Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Identification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs
Autore:
Yu, ZB; Lai, CM; Maoui, M; Banville, D; Shen, SH;
Indirizzi:
Natl Res Council Canada, Biotechnol Res Inst, Pharmaceut Sector, Montreal,PQ H4P 2R2, Canada Natl Res Council Canada Montreal PQ Canada H4P 2R2 eal,PQ H4P 2R2, Canada Univ Montreal, Dept Pathol & Microbiol, St Hyacinthe, PQ J2S 7C6, Canada Univ Montreal St Hyacinthe PQ Canada J2S 7C6 yacinthe, PQ J2S 7C6, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 26, volume: 276, anno: 2001,
pagine: 23816 - 23824
SICI:
0021-9258(20010629)276:26<23816:IACOSA>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-BINDING-SITE; MYELIN-ASSOCIATED GLYCOPROTEIN; HEMATOPOIETIC-CELL PHOSPHATASE; NATURAL-KILLER-CELLS; IMMUNOGLOBULIN SUPERFAMILY; INHIBITORY RECEPTOR; SH2 DOMAIN; MOLECULAR-CLONING; SIALOADHESIN; CD33;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Shen, SH Natl Res Council Canada, Biotechnol Res Inst, Pharmaceut Sector, 6100 Royalmount Ave, Montreal, PQ H4P 2R2, Canada Natl Res Council Canada 6100 Royalmount Ave Montreal PQ Canada H4P 2R2
Citazione:
Z.B. Yu et al., "Identification and characterization of S2V, a novel putative siglec that contains two V set Ig-like domains and recruits protein-tyrosine phosphatases SHPs", J BIOL CHEM, 276(26), 2001, pp. 23816-23824

Abstract

We describe the molecular cloning and characterization of S2V, a novel sialic acid binding immunoglobulin-like lectin. The cDNA of S2V encodes a type1 transmembrane protein with four extracellular immunoglobulin-like (Pg-like) domains and a cytoplasmic tail bearing a typical immunoreceptor tyrosine-based inhibitory motif (ITIM) and an ITIM-like motif. A unique feature ofS2V is the presence of two V-set Ig-like domains responsible for the binding to sialic acid, whereas all other known siglecs possess only one. S2V ispredominantly expressed in macrophage. In vivo S2V was tyrosine-phosphorylated. when co-expressed with exogenous c-Src kinase. Upon tyrosine phosphorylation, S2V recruits both Src homology 2 (SK2) domain-containing protein-tyrosine phosphatases SHP-1 and SHP-2, two important inhibitory regulators of immunoreceptor signal transduction. These findings suggest that S2V is involved in the negative regulation of the signaling in macrophage by functioning as an inhibitory receptor. When expressed in COS-7 cells, S2V was ableto mediate sialic acid-dependent binding to human red blood cells, suggesting that S2V may function through cell-cell interaction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 20:57:41