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Titolo:
TYROSINE KINASES LYN AND SYK REGULATE B-CELL RECEPTOR-COUPLED CA2+ MOBILIZATION THROUGH DISTINCT PATHWAYS
Autore:
TAKATA M; SABE H; HATA A; INAZU T; HOMMA Y; NUKADA T; YAMAMURA H; KUROSAKI T;
Indirizzi:
AMER CYANAMID CO,LEDERLE LABS,DEPT CARDIOVASC MOLEC BIOL PEARL RIVER NY 10965 AMER CYANAMID CO,LEDERLE LABS,DEPT CARDIOVASC MOLEC BIOL PEARL RIVER NY 10965 ROCKEFELLER UNIV,MOLEC BIOL LAB NEW YORK NY 10021 FUKUI MED SCH,DEPT BIOCHEM FUKUI 91011 JAPAN TOKYO METROPOLITAN GERIATR HOSP & INST GERONTOL TOKYO 173 JAPAN TOKYO METROPOLITAN GERIATR HOSP & INST GERONTOL,DEPT BIOSIGNAL RES,ITABASHI KU TOKYO 173 JAPAN TOKYO INST PSYCHIAT,DEPT NEUROCHEM,SETAGAYA KU TOKYO 156 JAPAN
Titolo Testata:
EMBO journal
fascicolo: 6, volume: 13, anno: 1994,
pagine: 1341 - 1349
SICI:
0261-4189(1994)13:6<1341:TKLASR>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
MURINE LYMPHOCYTES-B; T-CELL; ANTIGEN RECEPTOR; SIGNAL TRANSDUCTION; PHOSPHOLIPASE-C; ZETA-CHAIN; MEMBRANE IMMUNOGLOBULIN; MUSCARINIC RECEPTOR; INOSITOL PHOSPHATES; SELECTION MARKERS;
Keywords:
B-CELL RECEPTOR; CA2+ MOBILIZATION; LYN; PHOSPHATIDYLINOSITOL TURNOVER; SYK;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
77
Recensione:
Indirizzi per estratti:
Citazione:
M. Takata et al., "TYROSINE KINASES LYN AND SYK REGULATE B-CELL RECEPTOR-COUPLED CA2+ MOBILIZATION THROUGH DISTINCT PATHWAYS", EMBO journal, 13(6), 1994, pp. 1341-1349

Abstract

Stimulation of B lymphocytes through their antigen receptor (BCR) results in rapid increases in tyrosine phosphorylation on a number of proteins and induces both an increase of phosphatidylinositol and mobilization of cytoplasmic free calcium. The BCR associates with two classesof tyrosine kinase: Src-family kinase (Lyn, Fyn, Blk or Lck) and Syk kinase. To dissect the functional roles of these two types of kinase in BCR signaling, lyn-negative and syk-negative B cell lines were established. Syk-deficient B cells abolished the tyrosine phosphorylation of phospholipase C-gamma2, resulting in the loss of both inositol 1,4,5-trisphosphate (IP3) generation and calcium mobilization upon receptorstimulation. Crosslinking of BCR on Lyn-deficient cells evoked a delayed and slow Ca2+ mobilization, despite the normal kinetics of IP3 turnover. These results demonstrate that Syk mediates IP3 generation, whereas Lyn regulates Ca2+ mobilization through a process independent of IP3 generation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 17:41:51