| Glycosylation of amphipathic lactoside primers with consequent inhibition of endogenous glycosphingolipid synthesis. | |
MedLine Citation:
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PMID: 9644257 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The incubation of amphipathic lactosides with cultured cells was found to prime the glycosylation of lactosides whose oligosaccharide structures were exactly the same as those of glycosphingolipids produced by cells: B16 melanoma cells produced alpha2-3 sialylated lactosides; and PC12 cells, Galalpha1-4- and Galalpha1-3Galalpha1-4lactosides. Analysis of the cell-associated glycosylated products indicated that C16 series lactoside primers function 5-6 times more efficiently as acceptors than C12 series primers. The glycosylated lactosides were also secreted into the culture medium. Lactoside primers with longer hydrophobic chains hampered the release of glycosylated products from cells. The presence of an N-acyl chain in the lipophilic moiety of primers suppressed the secretion of glycosylated products. Owing to its overall availability, lactosides with the C12 alkyl chain were glycosylated 2-3 times more than C16 series lactosides and 1.4 times more than lactosides with the C12 acyl chain. C8-lactosides did not function as primers under the conditions of this study, but they were found to be the best acceptors for sialic acid transfer with the soluble enzyme fraction. The incubation of cells with 10 microM N-hexadecanoylaminoethyl-beta-O-lactoside caused a 30% decrease in endogenous GM3 of B16 cells and a 34% decrease in Gb3Cer synthesis of PC12 cells. The results of the present study demonstrate that lactoside primers serve as an efficient means to inhibit endogenous glycosphingolipids in studies to clarify glycosphingolipid functions. |
Authors:
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H Nakajima; Y Miura; T Yamagata |
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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: Journal of biochemistry Volume: 124 ISSN: 0021-924X ISO Abbreviation: J. Biochem. Publication Date: 1998 Jul |
Date Detail:
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Created Date: 1998-09-21 Completed Date: 1998-09-21 Revised Date: 2007-12-19 |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: JAPAN |
Other Details:
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Languages: eng Pagination: 148-56 Citation Subset: IM |
Affiliation:
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Department of Biomolecular Engineering, Tokyo Institute of Technology, Midori-ku, Yokohama, 226-8501, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Division / drug effects Culture Media Glycosides / metabolism*, pharmacology Glycosphingolipids / antagonists & inhibitors, biosynthesis* Glycosylation Melanoma, Experimental / metabolism, pathology PC12 Cells Rats Sialyltransferases / metabolism Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Culture Media; 0/Glycosides; 0/Glycosphingolipids; 0/lactosides; EC 2.4.99.-/Sialyltransferases; EC 2.4.99.4/beta-galactoside alpha-2,3-sialyltransferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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