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Titolo:
INHIBITION OF THE INTRINSIC NAD(+) GLYCOHYDROLASE ACTIVITY OF CD38 BYCARBOCYCLIC NAD ANALOGS
Autore:
WALL KA; KLIS M; KORNET J; COYLE D; AME JC; JACOBSON MK; SLAMA JT;
Indirizzi:
UNIV TOLEDO,COLL PHARM,DEPT MED & BIOL CHEM,2801 W BANCROFT ST TOLEDOOH 43606 UNIV TOLEDO,COLL PHARM,DEPT MED & BIOL CHEM TOLEDO OH 43606 UNIV KENTUCKY,COLL PHARM,DIV MED CHEM & PHARMACEUT LEXINGTON KY 40536
Titolo Testata:
Biochemical journal
, volume: 335, anno: 1998,
parte:, 3
pagine: 631 - 636
SICI:
0264-6021(1998)335:<631:IOTING>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC ADP-RIBOSE; NICOTINAMIDE-ADENINE-DINUCLEOTIDE; LYMPHOCYTE ANTIGEN CD38; SURFACE; HYDROLYSIS; MECHANISM; CYCLASE; CELLS; ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
K.A. Wall et al., "INHIBITION OF THE INTRINSIC NAD(+) GLYCOHYDROLASE ACTIVITY OF CD38 BYCARBOCYCLIC NAD ANALOGS", Biochemical journal, 335, 1998, pp. 631-636

Abstract

Carba-NAD and pseudocarba-NAD are carbocyclic analogues of NAD(+) in which a 2,3-dihydroxycyclopentane methanol replaces the beta-D-ribonucleotide ring of the nicotinamide riboside moiety of NAD(+) [Slama and Simmons (1988) Biochemistry 27, 183-193]. These carbocyclic NAD(+) analogues, related to each other as diastereomers, have been tested as inhibitors of the intrinsic NAD(+) glycohydrolase activity of human CD38, dog spleen NAD(+) glycohydrolase, mouse CD38 and Aplysia californicacADP-ribose synthetase. Pseudocarba-NAD, the carbocyclic dinucleotidein which L-2,3-dihydroxycyclopentane methanol replaces the D-ribose of the nicotinamide riboside moiety of NAD(+), was found to be the morepotent inhibitor. Pseudocarba-NAD was shown to inhibit the intrinsic NAD(+) glycohydrolase activity of human CD38 competitively, with K-i= 148 mu M determined for the recombinant extracellular protein domain and K-1 = 180 mu M determined for the native protein expressed as a cell-surface enzyme on cultured Jurkat cells. Pseudocarba-NAD was shown to be a non-competitive inhibitor of the purified dog spleen NAD(+) glycohydrolase, with K-is = 47 mu M and K-ii =198 mu M. Neither pseudocarba-NAD nor carba-NAD inhibited mouse CD38 or Aplysia californica cADP-ribose synthetase significantly at concentrations up to 1 mM. The results underscore significant species differences in the sensitivity of these enzymes to inhibition, and indicate that pseudocarba-NAD will be useful as an inhibitor of the enzymic activity of human but not mouse CD38 in studies using cultured cells.

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Documento generato il 04/12/20 alle ore 18:47:20