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Studies of the action of ceramide-like substances ( d - and l -PDMP) on sphingolipid glycosyltransferases and purified lactosylceramide synthase

dc.contributor.authorChatterjee, Subrotoen_US
dc.contributor.authorCleveland, Taviaen_US
dc.contributor.authorShi, Wan-Yangen_US
dc.contributor.authorInokuchi, Jin-Ichien_US
dc.contributor.authorRadin, Norman S.en_US
dc.date.accessioned2006-09-11T16:22:24Z
dc.date.available2006-09-11T16:22:24Z
dc.date.issued1996-06en_US
dc.identifier.citationChatterjee, Subroto; Cleveland, Tavia; Shi, Wan-Yang; Inokuchi, Jin-Ichi; Radin, Norman S.; (1996). "Studies of the action of ceramide-like substances ( d - and l -PDMP) on sphingolipid glycosyltransferases and purified lactosylceramide synthase." Glycoconjugate Journal 13(3): 481-486. <http://hdl.handle.net/2027.42/45706>en_US
dc.identifier.issn0282-0080en_US
dc.identifier.issn1573-4986en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/45706
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8781979&dopt=citationen_US
dc.description.abstractWe have studied the effects of D -threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol ( D -PDMP) and its L -enantiomer on glycosphingolipids in cultured normal human kidney proximal tubular cells. We found that D -PDMP exerted a concentration-dependent reduction in the metabolic labelling and cellular levels of glucosylceramide (GlcCer), lactosylceramide (LacCer), and the globo-series glycosphingolipids, GbOse 3 Cer and GbOse 4 Cer. It also directly inhibited the activity of UDP-glucose:ceramide β1 → 4-glucosyltransferase (GlcT-1) and UDP-galactose: GlcCer β1 → 4 galactosyltransferase (GalT-2). In contrast, L -PDMP had opposite effects on the metabolic labelling of GlcCer, LacCer, and GbOse 3 Cer. The levels of GlcCer and LacCer were increased, while the labelling and level of GbOse 4 Cer were strongly reduced. Purified GalT-2 from human kidney was inhibited by D -PDMP and stimulated by L -PDMP. It appears likely that the different glycosphingolipid glycosyltransferases possess similar binding sites for the ceramide moiety, which are blocked by binding to D -PDMP and, in the case of GbOse 4 Cer synthase, by L -PDMP as well. The stimulatory effects of L -PDMP on GlcCer and LacCer synthases may be the result of binding to a modulatory site on the glycosyltransferases; in intact cells, the enzyme-analog complex may afford protection against the normal catabolic inactivation of the enzymes.en_US
dc.format.extent610769 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; Chapman & Hall ; Springer Science+Business Mediaen_US
dc.subject.otherLife Sciencesen_US
dc.subject.otherPathologyen_US
dc.subject.otherBiochemistry, Generalen_US
dc.subject.otherPDMP (1-phenyl-2-decanoylamino-3-morpholino-1-propanol)en_US
dc.subject.otherGlucosylceramideen_US
dc.subject.otherLactosylceramideen_US
dc.subject.otherGlobotriaosylceramideen_US
dc.subject.otherGlobotetraosylceramideen_US
dc.subject.otherInhibition and Stimulation by PDMP Enantiomersen_US
dc.titleStudies of the action of ceramide-like substances ( d - and l -PDMP) on sphingolipid glycosyltransferases and purified lactosylceramide synthaseen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelDentistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumNephrology Division, University of Michigan Medical School, 48109-0676, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherSchool of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USAen_US
dc.contributor.affiliationotherSchool of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USAen_US
dc.contributor.affiliationotherSchool of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USAen_US
dc.contributor.affiliationotherSeikagaku Corp., Tokyo Institute, Higashiyamato, 207, Tokyo, Japanen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid8781979en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/45706/1/10719_2004_Article_BF00731481.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1007/BF00731481en_US
dc.identifier.sourceGlycoconjugate Journalen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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