PubMed:12361956 JSONTXT

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":112,"end":120},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T2","span":{"begin":251,"end":266},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T3","span":{"begin":270,"end":278},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T4","span":{"begin":403,"end":418},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T5","span":{"begin":460,"end":468},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T6","span":{"begin":505,"end":513},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T7","span":{"begin":538,"end":546},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T8","span":{"begin":660,"end":668},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T9","span":{"begin":843,"end":858},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T10","span":{"begin":902,"end":910},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T11","span":{"begin":1141,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T12","span":{"begin":1246,"end":1254},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T13","span":{"begin":1312,"end":1327},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T14","span":{"begin":1373,"end":1381},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T15","span":{"begin":1412,"end":1420},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T16","span":{"begin":1449,"end":1464},"obj":"https://acgg.asia/db/ggdb/info/gg075"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":112,"end":120},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T2","span":{"begin":251,"end":266},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T3","span":{"begin":270,"end":278},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T4","span":{"begin":403,"end":418},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T5","span":{"begin":460,"end":468},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T6","span":{"begin":505,"end":513},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T7","span":{"begin":538,"end":546},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T8","span":{"begin":660,"end":668},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T9","span":{"begin":843,"end":858},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T10","span":{"begin":902,"end":910},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T11","span":{"begin":1141,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T12","span":{"begin":1246,"end":1254},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T13","span":{"begin":1312,"end":1327},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"T14","span":{"begin":1373,"end":1381},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T15","span":{"begin":1412,"end":1420},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"T16","span":{"begin":1449,"end":1464},"obj":"https://acgg.asia/db/ggdb/info/gg075"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":148,"end":154},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":251,"end":257},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":403,"end":409},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":843,"end":849},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1087,"end":1093},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1109,"end":1115},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1312,"end":1318},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1449,"end":1455},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"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/G00031MO"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":177},"obj":"Sentence"},{"id":"T2","span":{"begin":178,"end":367},"obj":"Sentence"},{"id":"T3","span":{"begin":368,"end":469},"obj":"Sentence"},{"id":"T4","span":{"begin":470,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":821},"obj":"Sentence"},{"id":"T6","span":{"begin":822,"end":916},"obj":"Sentence"},{"id":"T7","span":{"begin":917,"end":1104},"obj":"Sentence"},{"id":"T8","span":{"begin":1105,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1382},"obj":"Sentence"},{"id":"T10","span":{"begin":1383,"end":1540},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":148,"end":154},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T2","span":{"begin":251,"end":257},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T3","span":{"begin":403,"end":409},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T4","span":{"begin":843,"end":849},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T5","span":{"begin":1087,"end":1093},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T6","span":{"begin":1109,"end":1115},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T7","span":{"begin":1312,"end":1318},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T8","span":{"begin":1449,"end":1455},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T2","span":{"begin":744,"end":758},"obj":"http://purl.obolibrary.org/obo/MAT_0000079"},{"id":"T3","span":{"begin":753,"end":758},"obj":"http://purl.obolibrary.org/obo/MAT_0000021"},{"id":"T4","span":{"begin":760,"end":767},"obj":"http://purl.obolibrary.org/obo/MAT_0000051"},{"id":"T5","span":{"begin":769,"end":784},"obj":"http://purl.obolibrary.org/obo/MAT_0000047"},{"id":"T6","span":{"begin":775,"end":784},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T7","span":{"begin":786,"end":792},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"T8","span":{"begin":794,"end":800},"obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"id":"T9","span":{"begin":802,"end":808},"obj":"http://purl.obolibrary.org/obo/MAT_0000080"},{"id":"T10","span":{"begin":814,"end":820},"obj":"http://purl.obolibrary.org/obo/MAT_0000085"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":112,"end":120},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":270,"end":278},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":280,"end":283},"obj":"https://acgg.asia/db/ggdb/info/gg135"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":460,"end":468},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":505,"end":513},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":538,"end":546},"obj":"https://acgg.asia/db/ggdb/info/gg075"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":584,"end":586},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":660,"end":668},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":902,"end":910},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":1141,"end":1149},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1246,"end":1254},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1373,"end":1381},"obj":"https://acgg.asia/db/ggdb/info/gg076"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1412,"end":1420},"obj":"https://acgg.asia/db/ggdb/info/gg076"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":148,"end":154},"obj":"Glycan"},{"id":"T2","span":{"begin":251,"end":257},"obj":"Glycan"},{"id":"T3","span":{"begin":403,"end":409},"obj":"Glycan"},{"id":"T4","span":{"begin":843,"end":849},"obj":"Glycan"},{"id":"T5","span":{"begin":995,"end":1001},"obj":"Glycan"},{"id":"T6","span":{"begin":1029,"end":1035},"obj":"Glycan"},{"id":"T7","span":{"begin":1087,"end":1093},"obj":"Glycan"},{"id":"T8","span":{"begin":1109,"end":1115},"obj":"Glycan"},{"id":"T9","span":{"begin":1312,"end":1318},"obj":"Glycan"},{"id":"T10","span":{"begin":1449,"end":1455},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"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/G00031MO"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"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":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":303,"end":306},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":802,"end":808},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"49990"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":587,"end":595},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":758},"obj":"Body_part"},{"id":"T6","span":{"begin":760,"end":767},"obj":"Body_part"},{"id":"T7","span":{"begin":769,"end":784},"obj":"Body_part"},{"id":"T8","span":{"begin":786,"end":792},"obj":"Body_part"},{"id":"T9","span":{"begin":794,"end":800},"obj":"Body_part"},{"id":"T10","span":{"begin":802,"end":808},"obj":"Body_part"},{"id":"T11","span":{"begin":814,"end":820},"obj":"Body_part"},{"id":"T12","span":{"begin":1523,"end":1539},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A4","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001044"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0002370"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0002106"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0013765"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":744,"end":758},"obj":"Body_part"},{"id":"T3","span":{"begin":760,"end":767},"obj":"Body_part"},{"id":"T4","span":{"begin":769,"end":784},"obj":"Body_part"},{"id":"T5","span":{"begin":786,"end":792},"obj":"Body_part"},{"id":"T6","span":{"begin":794,"end":800},"obj":"Body_part"},{"id":"T7","span":{"begin":802,"end":808},"obj":"Body_part"},{"id":"T8","span":{"begin":814,"end":820},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000079"},{"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_0000047"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"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_0000085"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":177},"obj":"Sentence"},{"id":"T2","span":{"begin":178,"end":367},"obj":"Sentence"},{"id":"T3","span":{"begin":368,"end":469},"obj":"Sentence"},{"id":"T4","span":{"begin":470,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":821},"obj":"Sentence"},{"id":"T6","span":{"begin":822,"end":916},"obj":"Sentence"},{"id":"T7","span":{"begin":917,"end":1104},"obj":"Sentence"},{"id":"T8","span":{"begin":1105,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1382},"obj":"Sentence"},{"id":"T10","span":{"begin":1383,"end":1540},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":177},"obj":"Sentence"},{"id":"T2","span":{"begin":178,"end":367},"obj":"Sentence"},{"id":"T3","span