scholarly journals Protein kinase C mechanisms that contribute to cardiac remodelling

2016 ◽  
Vol 130 (17) ◽  
pp. 1499-1510 ◽  
Author(s):  
Alexandra C. Newton ◽  
Corina E. Antal ◽  
Susan F. Steinberg
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Cardiac Contractility ◽  
Cellular Responses ◽  
Growth Responses ◽  
Kinase C ◽  
Wide Range ◽  
Clinical Disorders

Protein phosphorylation is a highly-regulated and reversible process that is precisely controlled by the actions of protein kinases and protein phosphatases. Factors that tip the balance of protein phosphorylation lead to changes in a wide range of cellular responses, including cell proliferation, differentiation and survival. The protein kinase C (PKC) family of serine/threonine kinases sits at nodal points in many signal transduction pathways; PKC enzymes have been the focus of considerable attention since they contribute to both normal physiological responses as well as maladaptive pathological responses that drive a wide range of clinical disorders. This review provides a background on the mechanisms that regulate individual PKC isoenzymes followed by a discussion of recent insights into their role in the pathogenesis of diseases such as cancer. We then provide an overview on the role of individual PKC isoenzymes in the regulation of cardiac contractility and pathophysiological growth responses, with a focus on the PKC-dependent mechanisms that regulate pump function and/or contribute to the pathogenesis of heart failure.

scholarly journals Role of Phosphoinositide 3-Kinase α, Protein Kinase C, and L-Type Ca 2+ Channels in Mediating the Complex Actions of Angiotensin II on Mouse Cardiac Contractility

Hypertension ◽  
2010 ◽  
Vol 56 (3) ◽  
pp. 422-429 ◽  
Author(s):  
Wenbin Liang ◽  
Gavin Y. Oudit ◽  
Mikin M. Patel ◽  
Ajay M. Shah ◽  
James R. Woodgett ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Cardiac Contractility ◽  
Kinase C ◽  
Phosphoinositide 3 Kinase

ROLE OF CAMP-RESPONSE ELEMENT-BINDING PROTEIN PHOSPHORYLATION IN HEPATIC APOPTOSIS UNDER PROTEIN KINASE C ?? SUPPRESSION DURING SEPSIS

Shock ◽  
2005 ◽  
Vol 24 (4) ◽  
pp. 357-363 ◽  
Author(s):  
Ya-Ching Hsieh ◽  
Yen-Hsu Chen ◽  
Hsiao-Ching Jao ◽  
Hseng-Kuang Hsu ◽  
Li-Ju Huang ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Binding Protein ◽  
Camp Response Element Binding ◽  
Camp Response Element ◽  
Response Element ◽  
Kinase C ◽  
Element Binding Protein

scholarly journals Role of Protein Kinase C-mediated Protein Phosphorylation in Mitochondrial Translocation of Mouse CYP1A1, Which Contains a Non-canonical Targeting Signal

2006 ◽  
Vol 281 (41) ◽  
pp. 30834-30847 ◽  
Author(s):  
Venkata Ramesh Dasari ◽  
Hindupur K. Anandatheerthavarada ◽  
Marie-Anne Robin ◽  
Ettickan Boopathi ◽  
Gopa Biswas ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Mitochondrial Translocation ◽  
Kinase C ◽  
Targeting Signal

scholarly journals Role of Protein Kinase C (PKC) in Short- and Long-Term Cellular Responses

1988 ◽  
Vol 12 ◽  
pp. 73-79 ◽  
Author(s):  
Doriano Fabbro ◽  
Nachman Mazurek ◽  
Christoph Borner ◽  
Jean-François Conscience ◽  
Paul Erne
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cellular Responses ◽  
Kinase C ◽  
Short And Long Term

scholarly journals Phorbol ester-induced actin assembly in neutrophils: role of protein kinase C.

1992 ◽  
Vol 116 (3) ◽  
pp. 695-706 ◽  
Author(s):  
G P Downey ◽  
C K Chan ◽  
P Lea ◽  
A Takai ◽  
S Grinstein
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Phosphorylation ◽  
Neutrophil Activation ◽  
Human Neutrophils ◽  
Actin Assembly ◽  
Membrane Ruffling ◽  
Kinase C

