Differential Membrane-Binding and Activation Mechanisms of Protein Kinase C-α and -ε†

Biochemistry ◽  
1998 ◽  
Vol 37 (14) ◽  
pp. 4892-4900 ◽  
Author(s):  
Martina Medkova ◽  
Wonhwa Cho
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Binding ◽  
Kinase C ◽  
Activation Mechanisms

scholarly journals Correlation between membrane binding and phosphorylation by protein kinase C of acylated protein.

1990 ◽  
Vol 54 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Toshihiko UTSUMI ◽  
Hiroshi KOFUJI ◽  
Keisuke EDASHIGE ◽  
Kozo UTSUMI ◽  
Daizo KOGA ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Binding ◽  
Kinase C

scholarly journals Correlation between Membrane Binding and Phosphorylation by Protein Kinase C of Acylated Protein

1990 ◽  
Vol 54 (1) ◽  
pp. 25-30
Author(s):  
Toshihiko Utsumi ◽  
Hiroshi Kofuji ◽  
Keisuke Edashige ◽  
Kozo Utsumi ◽  
Daizo Koga ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Binding ◽  
Kinase C

scholarly journals Peroxide generation by p47phox-Src activation of Nox2 has a key role in protein kinase C-induced arterial smooth muscle contraction

2009 ◽  
Vol 296 (4) ◽  
pp. H1048-H1057 ◽  
Author(s):  
Sachin A. Gupte ◽  
Pawel M. Kaminski ◽  
Shimran George ◽  
Lioubov Kouznestova ◽  
Susan C. Olson ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Muscle Contraction ◽  
Coronary Arteries ◽  
Rho Kinase ◽  
Smooth Muscle Contraction ◽  
Kinase C ◽  
Activation Mechanisms ◽  
Src Activation

Protein kinase C (PKC) stimulation of NAD(P)H oxidases (Nox) is an important component of multiple vascular disease processes; however, the relationship between oxidase activation and the regulation of vascular smooth muscle contraction by PKC remains poorly understood. Therefore, we examined the signaling cascade of PKC-elicited Nox activation and the role of superoxide and hydrogen peroxide in mediating PKC-induced vascular contraction. Endothelium-denuded bovine coronary arteries showed a PKC-dependent basal production of lucigenin (5 μM)-detected Nox oxidase-derived superoxide, which was stimulated fourfold by PKC activation with 10 μM phorbol 12,13-dibutyrate (PDBu). PDBu appeared to increase superoxide generation by Nox2 through both p47phox and peroxide-dependent Src activation mechanisms based on the actions of inhibitors, properties of Src phosphorylation, and the loss of responses in aorta from mice deficient in Nox2 and p47phox. The actions of inhibitors of contractile regulating mechanisms, scavengers of superoxide and peroxide, and responses in knockout mouse aortas suggest that a major component of the contraction elicited by PDBu appeared to be mediated through peroxide derived from Nox2 activation stimulating force generation through Rho kinase and calmodulin kinase-II mechanisms. Superoxide generated by PDBu also attenuated relaxation to nitroglycerin. Peroxide-derived from Nox2 activation by PKC appeared to be a major contributor to the thromboxane A2 receptor agonist U46619 (100 nM)-elicited contraction of coronary arteries. Thus a p47phox and Src kinase activation of peroxide production by Nox2 appears to be an important contributor to vascular contractile mechanisms mediated through activation of PKC.

scholarly journals Activation of protein kinase C in platelets by epinephrine and A23187: correlation with fibrinogen binding

Blood ◽  
1989 ◽  
Vol 74 (6) ◽  
pp. 2001-2006
Author(s):  
M Saitoh ◽  
EW Salzman ◽  
M Smith ◽  
JA Ware
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Phorbol Esters ◽  
Membrane Binding ◽  
Kinase C ◽  
Fibrinogen Binding ◽  
Pkc Activation ◽  
Initial Elevation

Activation of protein kinase C (PKC), as revealed by phosphorylation of a 47 kd protein (p47), occurs in platelets stimulated by some agonists (eg, thrombin or phorbol esters). It is not known if activation of PKC occurs with pairs of agonists, such as epinephrine and A23187, that do not individually phosphorylate p47, nor is it known what role the concentration of cytoplasmic Ca++ ([Ca++]i) plays in these events. We stimulated aequorin-loaded platelets with subaggregating concentrations of epinephrine and A23187, neither of which by itself phosphorylated p47. The combination of agonists resulted in p47 phosphorylation, an increase in platelet-bound fibrinogen, and aggregation, but only if the concentration of each agonist was sufficient to increase [Ca++]i if it was added separately. Subaggregating concentrations of A23187 alone released platelet fibrinogen and increased platelet membrane binding of [3H]-phorbol dibutyrate, but these were not enhanced by epinephrine. Epinephrine and A23187 did not increase production of diacylglycerol. Thus, epinephrine and A23187 together activate PKC by a mechanism that does not require phospholipase C or enhanced binding of PKC to the plasma membrane; PKC activation in turn is correlated with enhanced platelet fibrinogen binding and aggregation. These events require an initial elevation of [Ca++]i above a threshold.

Membrane Binding Kinetics of Protein Kinase C βII Mediated by the C2 Domain†

Biochemistry ◽  
2001 ◽  
Vol 40 (44) ◽  
pp. 13216-13229 ◽  
Author(s):  
Eric A. Nalefski ◽  
Alexandra C. Newton
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Binding ◽  
Binding Kinetics ◽  
C2 Domain ◽  
Kinase C ◽  
Kinetics Of
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