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Titolo:
CD38 AND ADP-RIBOSYL CYCLASE CATALYZE THE SYNTHESIS OF A DIMERIC ADP-RIBOSE THAT POTENTIATES THE CALCIUM-MOBILIZING ACTIVITY OF CYCLIC ADP-RIBOSE
Autore:
DEFLORA A; GUIDA L; FRANCO L; ZOCCHI E; BRUZZONE S; BENATTI U; DAMONTE G; LEE HC;
Indirizzi:
UNIV GENOA,INST BIOCHEM,VIALE BENEDETTO XV-1 I-16132 GENOA ITALY UNIV MINNESOTA,DEPT PHYSIOL MINNEAPOLIS MN 55455
Titolo Testata:
The Journal of biological chemistry
fascicolo: 20, volume: 272, anno: 1997,
pagine: 12945 - 12951
SICI:
0021-9258(1997)272:20<12945:CAACCT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
NAD+-GLYCOHYDROLASE; HUMAN ERYTHROCYTES; SKELETAL-MUSCLE; ANTIGEN CD38; INOSITOL TRISPHOSPHATE; SELF-AGGREGATION; SURFACE; RIBOSYLTRANSFERASE; HYDROLYSIS; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
A. Deflora et al., "CD38 AND ADP-RIBOSYL CYCLASE CATALYZE THE SYNTHESIS OF A DIMERIC ADP-RIBOSE THAT POTENTIATES THE CALCIUM-MOBILIZING ACTIVITY OF CYCLIC ADP-RIBOSE", The Journal of biological chemistry, 272(20), 1997, pp. 12945-12951

Abstract

CD38, a lymphocyte differentiation antigen, is also a bifunctional enzyme catalyzing the synthesis of cyclic ADP-ribose (cADPR) from NAD(+)and its hydrolysis to ADP-ribose (ADPR), An additional enzymatic activity of CD38 shared by monofunctional ADP ribosyl cyclase from Aplysiacalifornica is the exchange of the base group of NAD(+) (nicotinamide) with various nucleophiles, Both human CD38 (either recombinant or purified from erythrocyte membranes) and Aplysia cyclase were found to catalyze the exchange of ADPR with the nicotinamide group of NAD(+) leading to the formation of a dimeric ADPR ((ADPR)(2)), The dimeric structure of the enzymatic product, which was generated by recombinant CD38and by CD38(+) Namalwa cells from as low as 10 mu M NAD(+), was demonstrated using specific enzyme treatments (dinucleotide pyrophosphataseand 5'-nucleotidase) and mass spectrometry analyses of the resulting products, The linkage between the two ADPR units of (ADPR)(2) was identified as that between the N-1 of the adenine nucleus of one ADPR unitand the anomeric carbon of the terminal ribose of the second ADPR molecule by enzymatic analyses and by comparison with patterns of cADPR cleavage with Me2SO:tert-butoxide. Although (ADPR)(2) itself did not release Ca2+ from sea urchin egg microsomal vesicles, it specifically potentiated the Ca2+-releasing activity of subthreshold concentrations of cADPR, Therefore, (ADPR)(2) is a new product of CD38 that amplifies the Ca2+-mobilizing activity of cADPR.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 19:47:13