scholarly journals Five Constituents in Psoralea corylifolia L. Attenuate Palmitic Acid-Induced Hepatocyte Injury via Inhibiting the Protein Kinase C-α/Nicotinamide-Adenine Dinucleotide Phosphate Oxidase Pathway

2020 ◽  
Vol 10 ◽  
Author(s):  
Lishan Zhou ◽  
Jianqiao Tang ◽  
Xuan Yang ◽  
Hui Dong ◽  
Xiaoli Xiong ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Palmitic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Psoralea Corylifolia ◽  
Kinase C ◽  
Hepatocyte Injury

scholarly journals Protein Kinase C Epsilon Regulates Mitochondrial Pools of Nampt and NAD Following Resveratrol and Ischemic Preconditioning in the Rat Cortex

2014 ◽  
Vol 34 (6) ◽  
pp. 1024-1032 ◽  
Author(s):  
Kahlilia C Morris-Blanco ◽  
Charles H Cohan ◽  
Jake T Neumann ◽  
Thomas J Sick ◽  
Miguel A Perez-Pinzon
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Ischemic Preconditioning ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Dependent Manner ◽  
Nicotinamide Phosphoribosyltransferase ◽  
Resveratrol Treatment ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Preserving mitochondrial pools of nicotinamide adenine dinucleotide (NAD) or nicotinamide phosphoribosyltransferase (Nampt), an enzyme involved in NAD production, maintains mitochondrial function and confers neuroprotection after ischemic stress. However, the mechanisms involved in regulating mitochondrial-localized Nampt or NAD have not been defined. In this study, we investigated the roles of protein kinase C epsilon (PKCε) and AMP-activated protein kinase (AMPK) in regulating mitochondrial pools of Nampt and NAD after resveratrol or ischemic preconditioning (IPC) in the cortex and in primary neuronal-glial cortical cultures. Using the specific PKCε agonist ψεRACK, we found that PKCε induced robust activation of AMPK in vitro and in vivo and that AMPK was required for PKCε-mediated ischemic neuroprotection. In purified mitochondrial fractions, PKCε enhanced Nampt levels in an AMPK-dependent manner and was required for increased mitochondrial Nampt after IPC or resveratrol treatment. Analysis of intrinsic NAD autofluorescence using two-photon microscopy revealed that PKCε modulated NAD in the mitochondrial fraction. Further assessments of mitochondrial NAD concentrations showed that PKCε has a key role in regulating the mitochondrial NAD+/nicotinamide adenine dinucleotide reduced (NADH) ratio after IPC and resveratrol treatment in an AMPK- and Nampt-dependent manner. These findings indicate that PKCε is critical to increase or maintain mitochondrial Nampt and NAD after pathways of ischemic neuroprotection in the brain.

Palmitic Acid Increases Endothelin-1 Expression in Vascular Endothelial Cells through the Induction of Endoplasmic Reticulum Stress and Protein Kinase C Signaling

Cardiology ◽  
2018 ◽  
Vol 140 (3) ◽  
pp. 133-140 ◽  
Author(s):  
Juan Zhang ◽  
Wen-Shu Zhao ◽  
Xin Wang ◽  
Lin Xu ◽  
Xin-Chun Yang
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Palmitic Acid ◽  
Er Stress ◽  
Statistical Significance ◽  
Saturated Fatty Acids ◽  
Endothelin 1 ◽  
Kinase C

Objective: We investigated the regulation of endothelin-1 (ET-1) expression in in vivo high-fat diet (HFD)-fed mice and in vitro cultured human aortic endothelial cells (HAECs). Methods: Male C57BL/6 mice were fed on standard chow, serum was prepared, and ET-1 levels were analyzed using an ELISA kit. Quantitative PCR was performed using iQ SYBR Green Supermix. Statistical significance was assessed using SPSS, with p < 0.05 considered significant. Results: The serum ET-1 content and endothelial expression of ET-1 mRNA were increased in the HFD-fed mice compared to the chow-fed control mice. Moreover, the mRNA expression of ET-1 was significantly increased in cultured HAECs in response to acute (< 24 h) and chronic (12–16 days) treatments with palmitic acid (PA), one of the most abundant saturated fatty acids in obesity. We found that the induction of ET-1 expression by PA was abolished by pretreating the cells with the endoplasmic reticulum (ER) stress inhibitor 4-phenylbutyric acid or the protein kinase C (PKC) inhibitor Gö 6850. Conclusion: Our findings demonstrate for the first time that PA increases ET-1 expression in endothelial cells through the induction of ER stress and the activation of PKC, providing novel mechanistic insights into the pathogenesis of obesity-associated hypertension and cardiovascular diseases.

