Studies of the action of ceramide-like substances ( d - and l -PDMP) on sphingolipid glycosyltransferases and purified lactosylceramide synthase
dc.contributor.author | Chatterjee, Subroto | en_US |
dc.contributor.author | Cleveland, Tavia | en_US |
dc.contributor.author | Shi, Wan-Yang | en_US |
dc.contributor.author | Inokuchi, Jin-Ichi | en_US |
dc.contributor.author | Radin, Norman S. | en_US |
dc.date.accessioned | 2006-09-11T16:22:24Z | |
dc.date.available | 2006-09-11T16:22:24Z | |
dc.date.issued | 1996-06 | en_US |
dc.identifier.citation | Chatterjee, 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.issn | 0282-0080 | en_US |
dc.identifier.issn | 1573-4986 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45706 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8781979&dopt=citation | en_US |
dc.description.abstract | We 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.extent | 610769 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Chapman & Hall ; Springer Science+Business Media | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Pathology | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | PDMP (1-phenyl-2-decanoylamino-3-morpholino-1-propanol) | en_US |
dc.subject.other | Glucosylceramide | en_US |
dc.subject.other | Lactosylceramide | en_US |
dc.subject.other | Globotriaosylceramide | en_US |
dc.subject.other | Globotetraosylceramide | en_US |
dc.subject.other | Inhibition and Stimulation by PDMP Enantiomers | en_US |
dc.title | Studies of the action of ceramide-like substances ( d - and l -PDMP) on sphingolipid glycosyltransferases and purified lactosylceramide synthase | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Dentistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Nephrology Division, University of Michigan Medical School, 48109-0676, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | School of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USA | en_US |
dc.contributor.affiliationother | School of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USA | en_US |
dc.contributor.affiliationother | School of Medicine, Johns Hopkins University, 600 N. Wolfe St, CMSC 604, 21287-3654, Baltimore, MD, USA | en_US |
dc.contributor.affiliationother | Seikagaku Corp., Tokyo Institute, Higashiyamato, 207, Tokyo, Japan | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 8781979 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45706/1/10719_2004_Article_BF00731481.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00731481 | en_US |
dc.identifier.source | Glycoconjugate Journal | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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