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Titolo:
EXTRACELLULAR SYNTHESIS OF CADP-RIBOSE FROM NICOTINAMIDE-ADENINE DINUCLEOTIDE BY RAT CORTICAL ASTROCYTES IN CULTURE
Autore:
PAWLIKOWSKA L; COTTRELL SE; HARMS MB; LI Y; ROSENBERG PA;
Indirizzi:
CHILDRENS HOSP,DEPT NEUROL,300 LONGWOOD AVE,ENDERS RES BLDG BOSTON MA02115 CHILDRENS HOSP,DEPT NEUROL BOSTON MA 02115 CHILDRENS HOSP,PROGRAM NEUROSCI BOSTON MA 02115
Titolo Testata:
The Journal of neuroscience
fascicolo: 17, volume: 16, anno: 1996,
pagine: 5372 - 5381
SICI:
0270-6474(1996)16:17<5372:ESOCFN>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC ADP-RIBOSE; CALCIUM-MOBILIZING METABOLITE; LYMPHOCYTE ANTIGEN CD38; CA2+ RELEASE; INOSITOL TRISPHOSPHATE; NAD GLYCOHYDROLASES; RYANODINE RECEPTOR; CEREBRAL-CORTEX; CELL-CULTURE; CYCLASE;
Keywords:
CADP-RIBOSE; NAD; ADP-RIBOSYL CYCLASE; CADPR HYDROLASE; ASTROCYTES; EXTRACELLULAR ENZYMES; SIGNAL TRANSDUCTION; CALCIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
L. Pawlikowska et al., "EXTRACELLULAR SYNTHESIS OF CADP-RIBOSE FROM NICOTINAMIDE-ADENINE DINUCLEOTIDE BY RAT CORTICAL ASTROCYTES IN CULTURE", The Journal of neuroscience, 16(17), 1996, pp. 5372-5381

Abstract

cADPR is an endogenous calcium-mobilizing agent that in vertebrates is synthesized from nicotinamide-adenine dinucleotide (NAD) by bifunctional enzymes with ADP-ribosyl cyclase and cADPR hydrolase activity. ADP-ribosyl cyclase and cADPR hydrolase activity have been reported in the brain, but the cellular localization of these activities has not been determined previously. in the present study, selective culturing techniques were employed to localize ADP-ribosyl cyclase activity and cADPR hydrolase activity to astrocytes or neurons in cultures derived from rat embryonic cerebral cortex. ADP-ribosyl cyclase activity was determined by incubating cultures with 1 mM NAD in the extracellular medium for 60 min at 37 degrees C and measuring formation of cADPR by bioassay and by HPLC. Astrocyte cultures and mixed cultures of astrocytes and neurons had mean specific activities of 0.84+/-0.06 and 0.9+/-0.18nmol cADPR produced/mg protein/hr, respectively. No detectable ADP-ribosyl cyclase activity was found in neuron-enriched/astrocyte-poor cultures. cADPR hydrolase activity was detectable by incubating cultures with 300 mu M cADPR for 60 min at 37 degrees C and assaying loss of cADPR or accumulation of ADPR. The demonstration of extracellular ADP-ribosyl cyclase and cADPR hydrolase activities associated with astrocytes may have important implications for the role of extracellular cADPR in signal transduction and in intercellular communication in the nervous system.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:06:42