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Titolo:
2'-PHOSPHO-CYCLIC ADP-RIBOSE, A CALCIUM-MOBILIZING AGENT DERIVED FROMNADP
Autore:
VU CQ; LU PJ; CHEN CS; JACOBSON MK;
Indirizzi:
UNIV KENTUCKY,COLL PHARM,DIV MED CHEM & PHARMACEUT LEXINGTON KY 40536 UNIV KENTUCKY,COLL PHARM,DIV MED CHEM & PHARMACEUT LEXINGTON KY 40536 UNIV KENTUCKY,MED CTR,LUCILLE P MARKEY CANC CTR LEXINGTON KY 40536
Titolo Testata:
The Journal of biological chemistry
fascicolo: 9, volume: 271, anno: 1996,
pagine: 4747 - 4754
SICI:
0021-9258(1996)271:9<4747:2AACAD>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED CA2+ RELEASE; INOSITOL TRISPHOSPHATE; ANTIGEN CD38; ENZYME; CELLS; PURIFICATION; HOMEOSTASIS; MICROSOMES; METABOLITE; HYDROLYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
C.Q. Vu et al., "2'-PHOSPHO-CYCLIC ADP-RIBOSE, A CALCIUM-MOBILIZING AGENT DERIVED FROMNADP", The Journal of biological chemistry, 271(9), 1996, pp. 4747-4754

Abstract

Cyclic adenosine diphosphoribose (cADPR), a metabolite of NAD, appears to modulate changes in intracellular free Ca2+ levels by activation of ryanodine-sensitive Ca2+ channels. We report here that an ADPR cyclase purified from Aplysia californica readily catalyzes the conversionof NADP to 2'-phospho-cyclic adenosine diphosphoribose (2'-P-cADPR), cyclized at N-1 of the adenine moiety. An enzyme from canine spleen previously shown to contain NAD glycohydrolase, ADPR cyclase, and cADPR hydrolase activities also utilized NADP and 2'-P-cADPR as substrates. The apparent K-m value for NADP was 1.6 mu M compared with 9.9 mu M for NAD, and the V-max with NADP was twice that with NAD, indicating that 2'-P-cADPR is a likely metabolite in mammalian cells. 2'-P-cADPR wasas active as cADPR in eliciting Ca2+ release from rat brain microsomes, but was unable to elicit Ca2+ release following conversion to 2'-P-ADPR by the action of canine spleen NAD glycohydrolase, 2'-P-cADPR and1-D-myo-inositol 1,4,5-trisphosphate (IP3) appear to act by distinct mechanisms as microsomes desensitized to IP3 still released Ca2+ in response to 2'-P-cADPR and vice versa. Also, inhibition of IP3-induced Ca2+ release by heparin had no effect on release by 2'-P-cADPR. Both 2'-P-cADPR and cADPR appear to act by a similar mechanism based on similar kinetics of Ca2+ release, similar dose-response curves, cross-desensitization, and partial inhibition of release by procaine. The resultsof this study suggest that 2'-P-cADPR may function as a new componentof Ca2+ signaling and a possible link between NADP metabolism and Ca2 homeostasis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 03:18:13