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rdf:type |
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lifeskim:mentions |
umls-concept:C0003320,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0027882,
umls-concept:C0040005,
umls-concept:C0077730,
umls-concept:C0086418,
umls-concept:C1171362,
umls-concept:C1515670,
umls-concept:C1524084,
umls-concept:C1880022
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pubmed:issue |
1
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pubmed:dateCreated |
2002-12-30
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pubmed:databankReference |
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pubmed:abstractText |
To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human. In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13. In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1. Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1. pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes. pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1. In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1. pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons. pp-GalNAc-T13-deficient mice have been established in a previous work. Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse. pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Tumor-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/MUC5AC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muc5ac protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Mucin 5AC,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylgalactosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SDC3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sdc3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-3,
http://linkedlifedata.com/resource/pubmed/chemical/Tn antigen,
http://linkedlifedata.com/resource/pubmed/chemical/polypeptide...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:ChengLameiL,
pubmed-author:GotohMasanoriM,
pubmed-author:GuoJianmingJ,
pubmed-author:HennetThierryT,
pubmed-author:HisatomiHisashiH,
pubmed-author:InabaNiroN,
pubmed-author:IwasakiHirokoH,
pubmed-author:KalkaTimothy BTB,
pubmed-author:KubotaTomomiT,
pubmed-author:KudoTakashiT,
pubmed-author:MarthJamey DJD,
pubmed-author:NakajimaKazuyukiK,
pubmed-author:NakamuraMitsuruM,
pubmed-author:NarimatsuHisashiH,
pubmed-author:NishiharaShokoS,
pubmed-author:TogayachiAkiraA,
pubmed-author:WangHanH,
pubmed-author:ZhangYanY
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
573-84
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12407114-Amino Acid Sequence,
pubmed-meshheading:12407114-Animals,
pubmed-meshheading:12407114-Antigens, Tumor-Associated, Carbohydrate,
pubmed-meshheading:12407114-Astrocytes,
pubmed-meshheading:12407114-Base Sequence,
pubmed-meshheading:12407114-Cells, Cultured,
pubmed-meshheading:12407114-Cerebellar Cortex,
pubmed-meshheading:12407114-Chromatography, High Pressure Liquid,
pubmed-meshheading:12407114-Cloning, Molecular,
pubmed-meshheading:12407114-Glycopeptides,
pubmed-meshheading:12407114-Glycosylation,
pubmed-meshheading:12407114-Humans,
pubmed-meshheading:12407114-Membrane Glycoproteins,
pubmed-meshheading:12407114-Mice,
pubmed-meshheading:12407114-Mice, Knockout,
pubmed-meshheading:12407114-Molecular Sequence Data,
pubmed-meshheading:12407114-Mucin 5AC,
pubmed-meshheading:12407114-Mucins,
pubmed-meshheading:12407114-N-Acetylgalactosaminyltransferases,
pubmed-meshheading:12407114-Neurons,
pubmed-meshheading:12407114-Proteoglycans,
pubmed-meshheading:12407114-Recombinant Proteins,
pubmed-meshheading:12407114-Sequence Alignment,
pubmed-meshheading:12407114-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:12407114-Substrate Specificity,
pubmed-meshheading:12407114-Syndecan-3,
pubmed-meshheading:12407114-Tissue Distribution
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pubmed:year |
2003
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pubmed:articleTitle |
Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
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pubmed:affiliation |
Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Central-2, Open Space Laboratory, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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