GTP-sensitive Phosphorylation of Proteins in a Postmitochondrial Supernatant from Rat Brainstem Affected by ACTH1-24

Overview

Journal Neurochem Res

Specialties Chemistry
Neurology

Date 1981 Aug 1

PMID 6273759

Citations 2

Authors

A M van Dijk

G B King

P Schotman

W H Gispen

Affiliations

Soon will be listed here.

Abstract

The effect of ACTH1-24 and cyclic nucleotides on the endogenous phosphorylation of proteins from a postmitochondrial supernatant from rat brainstem was investigated in the presence and absence of GTP. Phosphorylation and its modulation by these compounds were studied in vitro by incorporation of labeled phosphate from [gamma-32P]ATP added to the incubation mixture. Phosphoproteins were subsequently analyzed by autoradiography after one- and two-dimensional separation. Eight ACTH-sensitive phosphoproteins of molecular weights 75 (IEP 4.0), 67, 64, 50 (IEP 4.7), 47 (IEP 4.8), 38, 34, and 24K were found. The effects of ACTH on phosphorylation were mainly inhibitory, and the affected protein bands did not coincide with the phosphoproteins sensitive to cyclic AMP and cyclic GMP. Phosphorylation of those phosphoprotein bands and its ACTH sensitivity appeared to be highly sensitive to GTP. It is suggested that the activity of protein kinases involved in hormone-sensitive phosphorylation in a postmitochondrial rat brainstem fraction is regulated by GTP-dependent mechanisms.

Citing Articles

Multiple phosphorylation of pp30, a rat brain polyribosomal protein, sensitive to polyamines and corticotropin.

Schrama L, Weeda G, Edwards P, Oestreicher A, Schotman P Biochem J. 1984; 224(3):747-53.

PMID: 6098265 PMC: 1144509. DOI: 10.1042/bj2240747.

Cyclic nucleotide- and calcium-independent phosphorylation of proteins in rat brain polyribosome: effects of ACTH, spermine, and hemin.

Schrama L, Frankena H, Edwards P, Schotman P Neurochem Res. 1984; 9(9):1267-81.

PMID: 6095130 DOI: 10.1007/BF00973039.

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