Promotion of granule cell survival by high K+ or excitatory amino acid treatment and Ca2+/calmodulin-dependent protein kinase activity

The effects of histamine on heart cAMP-dependent protein kinase activity, cAMP levels, phosphorylase activity, and contractile force was investigated in the perfused guinea pig heart. To accurately determine the protein kinase activity ratio in guinea pig heart, it was necessary to measure kinase activity in whole homogenates immediately after homogenization of the tissue. Histamine produced a rapid dose-dependent increase in cAMP and the protein kinase activity ratio followed by increased in contractile force and phosphorylase activity. There was a good correlation between the degree of protein kinase activation and the increase in phosphorylase and force. The beta-adrenergic blocking agent propranolol did not reduce the effects of histamine, but metiamide, a potent H2-receptor antagonist, greatly attenuated all the effects of histamine. The data support the hypothesis that increases in heart cAMP-dependent protein kinase activity produce corresponding increases in contractile force and phosphorylase activity.

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A phytotoxin Solanapyrone-A downregulates calcium-dependent protein kinase activity in potato

Genetics and Molecular Research ◽

10.4238/2013.may.13.7 ◽

2013 ◽

Vol 12 (2) ◽

pp. 1540-1545 ◽

Cited By ~ 1

Author(s):

A. Hassan ◽

N. Hatsugai ◽

M.M. Shah

Keyword(s):

Protein Kinase ◽

Kinase Activity ◽

Protein Kinase Activity ◽

Dependent Protein Kinase ◽

Calcium Dependent ◽

Dependent Protein ◽

Calcium Dependent Protein Kinase

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Imaging of cAMP-dependent protein kinase activity in living neural cells using a novel fluorescent substrate

FEBS Letters ◽

10.1016/s0014-5793(97)00970-8 ◽

1997 ◽

Vol 414 (1) ◽

pp. 55-60 ◽

Cited By ~ 29

Author(s):

Hideyoshi Higashi ◽

Kazuki Sato ◽

Atsuko Ohtake ◽

Akira Omori ◽

Sachiyo Yoshida ◽

...

Keyword(s):

Protein Kinase ◽

Kinase Activity ◽

Protein Kinase Activity ◽

Neural Cells ◽

Dependent Protein Kinase ◽

Fluorescent Substrate ◽

Camp Dependent Protein Kinase ◽

Dependent Protein

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The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle.

Molecular and Cellular Biology ◽

10.1128/mcb.11.8.4045 ◽

1991 ◽

Vol 11 (8) ◽

pp. 4045-4052 ◽

Cited By ~ 86

Author(s):

S Garrett ◽

M M Menold ◽

J R Broach

Keyword(s):

Cell Cycle ◽

Protein Kinase ◽

Kinase Activity ◽

Specific Activity ◽

S Phase ◽

Protein Kinase Activity ◽

Dependent Protein Kinase ◽

Protein Levels ◽

Cycle Arrest ◽

Dependent Protein

Null mutations in the gene YAK1, which encodes a protein with sequence homology to known protein kinases, suppress the cell cycle arrest phenotype of mutants lacking the cyclic AMP-dependent protein kinase (A kinase). That is, loss of the YAK1 protein specifically compensates for loss of the A kinase. Here, we show that the protein encoded by YAK1 has protein kinase activity. Yak1 kinase activity is low during exponential growth but is induced at least 50-fold by arrest of cells prior to the completion of S phase. Induction is not observed by arrest at stages later in the cell cycle. Depending on the arrest regimen, induction can occur either by an increase in Yak1 protein levels or by an increase in Yak1 specific activity. Finally, an increase in Yak1 protein levels causes growth arrest of cells with attenuated A kinase activity. These results suggest that Yak1 acts in a pathway parallel to that of the A kinase to negatively regulate cell proliferation.

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