Interfacial Membrane Properties Modulate Protein Kinase C Activation:  Role of the Position of Acyl Chain Unsaturation†

Biochemistry ◽  
1998 ◽  
Vol 37 (31) ◽  
pp. 10956-10960 ◽  
Author(s):  
Jennifer R. Giorgione ◽  
Ruud Kraayenhof ◽  
Richard M. Epand
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Acyl Chain ◽  
Membrane Properties ◽  
Kinase C ◽  
Protein Kinase C Activation ◽  
Interfacial Membrane

scholarly journals Mechanisms of Cardiac Hypertrophy and Injury. Possible Role of Protein Kinase C Activation.

1991 ◽  
Vol 55 (11) ◽  
pp. 1149-1157 ◽  
Author(s):  
ISSEI KOMURO ◽  
YOUICHI KATOH ◽  
EITETSU HOH ◽  
FUMIMARO TAKAKU ◽  
YOSHIO YAZAKI
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cardiac Hypertrophy ◽  
Kinase C ◽  
Protein Kinase C Activation

Modification of Na+/H+ Exchanger in Human Platelets by 1,2-Dioctanoylglycerol, a Protein Kinase C Activator

1990 ◽  
Vol 64 (01) ◽  
pp. 165-171 ◽  
Author(s):  
Yukio Ozaki ◽  
Yuki Mastsumoto ◽  
Yutaka Yatomi ◽  
Masaaki Higashihara
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rate Constant ◽  
Human Platelets ◽  
Kinase C ◽  
Km Value ◽  
The Difference ◽  
The One ◽  
Protein Kinase C Activation

SummaryProtein kinase C activation in human platelets has a modulatory role in maintaining intracellular pH (pHi), by adjusting pHi at a particular value (7.22). Changes in pHi induced by protein kinase C appeared to be dependent upon the difference between H+ efflux catalyzed by the Na+/H+ exchanger and H+ production. The pHi recovery after acid loading was significantly facilitated by protein kinase C activation. Analysis of the rate constant for pHi recovery suggested that the turnover rate or the apparent affinity of the Na+/H+ exchanger for H+ was increased. Protein kinase C also decreased the Km value of the Na+/H+ exchanger for extracellular Na+. Thus, it is suggested that the role of protein kinase C in platelet pHi regulation is dual, adjusting the pHi value at a certain setpoint on the one hand, and increasing the rate constant of the Na+/H+ exchanger on the other.

The role of protein kinase C activation in signal transmission by interleukin 2

1988 ◽  
Vol 154 (1) ◽  
pp. 187-193 ◽  
Author(s):  
Naofumi Mukaida ◽  
Hitoshi Yagisawa ◽  
Tadashi Kawai ◽  
Tadashi Kasahara
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Signal Transmission ◽  
Interleukin 2 ◽  
Kinase C ◽  
Protein Kinase C Activation

scholarly journals The phosphorylation of protein kinase C as a potential measure of activation

1989 ◽  
Vol 261 (1) ◽  
pp. 131-136 ◽  
Author(s):  
F E Mitchell ◽  
R M Marais ◽  
P J Parker
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Phosphorylation State ◽  
Kinase C ◽  
Epidermal Growth ◽  
Potential Measure ◽  
Protein Kinase C Activation

As a means of determining the role of protein kinase C in the signal transduction from novel growth factors and hormones, we investigated the effects of well-characterized agents on the phosphorylation state of protein kinase C itself. These studies show that agents that stimulate protein kinase C either directly (phorbol esters) or indirectly through phosphatidylinositol breakdown (platelet-derived growth factor) induce an increase in the phosphorylation state of the kinase. By contrast, epidermal growth factor, which does not stimulate protein kinase C in fibroblasts, does not increase the phosphorylation state of protein kinase C, but leads to a decrease. The data suggest that the phosphorylation state of protein kinase C is dynamically controlled and can be used to provide evidence of protein kinase C activation.

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