Enhanced Expression of Fas Ligand Is Associated with Aburatubolactam C-Induced Apoptosis in Human Jurkat T Cells

Author： Bae M.A. Kang H.S. Rue S.W. Seu J.H. Kim Y.H.

Publisher： Elsevier

ISSN： 0006-291X

Source： Biochemical and Biophysical Research Communications, Vol.246, Iss.1, 1998-05, pp. : 276-281

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

The mechanism for apoptosis induced by aburatubolactam C was investigated in human Jurkat T cells. When the cells were treated with 3 mug/ml of aburatubolactam C, apoptotic DNA fragmentation was first detectable in 3 hr and then increased time-dependently in accordance with upregulation in the protein level of Fas ligand (FasL). Both the DNA fragmentation and upregulation of FasL expression reached a maximal level in 7-8 hr, at which time a significant increase in the tyrosine phosphorylation of multiple cellular proteins was detected, suggesting that the enhanced tyrosine phosphorylation of cellular proteins may result from activation of Fas-mediated death signaling. However, these aburatubolactam C-induced cellular changes and accompanied apoptosis were completely blocked in the presence of genistein, a known protein tyrosine kinase inhibitor. These results indicate that upregulation of FasL expression dictated by protein tyrosine kinase activation and subsequent mediation of Fas death signaling account for aburatubolactam C-induced apoptosis in Jurkat T cells. Copyright 1998 Academic Press.