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Titolo:
The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38
Autore:
Ferrero, E; Malavasi, F;
Indirizzi:
Univ Turin, Dept Genet Biol & Biochem, I-10126 Turin, Italy Univ Turin Turin Italy I-10126 enet Biol & Biochem, I-10126 Turin, Italy Univ Ancona, Sch Med, Inst Biol & Genet, Ancona, Italy Univ Ancona Ancona Italy ona, Sch Med, Inst Biol & Genet, Ancona, Italy
Titolo Testata:
JOURNAL OF LEUKOCYTE BIOLOGY
fascicolo: 2, volume: 65, anno: 1999,
pagine: 151 - 161
SICI:
0741-5400(199902)65:2<151:TMOAMF>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADP-RIBOSYL CYCLASE; CELL-SURFACE ANTIGEN; EGG-SPECIFIC NADASE; 2ND-MESSENGER ENZYME; T-LYMPHOCYTES; EXPRESSION; ACTIVATION; PROTEIN; LIGATION; GLYCOHYDROLASE;
Keywords:
leukocyte antigen; ectoenzyme; molecular biology; evolution;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Ferrero, E Univ Turin, Dept Genet Biol & Biochem, Via Santena 19, I-10126 Turin, Italy Univ Turin Via Santena 19 Turin Italy I-10126 126 Turin, Italy
Citazione:
E. Ferrero e F. Malavasi, "The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38", J LEUK BIOL, 65(2), 1999, pp. 151-161

Abstract

Human CD38 is a 45-kDa type II membrane glycoprotein with an intricate pattern of expression in leukocytes, although evidence is ac cumulating of itsquite widespread expression in cells of nonvascular origin. CD38 is a member of a nascent eukaryotic gene family encoding cytosolic and membrane-bound enzymes whose substrate is NAD, a coenzyme ubiquitously distributed in nature, Functionally, CD38 is an eclectic molecule with the ability not only to catalyze but also to signal, to mobilize calcium, and to adhere to itself, to hyaluronan, and to other Ligands. Interaction with CD38 on various leukocyte subpopulations has profound though diverse consequences on their life-span, but these effects seem to be independent of the enzymatic activityof the molecule. CD38 challenges our expectations of a surface molecule and we must sift through its many guises to unmask its true nature.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 14:12:54