Lipopolysaccharide can trigger a cathepsin B-dependent programmed death response in human endothelial cells.

ABSTRACT: In this study, we examined the mechanisms that contribute to lipopolysaccharide (LPS)-induced death responses in cultured human umbilical vein endothelial cells (HUVECs). In the presence of the protein synthesis inhibitor cycloheximide, LPS primarily induces caspase-dependent apoptotic cell death of HUVECs, which is blocked by siRNA-mediated knockdown of myeloid differentiation factor 88 adaptor protein but not of Toll-like receptor-associated interferon-inducing factor. Knockdown of Fas-associated death domain protein (FADD) by either siRNA or overexpression of a truncated version of FADD that lacks the N-terminal death effector domain (FADD(DN)) increases the sensitivity of HUVECs to LPS plus cycloheximide-mediated death. However, based on the use of proteinase inhibitors, cell death cha

SUBMITTER: Li JH 

PROVIDER: S-EPMC2731131 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature