Objective: To study the intracellular signaling events associated with ligation of the surface receptor CD95 VSports手机版. .

Methods: A mutant clone of Jurkat T cells, DD3, which fails to transmit apoptotic signals through CD95, was selected for study. Surface expression of CD95 and the primary nucleotide sequence of CD95, as well as the functional effects of a mutant CD95 molecule found in DD3, were examined V体育安卓版. .

Results: DD3, while exhibiting impaired ability to undergo apoptosis after CD95 ligation, retained the ability to die after ultraviolet light stimulation. A CD95 complementary DNA (cDNA) cloned from DD3 encoded a mutant transmembrane protein lacking the carboxy-terminal "death domain. " Western blotting confirmed the presence of both wild-type and mutant CD95 protein in DD3 V体育ios版. Transfection of the mutant CD95 cDNA into parental Jurkat cells conferred protection from CD95-mediated apoptosis. .

Conclusion: A mutant CD95 receptor lacking the cytoplasmic "death domain" can interfere with wild-type receptor function in T cells. VSports最新版本.