20 research outputs found
Expression of uPAR in tumor-associated stromal cells is associated with colorectal cancer patient prognosis: a TMA study
Wild birds as pets in Campina Grande, Paraíba State, Brazil: An Ethnozoological Approach
Genetic variants in cellular transport do not affect mesalamine response in ulcerative colitis
Hyalinization and Molecular Pathways Involved in Orthodontic Tooth Movement: A Systematic Review and Meta-Analysis
Src kinase phosphorylates Caspase-8 on Tyr380: a novel mechanism of apoptosis suppression
We identified Caspase-8 as a new substrate for Src kinase. Phosphorylation occurs on Tyr380, situated in the linker region between the large and the small subunits of human Procaspase-8, and results in downregulation of Caspase-8 proapoptotic function. Src activation triggers Caspase-8 phosphorylation on Tyr380 and impairs Fas-induced apoptosis. Accordingly, Src failed to protect Caspase-8-defective human cells in which a Caspase-8-Y380F mutant is expressed from Fas-induced cell death. Remarkably, Src activation upon EGF-receptor stimulation triggers endogenous Caspase-8 phosphorylation and prevents Fas-induced apoptosis. Tyr380 is phosphorylated also in human colon cancers where Src is aberrantly activated. These data provide the first evidence for a direct role of tyrosine phosphorylation in the control of caspases and reveal a new mechanism through which tyrosine kinases inhibit apoptosis and participate in tumor progression