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Titolo:
Inhibition of natural killer cell activation signals by killer cell immunoglobulin-like receptors (CD158)
Autore:
Long, EO; Barber, DF; Burshtyn, DN; Faure, M; Peterson, M; Rajagopalan, S; Renard, V; Sandusky, M; Stebbins, CC; Wagtmann, N; Watzl, C;
Indirizzi:
NIAID, Immunogenet Lab, NIH, Rockville, MD 20852 USA NIAID Rockville MD USA 20852 mmunogenet Lab, NIH, Rockville, MD 20852 USA Univ Alberta, Dept Med Microbiol & Immunol, Heritage Med Res Ctr, Edmonton, AB T6G 2M7, Canada Univ Alberta Edmonton AB Canada T6G 2M7 Ctr, Edmonton, AB T6G 2M7, Canada M&E Biotech, Copenhagen, Denmark M&E Biotech Copenhagen DenmarkM&E Biotech, Copenhagen, Denmark Novo Nordisk AS, DK-2880 Bagsvaerd, Denmark Novo Nordisk AS Bagsvaerd Denmark DK-2880 AS, DK-2880 Bagsvaerd, Denmark
Titolo Testata:
IMMUNOLOGICAL REVIEWS
, volume: 181, anno: 2001,
pagine: 223 - 233
SICI:
0105-2896(200106)181:<223:IONKCA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLASS-I MOLECULES; LINKED LYMPHOPROLIFERATIVE DISEASE; TYROSINE-PHOSPHATASE SHP-1; COMPLEX CLASS-I; DOMAIN-CONTAINING PHOSPHATASE-1; HUMAN NK CELLS; HLA-C; KINASE ACTIVATION; CRYSTAL-STRUCTURE; CUTTING EDGE;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Long, EO NIAID, LIG, NIH, 12441 Parklawn Dr, Rockville, MD 20852 USA NIAID12441 Parklawn Dr Rockville MD USA 20852 ille, MD 20852 USA
Citazione:
E.O. Long et al., "Inhibition of natural killer cell activation signals by killer cell immunoglobulin-like receptors (CD158)", IMMUNOL REV, 181, 2001, pp. 223-233

Abstract

The killer cell immunoglobulin-like receptor (KIR) family includes receptors that bind to HLA class I molecules on target cells and inhibit natural killer (NK)-cell cytotoxicity, and receptors such as KIR3DL7 with no known ligand and function. Inhibitory KIR recruit the tyrosine phosphatase SHP-1 to block signals transduced by any one of a number of activation receptors. Inhibition of overall protein tyrosine phosphorylation by SHP-1 during binding of KIR to MHC class I on target cells is selective, suggesting that a limited number of substrates a-re dephosphorylated by SHP-1. We have chosen to study KIR inhibition as it occurs during binding of KIR to MHC class I on target cells, despite the technical limitations inherent to studies of processes regulated by cell contact. KIR binding to MHC class I on target cells inhibits tyrosine phosphorylation of the activation receptor 2B4 (CD244)and disrupts adhesion of NK cells to target cells. Inhibition of proximal events in NK activation may increase the availability of NK cells by liberating them from non-productive interactions with resistant target cells. As the receptors and the signaling pathways that induce NK cytotoxicity a-re not fully characterized, elucidation of the inhibitory mechanism employed byKIR may provide insight into NK activation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 14:49:30