Conduct unbecoming: C-reactive protein interactions with a broad range of protein molecules.

Background: C-reactive protein (CRP), a pentamer composed of five identical 23-kd subunits, is a member of a highly conserved family of proteins known as pentraxins. CRP has been recognized as a risk factor for the development of both the native and transplant-associated forms of atherosclerosis. Understanding the biology of CRP may be relevant to understanding atherosclerosis development and progression.

SU1498, an inhibitor of vascular endothelial growth factor receptor 2, causes accumulation of phosphorylated ERK kinases and inhibits their activity in vivo and in vitro.

SU1498, an inhibitor of vascular endothelial growth factor receptor 2, has been used successfully to study the physiological manifestations of receptor functions. Here we report that in addition to its anti-receptor activity, SU1498 stimulates accumulation of phosphorylated ERKs in human umbilical vein endothelial cells and in human aortic endothelial cells in a manner that is dependent on the functioning of the upstream components of the MAPK pathway, B-Raf, and MEK kinases. The enhanced accumulation of phospho-ERKs is observed only in cells that have been stimulated with sphingosine 1-phosphate or protein growth factors; SU1498 by itself is ineffective.