scholarly journals Phosphorylation of microtubule-associated proteins by a Ca2+/calmodulin-dependent protein kinase.

1984 ◽  
Vol 99 (1) ◽  
pp. 11-19 ◽  
Author(s):  
H Schulman
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Deae Cellulose ◽  
Affinity Column ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Apparent Homogeneity ◽  
Associated Proteins ◽  
Dependent Protein ◽  
Considerable Homology

In an earlier study I demonstrated that rat brain cytosol contains a Ca2+/calmodulin-dependent protein kinase activity that phosphorylates microtubule-associated protein 2 (MAP-2) but not MAP-1. Comparison of sites of phosphate incorporated in MAP-2 catalyzed by the Ca2+/calmodulin-dependent kinase activity and the cyclic AMP-dependent protein kinase activity in cytosolic extracts revealed distinct sites of phosphorylation (Schulman, H., 1984, Mol. Cell. Biol., 4:1175-1178; abstract by me and J.A. Kuret and K.H. Spitzer [1983, Fed. Proc., 42:2250]. I have now used MAP-2 as a substrate to purify the Ca2+/calmodulin-dependent protein kinase responsible for MAP-2 phosphorylation. The brain appears to contain a single predominant Ca2+/calmodulin-dependent protein kinase that phosphorylates MAP-2. The enzyme was purified to apparent homogeneity by column chromatography using DEAE-cellulose, phosphocellulose, hydroxylapatite, Sepharose 6B, and a calmodulin-Sepharose affinity column. The 580,000-dalton holoenzyme consists of 51,000- and 60,000-dalton subunits. The purified enzyme phosphorylates MAP-2 at the same "sites" that are phosphorylated in cytosolic extracts and thus has the same specificity as the activity present in cytosol. Analysis of phosphorylated MAP-2.1 and MAP-2.2, the two components of MAP-2, suggests considerable homology in their phosphorylated domains.

scholarly journals Protein phosphorylation in human peripheral blood lymphocytes. Subcellular distribution and partial characterization of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase

1979 ◽  
Vol 182 (2) ◽  
pp. 525-536 ◽  
Author(s):  
D D Chaplin ◽  
H J Wedner ◽  
C W Parker
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Human Peripheral Blood ◽  
Deae Cellulose ◽  
Peripheral Blood Lymphocytes ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Human Peripheral Blood Lymphocytes ◽  
Dependent Protein

Cytoplasmic and membrane fractions prepared from human peripheral-blood lymphocytes both contained cyclic AMP-dependent protein kinase activity and endogenous protein kinase substrates. Protein kinase activity in the particulate fractions was not eluted with 0.25 M-NaCl, suggesting that it was not derived from non-specifically absorbed soluble cytoplasmic protein kinase. Nor was the particulate protein kinase activity eluted by treatment with cyclic AMP, suggesting that the catalytic subunit is membrane-bound and arguing against cyclic AMP-induced translocation of particulate activity. Cyclic AMP-dependent protein-phosphorylating activity in the cytoplasmic fraction was highly sensitive to inhibition by Mn2+, and was co-eluted from DEAE-cellulose primarily with type-I rabbit skeletal-muscle kinase. Cyclic AMP-dependent phosphorylating activity in the plasma-membrane fractions was stimulated at low [Mn2+] and inhibited only at high [Mn2+]. When solubilized with Nonidet P-40, plasma-membrane protein kinase was co-eluted from DEAE-cellulose with type-II rabbit muscle kinase. These differences, together with the strong association of the particulate kinases with the particulate fraction, suggest the possibility of compartmentalized protein phosphorylation in intact lymphocytes.

Tenellones A and B from aDiaporthesp.:  Two Highly Substituted Benzophenone Inhibitors of Parasite cGMP-Dependent Protein Kinase Activity

2005 ◽  
Vol 68 (4) ◽  
pp. 611-613 ◽  
Author(s):  
Chaowei Zhang ◽  
John G. Ondeyka ◽  
Kithsiri B. Herath ◽  
Ziqiang Guan ◽  
Javier Collado ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Dependent Protein

Analytical subcellular distribution of cAMP-dependent protein kinase activity in bull sperm

1984 ◽  
Vol 10 (4) ◽  
pp. 433-444 ◽  
Author(s):  
Claude C. Pariset ◽  
Jacqueline S. Weinman ◽  
Francoise T. Escaig ◽  
Michele Y. Guyot ◽  
Francine C. Iftode ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Subcellular Distribution ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Bull Sperm

Involvement of cAMP-dependent protein kinase in the regulation of heart contractile force. II

1979 ◽  
Vol 236 (1) ◽  
pp. H84-H91
Author(s):  
S. L. Keely ◽  
A. Eiring
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Contractile Force ◽  
Protein Kinase Activity ◽  
Phosphorylase Activity ◽  
Dependent Protein Kinase ◽  
Guinea Pig Heart ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

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.

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

FEBS Letters ◽  
1997 ◽  
Vol 414 (1) ◽  
pp. 55-60 ◽  
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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