Source:http://linkedlifedata.com/resource/pubmed/id/12754287
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2003-5-19
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pubmed:abstractText |
Mucin O-glycosylation in cancer is characterized by aberrant expression of immature carbohydrate structures leading to exposure of simple mucin-type carbohydrate antigens and peptide epitopes. Glycosyltransferases controlling the initial steps of mucin O-glycosylation are responsible for the altered glycosylation observed in cancer. We studied the expression in gastric cell lines of six UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-T1, T2, T3, T4, T6, T11) that catalyze the initial key step in the regulation of mucin O-glycosylation, the transfer of GalNAc from UDP-GalNAc to serine and threonine residues. We also studied the expression of ST6GalNAc-I, the enzyme responsible for the synthesis of Sialyl-Tn antigen (NeuAcalpha2,6GalNAc) and the ST3Gal-I, the enzyme responsible for the synthesis of Sialyl-T antigen (NeuAcalpha2,3Galbeta1,3GalNAc). This study was done using specific monoclonal antibodies, enzymatic assays, and RT-PCR. Our results showed that GalNAc-T1, -T2, and -T3 have an ubiquitous expression in all gastric cell lines, whereas GalNAc-T4, -T6, and -T11 show a restricted expression pattern. The immunoreactivity with MAb VU-2-G7 suggests that, apart from GalNAc-T4, another GalNAc transferase is involved in the glycosylation of the Thr in the PDTR region of the MUC1 tandem repeat. The expression of ST3Gal-I correlates with the expression of the Sialyl-T antigen in gastric cell lines and in the control cell lines studied. The expression of ST6GalNAc-I is low in gastric cell lines, in accordance with the low/absent expression of the Sialyl-Tn antigen.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Tumor-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/CMP-N-acetylneuraminate-alpha-N-acet...,
http://linkedlifedata.com/resource/pubmed/chemical/Mucin-1,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylgalactosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Sialyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-galactoside...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1554
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
761-71
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12754287-Antibodies, Monoclonal,
pubmed-meshheading:12754287-Antigens, Tumor-Associated, Carbohydrate,
pubmed-meshheading:12754287-Fluorescent Antibody Technique,
pubmed-meshheading:12754287-Humans,
pubmed-meshheading:12754287-Mucin-1,
pubmed-meshheading:12754287-N-Acetylgalactosaminyltransferases,
pubmed-meshheading:12754287-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12754287-Sialyltransferases,
pubmed-meshheading:12754287-Stomach Neoplasms,
pubmed-meshheading:12754287-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines.
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pubmed:affiliation |
Institute of Molecular Pathology and Immunology of the University of Porto, Porto, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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