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Titolo:
CYCLIC ADP-RIBOSE METABOLISM IN RAT-KIDNEY - HIGH-CAPACITY FOR SYNTHESIS IN GLOMERULI
Autore:
CHINI EN; KLENER P; BEERS KW; CHINI CCS; GRANDE JP; DOUSA TP;
Indirizzi:
MAYO CLIN & MAYO GRAD SCH MED,DEPT PHYSIOL & BIOPHYS,RENAL PATHOPHYSIOL LAB,200 1ST ST SW ROCHESTER MN 55905 MAYO CLIN & MAYO GRAD SCH MED,DEPT PHYSIOL & BIOPHYS,RENAL PATHOPHYSIOL LAB ROCHESTER MN 55905 MAYO CLIN & MAYO GRAD SCH MED,DEPT LAB MED ROCHESTER MN 55905
Titolo Testata:
Kidney international
fascicolo: 5, volume: 51, anno: 1997,
pagine: 1500 - 1506
SICI:
0085-2538(1997)51:5<1500:CAMIR->2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DINUCLEOTIDE PHOSPHATE NAADP; EGG-SPECIFIC NADASE; ADENINE-DINUCLEOTIDE; CALCIUM-RELEASE; 2ND-MESSENGER ENZYME; CA2+ RELEASE; TRANSPORT; CELLS; NICOTINAMIDE; HYDROLASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
E.N. Chini et al., "CYCLIC ADP-RIBOSE METABOLISM IN RAT-KIDNEY - HIGH-CAPACITY FOR SYNTHESIS IN GLOMERULI", Kidney international, 51(5), 1997, pp. 1500-1506

Abstract

Recent discovery of cyclic ADP-ribose (cADPR) as an agent that triggers Ca2+ release from intracellular stores, through ryanodine receptor channel, is an important new development in the investigation of intracellular signaling mechanisms. We determined the capacity of kidney and its components for synthesis of cADPR from beta-NAD, that is catalyzed by enzyme ADP-ribosyl cyclase, and enzymatic inactivation that is catalyzed by cADPR-glycohydrolase. Little or no activity of ADP-ribosylcyclase was found in extracts from the whole rat kidney, renal cortex, outer and inner medulla. On the other hand. incubation of beta-NAD with similar extracts from rat liver, spleen, heart, and brain resultedin biosynthesis of cADPR. In addition. extracts from suspension of proximal tubules or microdissected proximal convoluted tubules virtuallylacked ADP-ribosyl cyclase activity. In sharp contrast to proximal tubules and cortex, extracts from glomeruli had high ADP-ribosyl cyclaseactivity, similar to that found in non-renal tissues. Authenticity ofcADPR biosynthesized in glomeruli was documented by several criteria such as HPLC analysis, effect of inhibitors and homologous desensitization of Ca2+-release bioassay. On the other hand, the activity of cADPR-glycohydrolase was similar in extracts from glomeruli and in extracts from kidney cortex. Mesangial cells and vascular smooth muscle cellsgrown in primary culture displayed considerable ADPR-ribose cyclase activity. Our results show that extracts from glomeruli, unlike extracts from renal tissue zones and proximal tubules, have a singularly highcapacity for synthesis of cADPR. We surmise that cADPR-triggered Ca2+-releasing system can serve as an intracellular signaling pathway thatmay be operant in regulations of glomerular cell functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 14:06:27