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Titolo:
ENZYME PROPERTIES OF APLYSIA ADP-RIBOSYL CYCLASE - COMPARISON WITH NAD GLYCOHYDROLASE OF CD38 ANTIGEN
Autore:
INAGEDA K; TAKAHASHI K; TOKITA K; NISHINA H; KANAHO Y; KUKIMOTO I; KONTANI K; HOSHINO S; KATADA T;
Indirizzi:
TOKYO INST TECHNOL,DEPT LIFE SCI,MIDORI KU YOKOHAMA KANAGAWA 227 JAPAN TOKYO INST TECHNOL,DEPT LIFE SCI,MIDORI KU YOKOHAMA KANAGAWA 227 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 1, volume: 117, anno: 1995,
pagine: 125 - 131
SICI:
0021-924X(1995)117:1<125:EPOAAC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
EGG-SPECIFIC NADASE; 2ND-MESSENGER ENZYME; CYCLIC METABOLITE; CALCIUM RELEASE; CELL ACTIVATION; MOLECULE; SURFACE; CA2+; MICROSOMES; HYDROLYSIS;
Keywords:
ADP-RIBOSYL CYCLASE; CD38 ANTIGEN; CYCLIC ADP-RIBOSE; NAD GLYCOHYDROLASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
K. Inageda et al., "ENZYME PROPERTIES OF APLYSIA ADP-RIBOSYL CYCLASE - COMPARISON WITH NAD GLYCOHYDROLASE OF CD38 ANTIGEN", Journal of Biochemistry, 117(1), 1995, pp. 125-131

Abstract

An ecto-enzyme of NAD glycohydrolase (NADase) induced by retinoic acid in HL-60 cells is attributed to the molecule of CD38 antigen [Kontani, K., Nishina, H., Ohoka, Y., Takahashi, K., and Katada, T. (1993) J. Biol. Chem. 268, 16895-16898]. CD38 antigen has an amino acid sequence homologous to Aplysia ADP-ribosyl cyclase which generates cyclic adenosine diphosphoribose (cADPR) and nicotinamide (NA) from beta-NAD(+). On the basis of this sequence homology, we compared enzyme propertiesbetween CD38 NADase expressed as a fusion protein in Escherichia coliand ADP-ribosyl cyclase purified from the ovotestis of Aplysia kurodai. 1) beta-NAD(+) analogs, nicotinamide 1, N-6-ethenoadenine dinucleotide, and nicotinamide hypoxanthine dinucleotide, did not serve as goodsubstrates for the ADP-ribosyl cyclase, suggesting that the intact adenine ring of beta-NAD(+) was required for the cyclase-catalyzed reaction. On the other hand, CD38 NADase utilized the NAD analogs to form ADP-ribose and NA. 2) Kinetic analyses of the ADP-ribosyl cyclase reaction revealed that NA was first released from the substrate (beta-NAD(+))-enzyme complex, followed by the release of another product, cADPR, which was capable of interacting with the free enzyme. 3) The enzyme reaction catalyzed by the ADP-ribosyl cyclase was fully reversible; beta-NAD(+) could be formed from cADPR and NA with a velocity similar to that observed in the degradation of beta-NAD(+). However, CD38 NADase did not catalyze the reverse reaction to form beta-NAD(+) from ADP-ribose and NA. 4) The CD38 NADase activity was, but the ADP-ribosyl cyclase activity was not, inhibited by dithiothreitol. These results indicated that enzyme reactions catalyzed by Aplysia ADP-ribosyl cyclase andCD38 NADase were quite different from each other in terms of their substrate specificities, reversible reactions, and susceptibilities to dithiothreitol, though both enzymes cleaved the N-glycoside bond of beta-NAD(+) resulting in the liberation of NA.

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Documento generato il 23/09/20 alle ore 05:50:41