":{"begin":368,"end":469},"obj":"Sentence"},{"id":"T4","span":{"begin":470,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":821},"obj":"Sentence"},{"id":"T6","span":{"begin":822,"end":916},"obj":"Sentence"},{"id":"T7","span":{"begin":917,"end":1104},"obj":"Sentence"},{"id":"T8","span":{"begin":1105,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1382},"obj":"Sentence"},{"id":"T10","span":{"begin":1383,"end":1540},"obj":"Sentence"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":148,"end":154},"obj":"Glycan"},{"id":"T2","span":{"begin":251,"end":257},"obj":"Glycan"},{"id":"T3","span":{"begin":403,"end":409},"obj":"Glycan"},{"id":"T4","span":{"begin":843,"end":849},"obj":"Glycan"},{"id":"T5","span":{"begin":995,"end":1001},"obj":"Glycan"},{"id":"T6","span":{"begin":1029,"end":1035},"obj":"Glycan"},{"id":"T7","span":{"begin":1087,"end":1093},"obj":"Glycan"},{"id":"T8","span":{"begin":1109,"end":1115},"obj":"Glycan"},{"id":"T9","span":{"begin":1312,"end":1318},"obj":"Glycan"},{"id":"T10","span":{"begin":1449,"end":1455},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":177},"obj":"Sentence"},{"id":"T2","span":{"begin":178,"end":367},"obj":"Sentence"},{"id":"T3","span":{"begin":368,"end":469},"obj":"Sentence"},{"id":"T4","span":{"begin":470,"end":604},"obj":"Sentence"},{"id":"T5","span":{"begin":605,"end":821},"obj":"Sentence"},{"id":"T6","span":{"begin":822,"end":916},"obj":"Sentence"},{"id":"T7","span":{"begin":917,"end":1104},"obj":"Sentence"},{"id":"T8","span":{"begin":1105,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1382},"obj":"Sentence"},{"id":"T10","span":{"begin":1383,"end":1540},"obj":"Sentence"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":303,"end":306},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":802,"end":808},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"49990"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":587,"end":595},"obj":"Body_part"},{"id":"T5","span":{"begin":744,"end":758},"obj":"Body_part"},{"id":"T6","span":{"begin":760,"end":767},"obj":"Body_part"},{"id":"T7","span":{"begin":769,"end":784},"obj":"Body_part"},{"id":"T8","span":{"begin":786,"end":792},"obj":"Body_part"},{"id":"T9","span":{"begin":794,"end":800},"obj":"Body_part"},{"id":"T10","span":{"begin":802,"end":808},"obj":"Body_part"},{"id":"T11","span":{"begin":814,"end":820},"obj":"Body_part"},{"id":"T12","span":{"begin":1523,"end":1539},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A4","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001044"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000945"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0002108"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000473"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0002370"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0002106"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0013765"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":307,"end":312},"obj":"Body_part"},{"id":"T2","span":{"begin":744,"end":758},"obj":"Body_part"},{"id":"T3","span":{"begin":760,"end":767},"obj":"Body_part"},{"id":"T4","span":{"begin":769,"end":784},"obj":"Body_part"},{"id":"T5","span":{"begin":786,"end":792},"obj":"Body_part"},{"id":"T6","span":{"begin":794,"end":800},"obj":"Body_part"},{"id":"T7","span":{"begin":802,"end":808},"obj":"Body_part"},{"id":"T8","span":{"begin":814,"end":820},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000079"},{"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_0000047"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000119"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000132"},{"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_0000085"}],"text":"Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.\nRecently, a UDP-Gal:GalNAc(alpha) peptide beta1,3-galactosyltransferase (core 1 synthase 1; C1Gal-T1) has been purified from rat liver and its complementary DNA cloned from several species. We isolated a second candidate for core 1 synthase from a Colo205 cDNA library and named it C1Gal-T2. The deduced amino acid sequence of C1Gal-T2, having 26% homology to C1Gal-T1, showed a topology typical of a type II membrane protein. Real time PCR analysis revealed that the expression of C1Gal-T2 transcripts was widespread in many tissues and of relatively high level in salivary gland, stomach, small intestine, kidney, testis, thymus, and spleen. LSC cells, having no core 1 synthase activity, were transfected stably with the C1Gal-T2 gene. Their microsome fraction showed beta1,3-galactosyltransferase activity toward GalNAc-alpha-para-nitrophenyl and GalNAc(alpha)1 peptides resulting in the synthesis of the core 1 structure. The core 1 synthesizing activity of C1Gal-T2 was also determined by flow cytometry and lectin blotting using the LSC cells stably expressing C1Gal-T2. Finally, LSC cells, and Jurkat cells that also lack the core 1 synthase activity, were found to have null alleles of C1Gal-T2. These results indicated that C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs."}