A new chapter in cardiac PKC signaling studies: searching for isoform-specific molecular targets. Focus on: “Isoenzyme-selective regulation of SERCA2 gene expression by protein kinase C in neonatal rat ventricular myocytes”

Open Access
Publisher Website
Google Scholar
Abstract
Recently, with the establishment of PKC isozymes as essential molecules for the transduction of extracellular signals, increasing effort has been devoted to the downstream signaling events that these kinases orchestrate. A number of investigations have embarked on the search of cellular molecules that are targets of PKC activation (1–4, 7–9, 11–14, 16–22). Indeed, there are disparities with respect to the molecular makeup of the downstream realm of individual PKC isozymes, which may be due in part to differences in species, cell models, and experimental conditions. Not-withstanding these differences, most studies support the notion that each isoform governs a myriad of downstream signaling events and that activation of an individual isozyme can lead to distinct cardiac phenotypes. In particular, it appears that some of the downstream signaling elements are commonly shared by all isozymes, whereas others are uniquely modulated in an isozyme-specific fashion; nevertheless, all are essential to mediate the biological functions of PKC.