| Opposing changes in N-acetylglucosaminyltransferase-V and -III during the cell cycle and all-trans retinoic acid treatment of hepatocarcinoma cell line. | |
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MedLine Citation:
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PMID: 10699467 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The changes in N-acetylglucosaminyltransferase-V and -III (GnT-V, GnT-III) during the cell-cycle of synchronized 7721 human hepatocarcinoma cell line were investigated. Using an HPLC method to assay GnT and flow cytometry (FCM) for cell cycle analysis, it was found that GnT-V showed the highest activity, but GnT-III reached the lowest activity when G(2)/M cells were most abundant. In contrast, GnT-V declined to the minimum while GnT-III elevated to maximum when G(0)/G(1) cells were most predominant. The opposing changes were more obvious when the activities of GnT-V and GnT-III were expressed as relative activities (activity of GnT-V or GnT-III/the sum of activities of GnT-V plus GnT-IV plus GnT-III). These opposing changes of GnT-V and GnT-III during the cell cycle might result from the different regulatory mechanisms of GnT-V and GnT-III expression in the cell cycle. The alterations in the structures of cell surface N-glycans were compatible with the changes of the activities of GnTs. The results from immunocytochemistry and Northern blot showed that the protein and mRNA contents of GnT-V were not significantly changed during the cell cycle. The activity of a cell cycle regulating protein kinase, p34(cdc2) kinase, correlated to the activity of GnT-V. These findings suggested that the change of GnT-V activity in cell cycle was not the consequence of the alteration of gene transcription or enzyme protein synthesis, but might be caused by the post-translational regulation. The decrease in GnT-V and the corresponding increase in GnT-III activities were also found after the cells were treated with all-trans retinoic acid (ATRA), and the mechanism of this might be different from that in the cell cycle. |
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Authors:
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H B Guo; A L Jiang; T Z Ju; H L Chen |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1495 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2000 Feb |
Date Detail:
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Created Date: 2000-08-09 Completed Date: 2000-08-09 Revised Date: 2012-06-08 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 297-307 Citation Subset: IM |
Affiliation:
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Key Laboratory of Glycoconjugate Research, Ministry of Health, Department of Biochemistry, Shanghai Medical University, Shanghai, PR China. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Antineoplastic Agents
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pharmacology Carcinoma, Hepatocellular / pathology Cell Cycle / physiology Cyclin-Dependent Kinases* Flow Cytometry G0 Phase / physiology G1 Phase / physiology G2 Phase / physiology Horseradish Peroxidase / metabolism Humans Immunohistochemistry Lectins / metabolism Mitosis / physiology N-Acetylglucosaminyltransferases / analysis, genetics, metabolism* Protein-Serine-Threonine Kinases / genetics, metabolism RNA, Messenger / metabolism Tretinoin / pharmacology* Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Antineoplastic Agents; 0/Lectins; 0/RNA, Messenger; 302-79-4/Tretinoin; EC 1.11.1.-/Horseradish Peroxidase; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC 2.4.1.144/beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase; EC 2.4.1.155/alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.22/Cyclin-Dependent Kinases; EC 2.7.11.22/cyclin-dependent kinase-activating kinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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