T11","span":{"begin":1588,"end":1596},"obj":"Body_part"},{"id":"T12","span":{"begin":1778,"end":1785},"obj":"Body_part"},{"id":"T13","span":{"begin":1889,"end":1894},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000137"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000080"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A10","pred":"mat_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MAT_0000526"},{"id":"A11","pred":"mat_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/MAT_0000086"},{"id":"A12","pred":"mat_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"A13","pred":"mat_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/MAT_0000526"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":703,"end":708},"obj":"Body_part"},{"id":"T2","span":{"begin":710,"end":725},"obj":"Body_part"},{"id":"T3","span":{"begin":727,"end":734},"obj":"Body_part"},{"id":"T4","span":{"begin":736,"end":742},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":751},"obj":"Body_part"},{"id":"T6","span":{"begin":752,"end":759},"obj":"Body_part"},{"id":"T9","span":{"begin":764,"end":770},"obj":"Body_part"},{"id":"T10","span":{"begin":1338,"end":1345},"obj":"Body_part"},{"id":"T11","span":{"begin":1354,"end":1359},"obj":"Body_part"},{"id":"T12","span":{"begin":1778,"end":1785},"obj":"Body_part"},{"id":"T13","span":{"begin":1889,"end":1894},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0003126"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0003127"},{"id":"A8","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_6005043"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0002370"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A13","pred":"uberon_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/UBERON_0001155"}],"text":"High-sensitivity O-glycomic analysis of mice deficient in core 2 {beta}1,6-N-acetylglucosaminyltransferases.\nCore 2 β1,6-N-acetylglucosaminyltransferase (C2GnT), which exists in three isoforms, C2GnT1, C2GnT2 and C2GnT3, is one of the key enzymes in the O-glycan biosynthetic pathway. These isoenzymes produce core 2 O-glycans and have been correlated with the biosynthesis of core 4 O-glycans and I-branches. Previously, we have reported mice with single and multiple deficiencies of C2GnT isoenzyme(s) and have evaluated the biological and structural consequences of the loss of core 2 function. We now present more comprehensive O-glycomic analyses of neutral and sialylated glycans expressed in the colon, small intestine, stomach, kidney, thyroid/trachea and thymus of wild-type, C2GnT2 and C2GnT3 single knockouts and the C2GnT1-3 triple knockout mice. Very high-quality data have emerged from our mass spectrometry techniques with the capability of detecting O-glycans up to at least 3500 Da. We were able to unambiguously elucidate the types of O-glycan core, branching location and residue linkages, which allowed us to exhaustively characterize structural changes in the knockout tissues. The C2GnT2 knockout mice suffered a major loss of core 2 O-glycans as well as glycans with I-branches on core 1 antennae especially in the stomach and the colon. In contrast, core 2 O-glycans still dominated the O-glycomic profile of most tissues in the C2GnT3 knockout mice. Analysis of the C2GnT triple knockout mice revealed a complete loss of both core 2 O-glycans and branched core 1 antennae, confirming that the three known isoenzymes are entirely responsible for producing these structures. Unexpectedly, O-linked mannosyl glycans are upregulated in the triple deficient stomach. In addition, our studies have revealed an interesting terminal structure detected on O-glycans of the colon tissues that is similar to the RM2 antigen from glycolipids."}