Distribution of membrane-bound cyclic AMP-dependent protein kinase in plasma membranes of cells of the kidney cortex

1975 ◽  
Vol 24 (1) ◽  
pp. 145-159 ◽  
Author(s):  
Rolf Kinne ◽  
Linda J. Shlatz ◽  
Evamaria Kinne-Saffran ◽  
Irving L. Schwartz
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Plasma Membranes ◽  
Kidney Cortex ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Membrane Bound

scholarly journals Substrates for cyclic AMP-dependent protein kinase in islets of Langerhans. Studies with forskolin and catalytic subunit

1985 ◽  
Vol 227 (3) ◽  
pp. 727-736 ◽  
Author(s):  
M R Christie ◽  
S J Ashcroft
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Insulin Release ◽  
Islets Of Langerhans ◽  
Plasma Membranes ◽  
Sodium Dodecyl ◽  
Catalytic Subunit ◽  
Subcellular Fractions ◽  
Dependent Protein Kinase ◽  
Dependent Protein

To investigate substrates for cyclic AMP-dependent protein kinase in intact islets of Langerhans, batches of islets were incubated with [32P]Pi for 1 h in the presence of 10 mM-glucose; the adenylate cyclase activator forskolin, which in parallel experiments was shown to increase islet cyclic AMP content and insulin release, was then added. Islets were homogenized and subcellular fractions prepared by differential centrifugation. Phosphopeptides were electrophoresed on sodium dodecyl sulphate/polyacrylamide gels and quantified by autoradiography and densitometry. Within 5 min forskolin caused increased labelling of Mr-25 000 and −30 000 cytosolic and Mr-23 000 and −32 000 particulate peptides; a rapid decrease in phosphorylation of Mr-18 000 and −34 000 cytosolic peptides was also observed. In addition, rather slower phosphorylation occurred of the Mr-15 000 peptide previously identified as histone H3 [Christie & Ashcroft (1984) Biochem. J. 218, 87-99]. When similar subcellular fractions were incubated with [gamma-32P]ATP and purified catalytic subunit of cyclic AMP-dependent protein kinase, peptides phosphorylated included cytosolic species of Mr 25 000 and 30 000 and particulate species of Mr 23 000 and 32 000. The distribution of RNA in the subcellular fractions suggested that the Mr-32 000 species could be a ribosomal protein. The 24 000 g pellet was heterogeneous, as judged by marker assays, and was therefore fractionated further by Percoll-density-gradient centrifugation. The peak containing the Mr-23 000 peptide was resolved from marker enzymes for plasma membranes, mitochondria and endoplasmic reticulum and coincided with a peak for insulin: hence the Mr-23 000 peptide is likely to be a secretory-granule component. The study demonstrates that the potentiation of insulin release that occurs when islet cyclic AMP is increased is accompanied by rapid phosphorylation of specific islet substrates for cyclic AMP-dependent protein kinase. The data are consistent with the hypothesis that protein phosphorylation is involved in the regulation of insulin secretion.

scholarly journals Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in the plasma membranes of different blood cells

FEBS Letters ◽  
1983 ◽  
Vol 161 (1) ◽  
pp. 158-162 ◽  
Author(s):  
Ágnes Enyedi ◽  
Anna Faragó ◽  
B. Sarkadi ◽  
Ilma Szász ◽  
G. Gárdos
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Blood Cells ◽  
Plasma Membranes ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Catalytic unit-independent phosphorylation and dephosphorylation of type II regulatory subunit of cyclic AMP-dependent protein kinase in rat liver plasma membranes

1986 ◽  
Vol 234 (1) ◽  
pp. 163-168 ◽  
Author(s):  
Z Kiss ◽  
Y Luo ◽  
G Vereb
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Regulatory Subunit ◽  
Dependent Protein Kinase ◽  
Liver Plasma Membranes ◽  
Catalytic Unit ◽  
Rat Liver Plasma Membranes ◽  
Dependent Protein ◽  
Membrane Bound

Rat liver plasma membranes contain a 55 kDa protein which proved to be identical with type II regulatory subunit (RII) of the cyclic AMP-dependent protein kinase (kinase A) by several criteria (gel electrophoretic behaviour, peptide map, position of the autophosphorylated site). Analysis of phosphopeptide maps revealed that the membrane-bound RII was phosphorylated by a kinase which is unrelated to the catalytic unit (C) of kinase A. Dephosphorylation of the membrane-bound RII by an endogenous phosphatase was stimulated by both cyclic AMP and fluoride. Addition of C did not stimulate dephosphorylation even in the presence of ADP; moreover, protein inhibitor of C did not modify the effects of cyclic AMP or fluoride. The effects of both cyclic AMP and fluoride were, however, inhibited by C. Results indicate that rat liver plasma membranes contain a phosphorylation-dephosphorylation system for which RII is a relatively specific substrate.

scholarly journals Species-dependent isoenzyme subtypes of membrane-bound cyclic AMP-dependent protein kinase in highly purified cardiac sarcolemma

1986 ◽  
Vol 238 (2) ◽  
pp. 341-344 ◽  
Author(s):  
J G Church ◽  
J B Derdemezi ◽  
S Yuan ◽  
A K Sen
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Cardiac Muscle ◽  
Type I ◽  
Type Ii ◽  
Dependent Protein Kinase ◽  
Cardiac Sarcolemma ◽  
Photoaffinity Label ◽  
Dependent Protein ◽  
Membrane Bound

Highly purified sarcolemma from dog and pig cardiac muscle has been shown to contain significant activities of a membrane-bound cyclic AMP-dependent protein kinase. In addition, these membranes undergo endogenous phosphorylation when incubated with Mg2+ and [gamma-32P]ATP. By comparing 32P-labelled patterns obtained with [gamma-32P]ATP and the photoaffinity label 8-azidoadenosine 3′:5′-[32P]monophosphate (8-azido-cyclic [32P]AMP), we have demonstrated that, whereas the major kinase isoenzyme in dog sarcolemma was Type II, that in the pig membrane was the Type I isoenzyme.

scholarly journals A cytosolic cyclic AMP-dependent protein kinase in Dictyostelium discoideum. I. Properties.

1984 ◽  
Vol 259 (1) ◽  
pp. 654-661 ◽  
Author(s):  
I H Majerfeld ◽  
B H Leichtling ◽  
J A Meligeni ◽  
E Spitz ◽  
H V Rickenberg
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Dictyostelium Discoideum ◽  
Dependent Protein Kinase ◽  
Dependent Protein
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