inhibits antigen‐mediated Syk, but not Lyn tyrosine kinase activation in mast cells

FEBS Letters

Vallé, Alain¹  Kinet, Jean-Pierre¹ 

[1] Molecular Allergy and Immunology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Twinbrook II, 12441 Parklawn Drive, Rockville, MD 20852, USA

关键词: FcϵRI receptor;    tyrosine kinase;    DNP-HSA;    dinitrophenyl-[30]-human serum albumin;    FcϵRI;    high-affinity IgE receptor;    NAC;    PLC;    phospholipase C;   

DOI  :  10.1016/0014-5793(94)01329-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

High affinity IgE receptors (αβγ ₂) mediate the activation of the non-receptor tyrosine kinases Lyn and Syk. Here we show that the antioxidant drug (NAC) inhibits antigen-mediated Syk activation whereas Lyn activation and phosphorylation of β and γ is maintained. Furthermore, NAC inhibits antigen-mediated calcium mobilization and exocytosis in a dose-dependent manner, but does not inhibit ionomycin-induced exocytosis. These data support a model in which the activation of Lyn is responsible for receptor phosphorylation and precedes the activation of Syk. The inhibition of Syk activation by NAC may be relevant to B and T cell antigen receptors, which are also linked to Syk/ZAP70 tyrosine kinases.

【 授权许可】

Unknown