Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2001-8-16
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
221
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-8
pubmed:dateRevised
2011-10-10
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
pubmed:year
2001
pubmed:articleTitle
Effect of p58GTA on beta-1,4-galactosyltransferase 1 activity and cell-cycle in human hepatocarcinoma cells.
pubmed:affiliation
Gene Research Center, Medical Center of Fudan University (Former Shanghai Medical University), Shanghai, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't