scholarly journals Diverse roles for protein kinase C δ and protein kinase C ε in the generation of high-fat-diet-induced glucose intolerance in mice: regulation of lipogenesis by protein kinase C δ

Diabetologia ◽  
2009 ◽  
Vol 52 (12) ◽  
pp. 2616-2620 ◽  
Author(s):  
G. Frangioudakis ◽  
J. G. Burchfield ◽  
S. Narasimhan ◽  
G. J. Cooney ◽  
M. Leitges ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Intolerance ◽  
High Fat Diet ◽  
High Fat ◽  
Kinase C

scholarly journals Diets enriched with cereal brans or inulin modulate protein kinase C activity and isozyme expression in rat colonic mucosa

2000 ◽  
Vol 84 (5) ◽  
pp. 635-643 ◽  
Author(s):  
Anne-Maria Pajari ◽  
Seija Oikarinen ◽  
Soile Gråsten ◽  
Marja Mutanen
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Wheat Bran ◽  
High Fat Diet ◽  
Colon Carcinogenesis ◽  
Rat Colon ◽  
High Fat ◽  
Tumour Development ◽  
Kinase C ◽  
Cereal Brans

The role of dietary fibres in colon carcinogenesis is controversial. To elucidate the mechanisms by which different dietary fibre sources may affect colonic tumour development, we studied the effects of diets enriched with cereal brans or inulin on protein kinase C (PKC) activity and isozyme expression in rat colon. Male Wistar rats (twelve per group) were fed one of the following AIN-93G-based diets () for 4 weeks: a non-fibre high-fat diet or one of the four high-fat diets supplemented with either rye, oat or wheat bran or inulin at 100 g/kg diet. The fat concentration (20 g/100 g) and fatty acid composition of the non-fibre high-fat diet was designed to approximate that in a typical Western-type diet. In the proximal colon, rats fed the inulin diet had a significantly higher membrane PKC activity and a higher membrane PKC δ level than rats fed the non-fibre diet (P<0·05). In the distal colon, rats fed the inulin and oat bran diets had a higher total PKC activity and a higher membrane PKC β2 level than rats fed the wheat-bran diet. Rats in the non-fibre and wheat-bran groups had the lowest concentrations of luminal diacylglycerol. In conclusion, feeding of wheat bran resulted in low distal PKC activity and expression of PKC β2, a PKC isozyme related to colonic cell proliferation and increased susceptibility for colon carcinogenesis, which may explain in part the protective effect of wheat bran against tumour development in a number of experimental colon cancer studies. The increase in PKC activity and PKC β2 expression by feeding inulin may be a drawback of inulin as a functional food.

scholarly journals Overexpression of Kinase-Negative Protein Kinase C  in Pancreatic  -Cells Protects Mice From Diet-Induced Glucose Intolerance and  -Cell Dysfunction

Diabetes ◽  
2009 ◽  
Vol 59 (1) ◽  
pp. 119-127 ◽  
Author(s):  
A. M. Hennige ◽  
F. Ranta ◽  
I. Heinzelmann ◽  
M. Dufer ◽  
D. Michael ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Intolerance ◽  
Cell Dysfunction ◽  
Kinase C ◽  
Pancreatic Cells

Protein Kinase C Is Activated and Diacylglycerol Is Elevated in Epidermal Cells from Sencar Mice Fed High Fat Diets

1992 ◽  
Vol 122 (12) ◽  
pp. 2322-2329 ◽  
Author(s):  
Myeon Choe ◽  
Edward S. Kris ◽  
Rajesh Luthra ◽  
James Copenhaver ◽  
Jill C. Pelling ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epidermal Cells ◽  
High Fat ◽  
Kinase C ◽  
High Fat Diets ◽  
Fat Diets

Alterations in the Expression and Cellular Localization of Protein Kinase C Isozymes   and   Are Associated With Insulin Resistance in Skeletal Muscle of the High-Fat-Fed Rat

Diabetes ◽  
1997 ◽  
Vol 46 (2) ◽  
pp. 169-178 ◽  
Author(s):  
C. Schmitz-Peiffer ◽  
C. L. Browne ◽  
N. D. Oakes ◽  
A. Watkinson ◽  
D. J. Chisholm ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cellular Localization ◽  
High Fat ◽  
Kinase C

scholarly journals Cardiomyocyte lipids impair β-adrenergic receptor function via PKC activation

