Literature DB >> 2844178

Stimulation by inositol trisphosphate and tetrakisphosphate of a protein phosphatase.

J Zwiller1, E M Ogasawara, S S Nakamoto, A L Boynton.   

Abstract

Several inositol trisphosphate isomers and inositol tetrakisphosphate activate a rat brain phosphoprotein phosphatase, using phosphohistone as well as phosphorylase kinase as substrate. Inositol mono- and bisphosphate have no effect. The protein phosphatase may correspond to type-1 since it is associated with the particulate fraction and is inhibited by heparin. Evidence is presented for the target of inositol phosphate being the catalytic subunit of the protein phosphatase. A parallelism is observed between the ability of the several inositol trisphosphates to activate the protein phosphatase and reported data indicating their ability to release calcium in permeabilized cells.

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Year:  1988        PMID： 2844178     DOI： 10.1016/s0006-291x(88)80561-8

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Phosphorylation of connexin43 gap junction protein in uninfected and Rous sarcoma virus-transformed mammalian fibroblasts.

Authors:  D S Crow; E C Beyer; D L Paul; S S Kobe; A F Lau
Journal:  Mol Cell Biol       Date:  1990-04       Impact factor: 4.272

2.  Stimulation of protein phosphatases as a mechanism of the muscarinic-receptor-mediated inhibition of cardiac L-type Ca2+ channels.

Authors:  S Herzig; A Meier; M Pfeiffer; J Neumann
Journal:  Pflugers Arch       Date:  1995-02       Impact factor: 3.657

3.  Chromostatin inhibits catecholamine secretion in adrenal chromaffin cells by activating a protein phosphatase.

Authors:  E Galindo; J Zwiller; M F Bader; D Aunis
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-15       Impact factor: 11.205
  3 in total

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