scholarly journals Hindbrain A2 noradrenergic neuron adenosine 5′-monophosphate-activated protein kinase activation, upstream kinase/phosphorylase protein expression, and receptivity to hormone and fuel reporters of short-term food deprivation are regulated by estradiol

2016 ◽  
Vol 95 (7) ◽  
pp. 1427-1437 ◽  
Author(s):  
Karen P. Briski ◽  
Fahaad S.H. Alenazi ◽  
Manita Shakya ◽  
Paul W. Sylvester
Keyword(s):  
Protein Kinase ◽  
Protein Expression ◽  
Food Deprivation ◽  
Noradrenergic Neuron ◽  
Short Term ◽  
Kinase Activation ◽  
Protein Kinase Activation ◽  
Upstream Kinase

Regulation of protein kinase by vasopressin in renal medulla in situ

1977 ◽  
Vol 232 (1) ◽  
pp. F50-F57
Author(s):  
T. P. Dousa ◽  
L. D. Barnes
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Kinase Inhibitor ◽  
Renal Medulla ◽  
Protein Kinase Activity ◽  
Kinase Activation ◽  
Heat Stable ◽  
Protein Kinase Activation ◽  
Heat Stable Protein

Results of this study demonstrate that vasopressin activates protein kinase in intact renal medullary cells as detected by measurement of the (-cyclic AMP/+cyclic AMP) protein kinase activity ratios in freshly prepared tissue extracts (40,000 X g supernates) from bovine renal medullary slices. The activation of protein kinase was specific for vasopressin since parathyroid hormone, histamine, angiotensin II, or the inactive analog of vasopressin did not activate protein kinase. There was a direct correlation between the extent of protein kinase activation and the elevation in tissue levels of cyclic AMP elicited by increasing doses of vasopressin or with an increase in incubation time. The elevation of tissue cyclic AMP level and maximum activation of protein kinase reached maximum level at a vasopressin concentration of about 2 X 10(-9) M. Incubation of slices with vasopressin caused a dose-dependent decrease in the cyclic AMP-dependent protein kinase activity in the 40,000 X g supernate of homogenate from the renal medullary slices. This effect of vasopressin was specific for protein kinase since activity of lactate dehydrogenase or a specific [3H]colchicine-binding activity was not affected, and the decrease in the protein kinase was not due to the accumulation of a heat-stable protein kinase inhibitor. There was an increase in protein kinase was not due to the accumulation of a heat-stable protein kinase inhibitor. There was an increase in protein kinase activity extracted from 40,000 X g pellets of homogenate prepared from slices exposed to vasopressin. Results thus provide evidence that cyclic AMP-mediated protein kinase activation in the intact cells is an integral part of cellular response of the mammalian renal medulla to vasopressin.

Use of Hyperosmolar Stress to Measure Stress-Activated Protein Kinase Activation and Function in Human HTR Cells and Mouse Trophoblast Stem Cells

2007 ◽  
Vol 14 (6) ◽  
pp. 534-547 ◽  
Author(s):  
Wenjing Zhong ◽  
Yufen Xie ◽  
Yingchun Wang ◽  
Jennifer Lewis ◽  
Anna Trostinskaia ◽  
...  
Keyword(s):  
Stem Cells ◽  
Protein Kinase ◽  
Kinase Activation ◽  
Trophoblast Stem Cells ◽  
Trophoblast Stem ◽  
Protein Kinase Activation ◽  
And Function
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