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Evidence for a novel function of the CD40 ligand as a signalling molecule in T‐lymphocytes
Author(s) -
Brenner Birgit,
Koppenhoefer Ursula,
Grassmé Heike,
Kun Jutta,
Lang Florian,
Gulbins Erich
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01306-9
Subject(s) - p38 mitogen activated protein kinases , kinase , phosphorylation , cd40 , microbiology and biotechnology , rac1 , chemistry , stimulation , proto oncogene tyrosine protein kinase src , ligand (biochemistry) , receptor tyrosine kinase , tyrosine phosphorylation , jurkat cells , tyrosine kinase , signal transduction , receptor , biology , t cell , protein kinase a , immune system , biochemistry , immunology , cytotoxic t cell , endocrinology , in vitro
The interaction of the CD40 receptor with its ligand has been shown to be crucial for the activation of B‐lymphocytes. Here, we provide evidence that the pg39 molecule/CD40 ligand (gp39/CD40L) also functions as a stimulatory molecule for T‐lymphocytes. Activation of T‐lymphocytes via gp39/CD40L induced a strong activation of Jun‐N‐terminal kinase (JNK) and p38‐K. Activation of these kinases correlates with a stimulation of Rac1 and inhibition of Rac1 prevents gp39/CD40L triggered JNK/p38‐K activation. Further, cellular stimulation via the CD40 ligand results in tyrosine phosphorylation of cellular proteins and the activation of p56 lck . Inhibition of src‐like kinases inhibits Rac1 as well as JNK/p38‐K stimulation suggesting a signalling cascade from the gp39/CD40L via p56 lck and Rac1 to JNK/p38‐K.