2011 ◽  
Vol 300 (3) ◽  
pp. E489-E499 ◽  
Author(s):  
Konstantinos Drosatos ◽  
Kalyani G. Bharadwaj ◽  
Anastasios Lymperopoulos ◽  
Shota Ikeda ◽  
Raffay Khan ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
High Fat Diet ◽  
Adrenergic Receptor ◽  
Lipid Uptake ◽  
Receptor Function ◽  
High Fat ◽  
Kinase C ◽  
Cellular Lipids ◽  
Pkc Activation

Normal hearts have increased contractility in response to catecholamines. Because several lipids activate PKCs, we hypothesized that excess cellular lipids would inhibit cardiomyocyte responsiveness to adrenergic stimuli. Cardiomyocytes treated with saturated free fatty acids, ceramide, and diacylglycerol had reduced cellular cAMP response to isoproterenol. This was associated with increased PKC activation and reduction of β-adrenergic receptor (β-AR) density. Pharmacological and genetic PKC inhibition prevented both palmitate-induced β-AR insensitivity and the accompanying reduction in cell surface β-ARs. Mice with excess lipid uptake due to either cardiac-specific overexpression of anchored lipoprotein lipase, PPARγ, or acyl-CoA synthetase-1 or high-fat diet showed reduced inotropic responsiveness to dobutamine. This was associated with activation of protein kinase C (PKC)α or PKCδ. Thus, several lipids that are increased in the setting of lipotoxicity can produce abnormalities in β-AR responsiveness. This can be attributed to PKC activation and reduced β-AR levels.

scholarly journals Defective Activation of Atypical Protein Kinase C ζ and λ by Insulin and Phosphatidylinositol-3,4,5-(PO4)3 in Skeletal Muscle of Rats Following High-Fat Feeding and Streptozotocin-Induced Diabetes

Endocrinology ◽  
2003 ◽  
Vol 144 (3) ◽  
pp. 947-954 ◽  
Author(s):  
Yoshinori Kanoh ◽  
Mini P. Sajan ◽  
Gautam Bandyopadhyay ◽  
Atsushi Miura ◽  
Mary L. Standaert ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vastus Lateralis ◽  
Diabetic Rats ◽  
High Fat ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Normal Chow

Insulin-stimulated glucose transport in skeletal muscle is thought to be effected at least partly through atypical protein kinase C isoforms (aPKCs) operating downstream of phosphatidylinositol (PI) 3-kinase and 3-phosphoinositide-dependent protein kinase-1 (PDK-1). However, relatively little is known about the activation of aPKCs in physiological conditions or insulin-resistant states. Presently, we studied aPKC activation in vastus lateralis muscles of normal chow-fed and high-fat-fed rats and after streptozotocin (STZ)-induced diabetes. In normal chow-fed rats, dose-dependent increases in aPKC activity approached maximal levels after 15–30 min of stimulation by relatively high and lower, presumably more physiological, insulin concentrations, achieved by im insulin or ip glucose administration. Insulin-induced activation of aPKCs was impaired in both high-fat-fed and STZ-diabetic rats, but, surprisingly, IRS-1-dependent and IRS-2-dependent PI 3-kinase activation was not appreciably compromised. Most interestingly, direct in vitro activation of aPKCs by PI-3,4,5-(PO4)3, the lipid product of PI 3-kinase, was impaired in both high-fat-fed and STZ-diabetic rats. Defects in activation of aPKCs by insulin and PI-3,4,5-(PO4)3 could not be explained by diminished PDK-1-dependent phosphorylation of threonine-410 in the PKC-ζ activation loop, as this phosphorylation was increased even in the absence of insulin treatment in high-fat-fed rats. Conclusions: 1) muscle aPKCs are activated at relatively low, presumably physiological, as well as higher supraphysiological, insulin concentrations; 2) aPKC activation is defective in muscles of high-fat-fed and STZ-diabetic rats; and 3) defective aPKC activation in these states is at least partly due to impaired responsiveness to PI-3,4,5-(PO4)3, apparently at activation steps distal to PDK-1-dependent loop phosphorylation.

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