The shape changes and membrane ruffling that accompany neutrophil activation are dependent on the assembly and reorganization of the actin cytoskeleton, the molecular basis of which remains to be clarified. A role of protein kinase C (PKC) has been postulated because neutrophil activation, with the attendant shape and membrane ruffling changes, can be initiated by phorbol esters, known activators of PKC. It has become apparent, however, that multiple isoforms of PKC with differing substrate specificities exist. To reassess the role of PKC in cytoskeletal reorganization, we compared the effects of diacylglycerol analogs and of PKC antagonists on kinase activity and on actin assembly in human neutrophils. Ruffling of the plasma membrane was assessed by scanning EM, and spatial redistribution of filamentous (F)-actin was assessed by scanning confocal microscopy. Staining with NBD-phallacidin and incorporation of actin into the Triton X-100-insoluble ("cytoskeletal") fraction were used to quantify the formation of (F)-actin. [32P]ATP was used to detect protein phosphorylation in electroporated cells. Exposure of neutrophils to 4 beta-PMA (an activator of PKC) induced protein phosphorylation, membrane ruffling, and assembly and reorganization of the actin cytoskeleton, whereas the 4a-isomer, which is inactive towards PKC, failed to produce any of these changes. Moreover, 1,2-dioctanoylglycerol, mezerein, and 3-(N-acetylamino)-5-(N-decyl-N-methylamino)-benzyl alcohol, which are nonphorbol activators of PKC, also promoted actin assembly. Although these effects were consistent with a role of PKC, the following observations suggested that stimulation of conventional isoforms of the kinase were not directly responsible for actin assembly: (a) Okadaic acid, an inhibitor of phosphatases 1 and 2A, potentiated PMA-induced protein phosphorylation, but not actin assembly; and (b) PMA-induced actin assembly and membrane ruffling were not prevented by the conventional PKC inhibitors 1-(5-isoquinolinesulfonyl)-2-methylpiperazine, staurosporine, calphostin C, or sphingosine at concentrations that precluded PMA-induced protein phosphorylation and superoxide production. On the other hand, PMA-induced actin assembly was inhibited by long-chain fatty acid coenzyme A esters, known inhibitors of nuclear PKC (nPKC). We conclude that PMA-induced actin assembly is unlikely to be mediated by the conventional isoforms of PKC, but may be mediated by novel isoforms of the kinase such as nPKC.

Role of Protein Kinase C (PKC) in Short- and Long-Term Cellular Responses

1988 ◽  
Vol 12 (Supplement) ◽  
pp. 73-79
Author(s):  
Doriano Fabbro ◽  
Nachman Mazurek ◽  
Christoph Borner ◽  
Jean-François Conscience ◽  
Paul Erne
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cellular Responses ◽  
Kinase C ◽  
Short And Long Term

scholarly journals Long-term modulation of mitochondrial Ca2+ signals by protein kinase C isozymes

2004 ◽  
Vol 165 (2) ◽  
pp. 223-232 ◽  
Author(s):  
Paolo Pinton ◽  
Sara Leo ◽  
Mariusz R. Wieckowski ◽  
Giulietta Di Benedetto ◽  
Rosario Rizzuto
Keyword(s):  
Protein Kinase C ◽  
Insulin Secretion ◽  
Protein Kinase ◽  
Regulatory Mechanism ◽  
Cellular Responses ◽  
Kinase C ◽  
A Cell ◽  
Dynamic Interplay

The modulation of Ca2+ signaling patterns during repetitive stimulations represents an important mechanism for integrating through time the inputs received by a cell. By either overexpressing the isoforms of protein kinase C (PKC) or inhibiting them with specific blockers, we investigated the role of this family of proteins in regulating the dynamic interplay of the intracellular Ca2+ pools. The effects of the different isoforms spanned from the reduction of ER Ca2+ release (PKCα) to the increase or reduction of mitochondrial Ca2+ uptake (PKCζ and PKCβ/PKCδ, respectively). This PKC-dependent regulatory mechanism underlies the process of mitochondrial Ca2+ desensitization, which in turn modulates cellular responses (e.g., insulin secretion). These results demonstrate that organelle Ca2+ homeostasis (and in particular mitochondrial processing of Ca2+ signals) is tuned through the wide molecular repertoire of intracellular Ca2+ transducers.

scholarly journals Potential Role of Protein Kinase C in the Pathophysiology of Diabetes-Associated Atherosclerosis

2021 ◽  
Vol 12 ◽  
Author(s):  
Chih-Feng Lien ◽  
Sy-Jou Chen ◽  
Min-Chien Tsai ◽  
Chin-Sheng Lin
Keyword(s):  
Oxidative Stress ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
Vascular Complications ◽  
Cellular Responses ◽  
Diabetic Vascular Complications ◽  
Kinase C ◽  
Pkc Activation

Diabetes mellitus is a metabolic syndrome that affects millions of people worldwide. Recent studies have demonstrated that protein kinase C (PKC) activation plays an important role in hyperglycemia-induced atherosclerosis. PKC activation is involved in several cellular responses such as the expression of various growth factors, activation of signaling pathways, and enhancement of oxidative stress in hyperglycemia. However, the role of PKC activation in pro-atherogenic and anti-atherogenic mechanisms remains controversial, especially under hyperglycemic condition. In this review, we discuss the role of different PKC isoforms in lipid regulation, oxidative stress, inflammatory response, and apoptosis. These intracellular events are linked to the pathogenesis of atherosclerosis in diabetes. PKC deletion or treatment with PKC inhibitors has been studied in the regulation of atherosclerotic plaque formation and evolution. Furthermore, some preclinical and clinical studies have indicated that PKCβ and PKCδ are potential targets for the treatment of diabetic vascular complications. The current review summarizes these multiple signaling pathways and cellular responses regulated by PKC activation and the potential therapeutic targets of PKC in diabetic complications.

Glutamate-induced protein phosphorylation in cerebellar granule cells: Role of protein kinase C

1994 ◽  
Vol 19 (10) ◽  
pp. 1257-1264 ◽  
Author(s):  
Maria Luisa Eboli ◽  
Delio Mercanti ◽  
Maria Teresa Ciotti ◽  
Angelo Aquino ◽  
Loriana Castellani
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Cerebellar Granule ◽  
Kinase C
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