Role of protein kinase Cα in melatonin signal transduction

2006 ◽  
Vol 252 (1-2) ◽  
pp. 82-87 ◽  
Author(s):  
S.R. Sampson ◽  
Z. Lupowitz ◽  
L. Braiman ◽  
N. Zisapel
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase Cα

scholarly journals Direct evidence for a key role of protein kinase C in the development of vasospasm after subarachnoid hemorrhage

1992 ◽  
Vol 76 (4) ◽  
pp. 635-639 ◽  
Author(s):  
Shigeru Nishizawa ◽  
Nobukazu Nezu ◽  
Kenichi Uemura
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Direct Evidence ◽  
Control Group ◽  
Content Type ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Fine Print

✓ Vascular contraction is induced by the activation of intracellular contractile proteins mediated through signal transduction from the outside to the inside of cells. Protein kinase C plays a crucial role in this signal transduction. It is hypothesized that protein kinase C plays a causative part in the development of vasospasm after subarachnoid hemorrhage (SAH). To verify this directly, the authors measured protein kinase C activity in canine basilar arteries in an SAH model with (γ-32P)adenosine triphosphate and the data were compared to those in a control group. Protein kinase C is translocated to the membrane from the cytosol when it is activated, and the translocation is an index of the activation; thus, protein kinase C activity was measured both in the cytosol and in the membrane fractions. Protein kinase C activity in the membrane in the SAH model was remarkably enhanced compared to that in the control group. The percentage of membrane activity to the total was also significantly greater in the SAH vessels than in the control group, and the percentage of cytosol activity in the SAH group was decreased compared to that in the control arteries. The results indicate that protein kinase C in the vascular smooth muscle was translocated to the membrane from the cytosol and was activated when SAH occurred. It is concluded that this is direct evidence for a key role of protein kinase C in the development of vasospasm.

Role of Protein Kinase Cα in Signaling from the Histamine H1 Receptor to the Nucleus

2001 ◽  
Vol 59 (5) ◽  
pp. 1012-1021 ◽  
Author(s):  
A. C. Megson ◽  
E. M. Walker ◽  
S. J. Hill
Keyword(s):  
Protein Kinase ◽  
H1 Receptor ◽  
Histamine H1 Receptor ◽  
Protein Kinase Cα

Role of protein kinase system in the signal transduction of stretch-mediated protooncogene expression and hypertrophy of cardiac myocytes

1993 ◽  
Vol 119 (1-2) ◽  
pp. 11-16 ◽  
Author(s):  
Yoshio Yazaki ◽  
Issei Komuro ◽  
Tsutomu Yamazaki ◽  
Kazuyuki Tobe ◽  
Kouji Maemura ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Cardiac Myocytes

scholarly journals Role of the Ca2+/Phosphatidylserine Binding Region of the C2 Domain in the Translocation of Protein Kinase Cα to the Plasma Membrane

2003 ◽  
Vol 278 (12) ◽  
pp. 10282-10290 ◽  
Author(s):  
Stephen R. Bolsover ◽  
Juan C. Gomez-Fernandez ◽  
Senena Corbalan-Garcia
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
C2 Domain ◽  
Binding Region ◽  
Protein Kinase Cα

scholarly journals Targeting of Protein Kinase Cα to Caveolae

1998 ◽  
Vol 141 (3) ◽  
pp. 601-610 ◽  
Author(s):  
Chieko Mineo ◽  
Yun-Shu Ying ◽  
Christine Chapline ◽  
Susan Jaken ◽  
Richard G.W. Anderson
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Regulatory Domain ◽  
Calcium Dependent ◽  
High Affinity ◽  
Membrane Invagination ◽  
Protein Kinase Cα ◽  
Flanking Sequences ◽  
Modulate Signal ◽  
Regulatory Functions

Previously, we showed caveolae contain a population of protein kinase Cα (PKCα) that appears to regulate membrane invagination. We now report that multiple PKC isoenzymes are enriched in caveolae of unstimulated fibroblasts. To understand the mechanism of PKC targeting, we prepared caveolae lacking PKCα and measured the interaction of recombinant PKCα with these membranes. PKCα bound with high affinity and specificity to caveolae membranes. Binding was calcium dependent, did not require the addition of factors that activate the enzyme, and involved the regulatory domain of the molecule. A 68-kD PKCα-binding protein identified as sdr (serum deprivation response) was isolated by interaction cloning and localized to caveolae. Antibodies against sdr inhibited PKCα binding. A 100–amino acid sequence from the middle of sdr competitively blocked PKCα binding while flanking sequences were inactive. Caveolae appear to be a membrane site where PKC enzymes are organized to carry out essential regulatory functions as well as to modulate signal transduction at the cell surface.

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