Diversity of the protein kinase C gene family Implications for cardiovascular disease

Abstract

All eukaryotic cells are capable of responding to a changing intracellular environment and to extracellular stimuli. These functional responses are highly regulated by diverse means; one of the most common mechanisms of regulation requires the covalent phosphorylation of intracellular proteins, which when phosphorylated, mediate many functional events. The general class of enzymes that catalyzes the phosphorylation of effectors (substrates), the protein kinases, may be divided into two broad categories, depending on whether they phosphorylate serine and threonine residues or tyrosine residues. Evidence has accumulated that implicates abnormal activation of protein kinase C (PKC), which is one family of serine-threonine protein kinases, in cells and tissues from patients or models of cardiovascular disease. In this review, we present the molecular and biochemical basis for the diversity of the PKC family, and briefly summarize the evidence that PKC is implicated in cardiovascular pathology and the potential therapeutic implications and approaches.