Characterization of the guanosine 3??5?-monophosphate-dependent protein kinase from silkworm eggs and analysis of the endogenous protein substrates

1985 ◽  
Vol 155 (6) ◽  
pp. 693-701 ◽  
Author(s):  
Susumu Y. Takahashi
Keyword(s):  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Protein Substrates ◽  
Endogenous Protein ◽  
Dependent Protein

scholarly journals Identification and characterization of Ca2+-phospholipid-dependent protein kinase in rat islets and hamster β-cells

1984 ◽  
Vol 219 (2) ◽  
pp. 547-551 ◽  
Author(s):  
J M Lord ◽  
S J H Ashcroft
Keyword(s):  
Protein Kinase ◽  
Beta Cells ◽  
Kinetic Properties ◽  
Dependent Protein Kinase ◽  
Protein Substrates ◽  
Rat Islets ◽  
Endogenous Protein ◽  
Dependent Protein ◽  
Rat Islets Of Langerhans

We show that extracts of rat islets of Langerhans and of cloned hamster beta-cells (HIT-T15 cells) contain Ca2+-phospholipid-dependent protein kinase and endogenous protein substrates for the kinase. We purified Ca2+-phospholipid-dependent protein kinase from HIT-T15 beta-cells and report here its physical and kinetic properties.

Parathyroid hormone modulates protein kinase in giant cell tumors of human bone

1980 ◽  
Vol 239 (2) ◽  
pp. E144-E149 ◽  
Author(s):  
D. A. Ausiello ◽  
M. Rosenblatt ◽  
J. M. Dayer
Keyword(s):  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Giant Cell ◽  
Giant Cell Tumors ◽  
Dependent Protein Kinase ◽  
Protein Substrates ◽  
Endogenous Protein ◽  
Dependent Protein ◽  
Tumors Of Bone

The physiological effects of parathyroid hormone (PTH) in bone are mediated at least in part by cyclic AMP. The biochemical events subsequent to this step have not been well characterized in this tissue. Giant cell tumors of bone (GT) increase cyclic AMP in response to PTH. This response can be inhibited by an analogue of bovine PTH, [Nle8, Nle18, Tyr34] bPTH-(3-34) amide (PTH-Inh). Cyclic AMP content and cyclic AMP-dependent protein kinase (cAMP-PK) were assayed in fresh tumors and cells in culture incubated with 1 microgram/ml of bPTH and/or PTH-Inh. PTH fully activated cAMP-PK in GT, and PTH-Inh completely inhibited PTH-stimulated increases in cyclic AMP content and cAMP-PK activity. When endogenous protein substrates were sought for cAMP-PK, three phosphoproteins of 55,000, 43,000, and 38,000 mol wt maximally increased their phosphorylation by 30% after 12-min incubation with bPTH. Dephosphorylation of proteins of 200,000 and 120,000 mol wt was also observed. These data are consistent with the hypothesis that PTH action in bone is mediated by the phosphorylation and dephosphorylation of specific substrates.

scholarly journals Characterization of Ca2+/calmodulin-dependent protein kinase IV. Role in transcriptional regulation.

1994 ◽  
Vol 269 (22) ◽  
pp. 15520-15527 ◽  
Author(s):  
H. Enslen ◽  
P. Sun ◽  
D. Brickey ◽  
S.H. Soderling ◽  
E. Klamo ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein
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