Protein kinase C, an enzyme that is activated by the receptor-mediated hydrolysis of inositol phospholipids, relays information in the form of a variety of extracellular signals across the membrane to regulate many Ca2+-dependent processes. At an early phase of cellular responses, the enzyme appears to have a dual effect, providing positive forward as well as negative feedback controls over various steps of its own and other signaling pathways, such as the receptors that are coupled to inositol phospholipid hydrolysis and those of some growth factors. In biological systems, a positive signal is frequently followed by immediate negative feedback regulation. Such a novel role of this protein kinase system seems to give a logical basis for clarifying the biochemical mechanism of signal transduction, and to add a new dimension essential to our understanding of cell-to-cell communication.

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Studies and perspectives of protein kinase C

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Estimation of the molecular weights of proteins by Sephadex gel-filtration.

Protein phosphorylation and regulation of adaptive responses in bacteria.

A theory of gel filtration and its exeperimental verification

Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases.

The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.

Phosphorylation of purified rat liver pyruvate kinase by cyclic 3′,5′-AMP-stimulated protein kinase

Publisher Summary This chapter discusses the regulation of liver pyruvate kinase by phosphorylation–dephosphorylation. The rate and extent of the phosphorylation of L-type liver pyruvate kinase in vitro indicate that it is a specific reaction. This is supported by inhibition of the enzyme by the phosphorylation, which may be expected with regard to the known effect of cAMP on liver gluconeogenesis. The specificity of the phosphorylation reaction is also demonstrated by the fact that neither the A-type enzyme from pig kidney nor the M-type muscle enzyme from the rabbit or pig are substrates of cAMP-stimulated protein kinase. However, phosphorylation of the type-A enzyme from chicken liver has been preliminarily reported. The phosphorylation of liver pyruvate kinase in vitro is reversible, owing to the presence in rat liver cell sap of phosphoprotein phosphatase, which acts on phosphorylated pyruvate kinase. In vitro experiments strongly indicate that L-type liver pyruvate kinase is an enzyme whose activity is regulated by reversible protein phosphorylation in vivo .

The regulation of liver pyruvate kinase by phosphorylation--dephosphorylation.

Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme.

Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase.

Lorentz Engström

Papers

The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.

Phosphorylation of purified rat liver pyruvate kinase by cyclic 3′,5′-AMP-stimulated protein kinase

The regulation of liver pyruvate kinase by phosphorylation--dephosphorylation.

Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme.

Regulation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic-AMP dependent protein kinases and a histone phosphatase.