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A regulation of the level of phosphorylated phospholamban by inhibitor-1 in rat heart preparations in vitro.

Abstract：

:Inhibitor-1 following phosphorylation by protein kinase A inhibits phosphoprotein phosphatase-1. We have found that in the rat heart inhibitor-1 is present only in the cytosolic fraction and that its phosphorylation in ventricular slices was increased by isoproterenol but not by isoproterenol and propranolol together. Cardiac microsomal phosphoprotein phosphatase activity, with added phosphorylase a as the substrate, was inhibited 33% by phosphorylated inhibitor-1. Phosphorylated inhibitor-1 decreased the dephosphorylation by exogenous phosphoprotein phosphatase-1 of phospholamban present in the sarcoplasmic reticulum membranes. These results suggest an interaction of cytoplasmic inhibitor-1 with either cytoplasmic or membrane-bound phosphoprotein phosphatase-1 with a subsequent effect on the level of phosphorylated phospholamban and the probable involvement of this interaction in the cardiac response to beta-adrenergic hormones.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

Iyer RB,Koritz SB,Kirchberger MA

doi

10.1016/0303-7207(88)90084-6

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

1-6

issue

1

eissn

0303-7207

issn

1872-8057

journal_volume

55

pub_type

杂志文章

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