Vitronectin, a 75 kDa polypeptide along with a 10 kDa fragment, is a glycoprotein present on most cell surfaces, in extracellular fluids and plasma (1). Vitronectin promotes cellular adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to several serpin serine protease inhibitors (2). As a member of the integrin family, Vitronectin contains the cell binding sequence arg gly asp (RGD), first found in fibronectin, and serves as a cell-to-substrate adhesion molecule (3). Vitronectin acts as an inhibitor of the complement cascade by binding to the C5b9 complex and it has also been shown to have has a novel and direct role in self-senescent-self intercellular recognition leading to macrophage phagocytosis of cells undergoing apoptosis (4).
Senescence and Autophagy
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