Source:http://linkedlifedata.com/resource/pubmed/id/11506180
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2001-8-16
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pubmed:abstractText |
Beta-1,4-galactosyltransferase 1 (beta1,4-GT 1) is the key enzyme transferring galactose to the terminal N-acetylglucosamine (GlcNAc) forming Galbeta3-->4GlcNAc structure in the Golgi apparatus. In addition, it also serves as a cell adhesion molecule by recognizing and binding to terminal GlcNAc of glycoconjugates on the adjacent cell surface and matrix through a subpopulation of the enzyme distributed on the cell surface. Transient expression of the p58GTA protein kinase, which belongs to the p34cdc2-related supergene family, could enhance beta1,4-GT 1 total activity in COS cells. In this study, the p58GTA interaction with beta1,4-GT 1 was confirmed using an in vitro assay with the TNT Coupled Reticulocyte Lysate System. An expression vector containing p58GTA was stably transfected into 7721 cells, a human hepatocarcinoma cell line, expression was confirmed by Northern and Western blot analyses. The cells transfected with p58GTA (p58GTA/7721) contained 1.9 times higher total beta1,4-GT 1 activity and 2.6 times higher cell-surface beta1,4-GT 1 activity than the mock transfected cells (pcDNA3/7721). However, Ricinus communis agglutinin-I lectin blot analysis revealed that the enhanced beta1,4-GT1 activity did not increase the Galbetal-->4GlcNAc groups on most of the membrane proteins in p58GTA/7721 cells. By flow cytometry analysis, it was found that the p58GTA/7721 cells were G2/M phase arrested, compared with the pcDNA3/7721 cells. These results suggest that the p58GTA stable transfection into human hepatocarcinoma cells could enhance the two beta1,4-GT1 subcellular pool activities independently and change its cell-cycle without modifying the beta-1,4-linked galactose residues on most membrane proteins.
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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/CDK11a protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ricinus communis agglutinin-1,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,4-galactosyltransferase I
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
221
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-8
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pubmed:dateRevised |
2011-10-10
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pubmed:meshHeading |
pubmed-meshheading:11506180-Animals,
pubmed-meshheading:11506180-Blotting, Northern,
pubmed-meshheading:11506180-COS Cells,
pubmed-meshheading:11506180-Carcinoma, Hepatocellular,
pubmed-meshheading:11506180-Cell Cycle,
pubmed-meshheading:11506180-Cyclin-Dependent Kinases,
pubmed-meshheading:11506180-Enzyme Activation,
pubmed-meshheading:11506180-Flow Cytometry,
pubmed-meshheading:11506180-Galactose,
pubmed-meshheading:11506180-Galactosyltransferases,
pubmed-meshheading:11506180-Glycoproteins,
pubmed-meshheading:11506180-Humans,
pubmed-meshheading:11506180-Lectins,
pubmed-meshheading:11506180-Membrane Proteins,
pubmed-meshheading:11506180-Plant Lectins,
pubmed-meshheading:11506180-Protein Kinases,
pubmed-meshheading:11506180-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11506180-RNA, Messenger,
pubmed-meshheading:11506180-Transfection,
pubmed-meshheading:11506180-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
Effect of p58GTA on beta-1,4-galactosyltransferase 1 activity and cell-cycle in human hepatocarcinoma cells.
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pubmed:affiliation |
Gene Research Center, Medical Center of Fudan University (Former Shanghai Medical University), Shanghai, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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