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Titolo:
ADP RIBOSYL CYCLASE ACTIVITY IN RAT PAROTID ACINAR-CELLS
Autore:
LOOMS D; NAUNTOFTE B; DISSING S;
Indirizzi:
UNIV COPENHAGEN,PANUM INST,DEPT MED PHYSIOL,BLEGDAMSVEJ 3 DK-2200 COPENHAGEN N DENMARK UNIV COPENHAGEN,PANUM INST,DEPT MED PHYSIOL DK-2200 COPENHAGEN N DENMARK UNIV COPENHAGEN,PANUM INST,DEPT ORAL FUNCT & PHYSIOL DK-2200 COPENHAGEN N DENMARK
Titolo Testata:
European journal of morphology
, volume: 36, anno: 1998, supplemento:, S
pagine: 181 - 185
SICI:
0924-3860(1998)36:<181:ARCAIR>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE ANTIGEN CD38; NAD(+) GLYCOHYDROLASE; CALCIUM; STIMULATION; INHIBITION; CATALYZES; RELEASE;
Keywords:
ADP RIBOSYL CYCLASE; CYCLIC ADP-RIBOSE; INTRACELLULAR CALCIUM; PAROTID ACINAR CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
D. Looms et al., "ADP RIBOSYL CYCLASE ACTIVITY IN RAT PAROTID ACINAR-CELLS", European journal of morphology, 36, 1998, pp. 181-185

Abstract

Cyclic ADP-ribose is an intracellular compound responsible for Ca2+ release in a wide variety of cell types. It may be implicated in releasing Ca2+ from ryanodine-sensitive pools in exocrine acinar cells. A bifunctional enzyme CD38 can synthesize cADP-ribose and we have characterized its properties by applying a technique in which nicotinamide guanine dinucleotide (NGD(+)) is used as a substrate for the synthesis offluorescent cyclic GDP-ribose. This reaction mimics the physiologically relevant reaction in which nicotinamide adenine dinucleotide (NAD(+)) is converted into non-fluorescent cyclic ADP-ribose. Using NGD+ as a substrate, the reaction shows a half maximal rate of synthesis at 2.6 mu M and is competitively inhibited by NAD(+) with a k(i) of 12.6 muM. This reveals that both NGD(+) and NAD(+) are converted by CD38 to their cyclic nucleotides. We have used this fluorescence technique to characterize the extent to which parotid acinar cells contain enzymes capable of synthesizing this class of cyclic nucleotides. We found that after treatment of acinar cells with a detergent which releases intracellular enzymes, NGD(+) is converted into its fluorescent derivativewith a half maximal rate of synthesis at 16 mu M. This reaction is also competitively inhibited by NAD(+) with a k(i) of 10 mu M. The data indicate that parotid acinar cells contain an enzyme capable of synthesizing the Ca2+ releasing compound, cyclic ADP-ribose. This finding suggests that cyclic ADP-ribose could play a role in Ca2+ release processes from internal stores - an important event in stimulus-secretion coupling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:32:41