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Titolo:
THE CD38 CYCLIC ADP-RIBOSE SYSTEM - A TOPOLOGICAL PARADOX/
Autore:
DEFLORA A; GUIDA L; FRANCO L; ZOCCHI E;
Indirizzi:
UNIV GENOA,INST BIOCHEM,VIALE BENEDETTO XV 1 I-16132 GENOA ITALY
Titolo Testata:
International journal of biochemistry & cell biology
fascicolo: 10, volume: 29, anno: 1997,
pagine: 1149 - 1166
SICI:
1357-2725(1997)29:10<1149:TCCAS->2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE-ANTIGEN CD38; NICOTINAMIDE-ADENINE-DINUCLEOTIDE; CALCIUM-MOBILIZING METABOLITE; PANCREATIC BETA-CELLS; TRANSMEMBRANE GLYCOPROTEIN CD38; INTRACELLULAR CA2+ MOBILIZATION; LEUKEMIC HL-60 CELLS; C-CBL PROTOONCOGENE; SEA-URCHIN EGGS; HUMAN ERYTHROCYTES;
Keywords:
CD38; CYCLIC ADP-RIBOSE; ECTOENZYMES; SIGNAL TRANSDUCTION; INTRACELLULAR CALCIUM HOMEOSTASIS;
Tipo documento:
Review
Natura:
Periodico
Citazioni:
108
Recensione:
Indirizzi per estratti:
Citazione:
A. Deflora et al., "THE CD38 CYCLIC ADP-RIBOSE SYSTEM - A TOPOLOGICAL PARADOX/", International journal of biochemistry & cell biology, 29(10), 1997, pp. 1149-1166

Abstract

CD38 was first identified as a lymphocyte differentiation antigen that showed typical properties of an orphan receptor involved in many programs of cell proliferation and activation. However, CD38 proved also to be a bifunctional ectoenzyme that catalyzes the transient formationof cyclic ADP-ribose (cADPR) in a variety of cell types. This property raises many intriguing and so far unanswered questions, since cADPR is a new second messenger molecule directly involved in the control ofcalcium homeostasis by means of receptor-mediated release of calcium from ryanodine-sensitive intracellular stores, The relationship between receptor-like and enzymatic properties of CD38 is still unknown. Theapparent topological paradox of ectocellular synthesis and intracellular activity of cADPR might be explained by: (a) influx of cADPR across the plasma membrane to reach its target stores, as suggested by experiments on cerebellar granule cells; and (b) NAD(+)-induced internalization, following membrane oligomerization, of CD38 with consequent partial import of cADPR metabolism to an intracellular compartment, as recently observed in lymphoid B cells. These two distinct mechanisms andother potential ones (e.g. binding of ectocellularly formed cADPR to cell surface receptors and initiation of signal-transducing pathways across the plasmamembrane) seem to be paradigmatic of processes affecting different types of cells. Although in some biological systems, suchas Aplysia and sea urchin egg, cADPR metabolism is restricted to the intracellular environment, in mammalian cells the CD38/cADPR system provides new challenges in terms of subcellular compartmentation and qualifies as an unusual example of ''ectobiochemistry'' with potential, still unrecognized, properties of cellular regulation. (C) 1997 Elsevier Science Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:25:07