scholarly journals Regularities of endogenous lipid metabolites formation in phorbol 12-miristate 13-acetate-stimulated peripheral blood lymphocytes at leukemia

2011 ◽  
Vol 57 (4) ◽  
pp. 420-428
Author(s):  
T.B. Batikyan ◽  
G.V. Hakopyan ◽  
M.P. Lazyan ◽  
T.P. Torgomyan ◽  
R.A. Kazaryan ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Palmitic Acid ◽  
Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Biologically Active ◽  
Leukemic Cells ◽  
Blood Lymphocytes ◽  
Kinase C ◽  
Lipid Metabolites

Regularities of biologically active lipid metabolites formation in dynamics (5, 10, 30, 60 s) by phorbol 12-miristate 13-acetate stimulation in [14C]palmitic acid have been investigated in normal and leukemia peripheral blood lymphocytes prelabeled with [14C]palmitate. In normal cells there was two-phase formation of 1,2-diacylglycerol (5, 30 s), lysophosphatidylcholine (10, 60 s), as well as free palmitic acid at 10 s of stimulation. Under the identical experimental conditions there was inhibition of investigated lipid release processes at early (5 and 10 s) stages of stimulation of leukemic lymphocytes. At later (30, 60 s) terms of these lymphocytes the activation, basically, similar to norm changes in the formation of palmitic acid-containing metabolites except free palmitic acid (the level of which raised only at 60 second of the post-stimulation) was found. Various protein kinases C are involved in the regulation of investigated lipid levels at certain stages of signal transduction both in norm, and in blast cells. Short-term (5, 10 s) activations of healthy donors lymphocytes are coupled to functioning of Са2+-independent isoforms of protein kinase C. The inhibition of this protein kinase C in leukemic cells leads to normalization of the investigated lipid release. The data obtained suggests disorders of early membrane-bound reactions in agonist - and a protein kinase C-mediated processes of formation palmitic acid-containing lipid metabolites in the leukemic cells in comparison with the norm.

scholarly journals Induction of autophagy by palmitic acid via protein kinase C-mediated signaling pathway independent of mTOR (mammalian target of rapamycin).

2014 ◽  
Vol 289 (14) ◽  
pp. 9501-9501 ◽  
Author(s):  
Shi Hao Tan ◽  
Guanghou Shui ◽  
Jing Zhou ◽  
Jasmine Jia'En Li ◽  
Boon-Huat Bay ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Palmitic Acid ◽  
Signaling Pathway ◽  
Mammalian Target Of Rapamycin ◽  
Target Of Rapamycin ◽  
Kinase C

scholarly journals Diabetes Mellitus Increases Reactive Oxygen Species Production in the Thyroid of Male Rats

Endocrinology ◽  
2013 ◽  
Vol 154 (3) ◽  
pp. 1361-1372 ◽  
Author(s):  
Maria C. S. Santos ◽  
Ruy A. N. Louzada ◽  
Elaine C. L. Souza ◽  
Rodrigo S. Fortunato ◽  
Andressa L. Vasconcelos ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Reactive Oxygen Species ◽  
Protein Kinase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Thyroid Disease ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Reactive Oxygen ◽  
Nicotinamide Adenine ◽  
H2o2 Production ◽  
Oxygen Species

Abstract Diabetes mellitus (DM) disrupts the pituitary-thyroid axis and leads to a higher prevalence of thyroid disease. However, the role of reactive oxygen species in DM thyroid disease pathogenesis is unknown. Dual oxidases (DUOX) is responsible for H2O2 production, which is a cosubstrate for thyroperoxidase, but the accumulation of H2O2 also causes cellular deleterious effects. Nicotinamide adenine dinucleotide phosphate oxidase 4 (NOX4) is another member of the nicotinamide adenine dinucleotide phosphate oxidase family expressed in the thyroid. Therefore, we aimed to evaluate the thyroid DUOX activity and expression in DM rats in addition to NOX4 expression. In the thyroids of the DM rats, we found increased H2O2 generation due to higher DUOX protein content and DUOX1, DUOX2, and NOX4 mRNA expressions. In rat thyroid PCCL3 cells, both TSH and insulin decreased DUOX activity and DUOX1 mRNA levels, an effect partially reversed by protein kinase A inhibition. Most antioxidant enzymes remained unchanged or decreased in the thyroid of DM rats, whereas only glutathione peroxidase 3 was increased. DUOX1 and NOX4 expression and H2O2 production were significantly higher in cells cultivated with high glucose, which was reversed by protein kinase C inhibition. We conclude that thyroid reactive oxygen species is elevated in experimental rat DM, which is a consequence of low-serum TSH and insulin but is also related to hyperglycemia per se.

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