3'Phosphoinositide-dependent kinase-1 is essential for ischemic preconditioning of the myocardium.

Brief periods of ischemia and reperfusion that precede sustained ischemia lead to a reduction in myocardial infarct size. This phenomenon, known as ischemic preconditioning, is mediated by signaling pathway(s) that are yet to be fully defined. 3'-Phosphoinositide-dependent kinase-1 (PDK1) has been implicated in numerous cellular processes.

AMP-activated protein kinase mediates preconditioning in cardiomyocytes by regulating activity and trafficking of sarcolemmal ATP-sensitive K(+) channels.

Brief periods of ischemia and reperfusion that precede sustained ischemia lead to a reduction in myocardial infarct size. This phenomenon, known as ischemic preconditioning, is mediated by signaling pathway(s) that is complex and yet to be fully defined. AMP-activated kinase (AMPK) is activated in cells under conditions associated with ATP depletion and increased AMP/ATP ratio.

Overexpression of SUR2A generates a cardiac phenotype resistant to ischemia.

ATP-sensitive K+ (K(ATP)) channels are present in the sarcolemma of cardiac myocytes where they link membrane excitability with the cellular bioenergetic state. These channels are in vivo composed of Kir6.2, a pore-forming subunit, SUR2A, a regulatory subunit, and at least four accessory proteins.

Preparation of intact microsomes from cultured mammalian H4IIE cells.

Introduction: Mammalian cell culture is widely used for the cloning and expression of insoluble proteins. The established methods of sub-cellular fractionation of tissues are not always directly suitable for the sub-cellular fractionation of cultured cells. In this study we have optimized the conditions for the preparation of microsomal fractions from cultured cells with the aim of isolating intact vesicles that are suitable for the assay of transport proteins and lumenal enzymes.

Immunodetection of the expression of microsomal proteins encoded by the glucose 6-phosphate transporter gene.

Glucose 6-phosphate transport has been well characterized in liver microsomes. The transport is required for the functioning of the glucose-6-phosphatase enzyme that is situated in the lumen of the hepatic endoplasmic reticulum. The genetic deficiency of the glucose 6-phosphate transport activity causes a severe metabolic disease termed type 1b glycogen storage disease.

Histone 2A stimulates glucose-6-phosphatase activity by permeabilization of liver microsomes.

Histone 2A increases glucose-6-phosphatase activity in liver microsomes. The effect has been attributed either to the conformational change of the enzyme, or to the permeabilization of microsomal membrane that allows the free access of substrate to the intraluminal glucose-6-phosphatase catalytic site. The aim of the present study was the critical reinvestigation of the mechanism of action of histone 2A.