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Titolo:
Signaling through CD38 induces NK cell activation
Autore:
Mallone, R; Funaro, A; Zubiaur, M; Baj, G; Ausiello, CM; Tacchetti, C; Sancho, J; Grossi, C; Malavasi, F;
Indirizzi:
Univ Turin, Immunogenet Lab, Dipartimento Genet Biol & Biochim, I-10126 Turin, Italy Univ Turin Turin Italy I-10126 enet Biol & Biochim, I-10126 Turin, Italy CSIC, Dept Cellular Biol & immunol, Inst Parasitol & Biomed, Granada 18071, Spain CSIC Granada Spain 18071 , Inst Parasitol & Biomed, Granada 18071, Spain Natl Inst Hlth ISS, I-00161 Rome, Italy Natl Inst Hlth ISS Rome Italy I-00161 Inst Hlth ISS, I-00161 Rome, Italy Univ Genoa, Dept Expt Med, Sect Human Anat, I-16100 Genoa, Italy Univ Genoa Genoa Italy I-16100 ed, Sect Human Anat, I-16100 Genoa, Italy
Titolo Testata:
INTERNATIONAL IMMUNOLOGY
fascicolo: 4, volume: 13, anno: 2001,
pagine: 397 - 409
SICI:
0953-8178(200104)13:4<397:STCINC>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
NATURAL-KILLER-CELLS; 70-KDA TYROSINE PHOSPHOPROTEIN; FLOW CYTOMETRIC MEASUREMENT; ADP-RIBOSYL CYCLASE; C-CBL PROTOONCOGENE; HUMAN T-CELLS; PHOSPHATIDYLINOSITOL 3-KINASE; MONOCLONAL-ANTIBODY; LYMPHOKINE GENES; PROTEIN-KINASE;
Keywords:
calcium; CD16; ectoenzymes; surface receptors; tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Malavasi, F Univ Turin, Immunogenet Lab, Dipartimento Genet Biol & Biochim, Via Santena 19, I-10126 Turin, Italy Univ Turin Via Santena 19 Turin Italy I-10126 26 Turin, Italy
Citazione:
R. Mallone et al., "Signaling through CD38 induces NK cell activation", INT IMMUNOL, 13(4), 2001, pp. 397-409

Abstract

Human CD38 is a signal transduction molecule, and, concurrently, an ectoenzyme catalyzing the synthesis and degradation of cyclic ADP-ribose (cADPR),a potent Ca2+ mobilizer, One facet of CD38 that has not yet been addressedis its role in NK cells. To this end, the events triggered by CD38 ligation with agonistic mAb were analyzed on freshly purified human NK cells. Ligation was followed by (i) a significant rise in the intracellular level of Ca2+, (ii) increased expression of HLA class II and CD25, and (iii) tyrosinephosphorylation of discrete cytoplasmic substrates, The phosphorylation cascade involved CDS-S and Fc epsilon Rl gamma chains, zeta -associated protein (ZAP)-70 and the proto-oncogene product c-Cbl, NK effector functions were then analyzed: CD38 signaling was able (iv) to induce release of IFN-gamma and, more prominently, of granulocyte macrophage colony stimulating factor, as assessed by measuring both mRNA and protein products; and, lastly, (v) to induce cytolytic effector functions on target cells after IL-2 activation, as shown both by cytotoxicity assays and ultrastructural changes. The tyrosine-phosphorylated substrates and all the effects mediated by CD38 were similar to those observed following triggering via CD16 (Fc gamma RIIIA);moreover, Ca2+ mobilization via CD38 no longer operated in NK-derived celllines lacking CD16. These results suggest that the activation signals transduced by CD38 in NK cells elicit relevant cellular events. The effects aresimilar to those elicited via CD16 and possibly rely on common signaling pathways.

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Documento generato il 30/05/20 alle ore 14:50:05