Hepatic steatosis by dietary-conjugated linoleic acid is accompanied by accumulation of diacylglycerol and increased membrane-associated protein kinase C ε in mice

2011 ◽  
Vol 55 (7) ◽  
pp. 1010-1017 ◽  
Author(s):  
Michael B. Stout ◽  
Li-Fen Liu ◽  
Martha A. Belury
Keyword(s):  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Conjugated Linoleic Acid ◽  
Hepatic Steatosis ◽  
Kinase C ◽  
Dietary Conjugated Linoleic Acid

Conjugated Linoleic Acid Inhibits Proliferation and Modulates Protein Kinase C Isoforms in Human Prostate Cancer Cells

2004 ◽  
Vol 49 (1) ◽  
pp. 100-108 ◽  
Author(s):  
Hyun-Ju Song ◽  
Alan A. Sneddon ◽  
Pamela A. Barker ◽  
Charles Bestwick ◽  
Sun-Nam Choe ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Conjugated Linoleic Acid ◽  
Human Prostate Cancer ◽  
Prostate Cancer Cells ◽  
Kinase C ◽  
Protein Kinase C Isoforms

Schistosoma mansoni: Possible involvement of protein kinase C in linoleic acid-induced proteolytic enzyme release from cercariae

1991 ◽  
Vol 72 (3) ◽  
pp. 311-320 ◽  
Author(s):  
Kenichiro Matsumura ◽  
Yoshinori Mitsui ◽  
Katsuyuki Sato ◽  
Makoto Sakamoto ◽  
Yoshiki Aoki
Keyword(s):  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Schistosoma Mansoni ◽  
Proteolytic Enzyme ◽  
Enzyme Release ◽  
Kinase C

scholarly journals Dietary Conjugated Linoleic Acid Modulates the Hepatic Circadian Clock Program via PPARα/REV-ERBα-Mediated Chromatin Modification in Mice

2021 ◽  
Vol 8 ◽  
Author(s):  
Hao-Yu Liu ◽  
Haotian Gu ◽  
Yanwei Li ◽  
Ping Hu ◽  
Yatian Yang ◽  
...  
Keyword(s):  
Linoleic Acid ◽  
Circadian Clock ◽  
Conjugated Linoleic Acid ◽  
Hepatic Steatosis ◽  
Clock Genes ◽  
Transcriptional Profiling ◽  
Chromatin Modification ◽  
Dietary Factors ◽  
Response Element ◽  
Dietary Conjugated Linoleic Acid

Scope: Disruptions of circadian rhythm cause metabolic disorders and are closely related to dietary factors. In this study, we investigated the interplays between the dietary conjugated linoleic acid (CLA)-induced hepatic steatosis and the circadian clock regulation, in association with lipid homeostasis.Methods and Results: Exposure of mice to 1.5% dietary CLA for 28 days caused insulin resistance, enlarged livers, caused hepatic steatosis, and increased triglyceride levels. Transcriptional profiling showed that hepatic circadian clock genes were significantly downregulated with increased expression of the negative transcription factor, REV-ERBα. We uncovered that the nuclear receptor (NR) PPARα, as a major target of dietary CLA, drives REV-ERBα expression via its binding to key genes of the circadian clock, including Cry1 and Clock, and the recruitment of histone marks and cofactors. The PPARα or REV-ERBα inhibition blocked the physical connection of this NR pair, reduced the cobinding of PPARα and REV-ERBα to the genomic DNA response element, and abolished histone modifications in the CLA-hepatocytes. In addition, we demonstrated that CLA promotes PPARα driving REV-ERBα transcriptional activity by directly binding to the PPAR response element (PPRE) at the Nr1d1 gene.Conclusions: Our results add a layer to the understanding of the peripheral clock feedback loop, which involves the PPARα-REV-ERBα, and provide guidance for nutrients optimization in circadian physiology.

scholarly journals Distinct Effects of Fatty Acids on Translocation of γ- and ε-Subspecies of Protein Kinase C

1998 ◽  
Vol 143 (2) ◽  
pp. 511-521 ◽  
Author(s):  
Yasuhito Shirai ◽  
Kaori Kashiwagi ◽  
Keiko Yagi ◽  
Norio Sakai ◽  
Naoaki Saito
Keyword(s):  
Fatty Acids ◽  
Arachidonic Acid ◽  
Plasma Membrane ◽  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Fluorescent Protein ◽  
Target Site ◽  
Simultaneous Application ◽  
Kinase C

Effects of fatty acids on translocation of the γ- and ε-subspecies of protein kinase C (PKC) in living cells were investigated using their proteins fused with green fluorescent protein (GFP). γ-PKC–GFP and ε-PKC–GFP predominated in the cytoplasm, but only a small amount of γ-PKC–GFP was found in the nucleus. Except at a high concentration of linoleic acid, all the fatty acids examined induced the translocation of γ-PKC–GFP from the cytoplasm to the plasma membrane within 30 s with a return to the cytoplasm in 3 min, but they had no effect on γ-PKC–GFP in the nucleus. Arachidonic and linoleic acids induced slow translocation of ε-PKC–GFP from the cytoplasm to the perinuclear region, whereas the other fatty acids (except for palmitic acid) induced rapid translocation to the plasma membrane. The target site of the slower translocation of ε-PKC–GFP by arachidonic acid was identified as the Golgi network. The critical concentration of fatty acid that induced translocation varied among the 11 fatty acids tested. In general, a higher concentration was required to induce the translocation of ε-PKC–GFP than that of γ-PKC–GFP, the exceptions being tridecanoic acid, linoleic acid, and arachidonic acid. Furthermore, arachidonic acid and the diacylglycerol analogue (DiC8) had synergistic effects on the translocation of γ-PKC–GFP. Simultaneous application of arachidonic acid (25 μM) and DiC8 (10 μM) elicited a slow, irreversible translocation of γ-PKC– GFP from the cytoplasm to the plasma membrane after rapid, reversible translocation, but a single application of arachidonic acid or DiC8 at the same concentration induced no translocation. These findings confirm the involvement of fatty acids in the translocation of γ- and ε-PKC, and they also indicate that each subspecies has a specific targeting mechanism that depends on the extracellular signals and that a combination of intracellular activators alters the target site of PKCs.

Protein Kinase C and Linoleic Acid-Induced Inhibition of Melanogenesis

1990 ◽  
Vol 3 (4) ◽  
pp. 200-206 ◽  
Author(s):  
HIDEYA ANDO ◽  
MASAHIRO OKA ◽  
MASAMITSU ICHIHASHI ◽  
YUTAKA MISHIMA
Keyword(s):  
Protein Kinase C ◽  
Linoleic Acid ◽  
Protein Kinase ◽  
Kinase C
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