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Titolo:
FUNCTIONAL-ANALYSIS OF CSK IN SIGNAL-TRANSDUCTION THROUGH THE B-CELL ANTIGEN RECEPTOR
Autore:
HATA A; SABE H; KUROSAKI T; TAKATA M; HANAFUSA H;
Indirizzi:
ROCKEFELLER UNIV,DEPT MOLEC ONCOL,MOLEC ONCOL LAB,1230 YORK AVE,BOX 169 NEW YORK NY 10021 ROCKEFELLER UNIV,DEPT MOLEC ONCOL,MOLEC ONCOL LAB NEW YORK NY 10021 AMER CYANAMID CO,LEDERLE LABS,DEPT CARDIOVASC MOLEC BIOL PEARL RIVER NY 10965 KYOTO UNIV,INST VIRUS RES,DEPT BIOL RESPONSES,SAKYO KU KYOTO 606 JAPAN
Titolo Testata:
Molecular and cellular biology
fascicolo: 11, volume: 14, anno: 1994,
pagine: 7306 - 7313
SICI:
0270-7306(1994)14:11<7306:FOCIST>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; SRC FAMILY KINASES; LYMPHOCYTES-B; C-SRC; MEMBRANE IMMUNOGLOBULIN; MOLECULAR-CLONING; PHOSPHOLIPASE-C; CROSS-LINKING; IG-ALPHA; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
A. Hata et al., "FUNCTIONAL-ANALYSIS OF CSK IN SIGNAL-TRANSDUCTION THROUGH THE B-CELL ANTIGEN RECEPTOR", Molecular and cellular biology, 14(11), 1994, pp. 7306-7313

Abstract

In B cells, two classes of protein tyrosine kinases (PTKs), the Src family of PTKs (Lyn, Fyn, Lck, and Blk) and non-Src family of PTKs (Syk), are known to be involved in signal transduction induced by the stimulation of the B-cell antigen receptor (BCR). Previous studies using Lyn-negative chicken B-cell clones revealed that Lyn is necessary for transduction of signals through the BCR The kinase activity of the Src family of PTKs is negatively regulated by phosphorylation at the C-terminal tyrosine residue, and the PTK Csk has been demonstrated to phosphorylate this C-terminal tyrosine residue of the Src family of PTKs. To investigate the role of Csk in BCR signaling, Csk-negative chicken B-cell clones were generated. In these Csk-negative cells, Lyn became constitutively active and highly phosphorylated at the autophosphorylation site, indicating that Csk is necessary to sustain Lyn in an inactive state. Since the C-terminal tyrosine phosphorylation of Lyn is barely detectable in the unstimulated, wild-type B cells, our data suggestthat the activities of Csk and a certain protein tyrosine phosphatase(s) are balanced to maintain Lyn at a hypophosphorylated and inactive state. Moreover, we show that the kinase activity of Syk was also constitutively activated in Csk-negative cells. The degree of activation of both the Lyn and Syk kinases in Csk-negative cells was comparable tothat observed in wild-type cells after BCR stimulation. However, BCR stimulation was still necessary in Csk-negative cells to elicit tyrosine phosphorylation of cellular proteins, as well as calcium mobilization and inositol 1,4,5-trisphosphate generation. These results suggest that not only activation of the Lyn and Syk kinases but also additional signals induced by the cross-linking of the BCR are required for full transduction of BCR signaling.

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Documento generato il 17/01/21 alle ore 18:21:46