scholarly journals Comparison of lipid oxidation, messenger ribonucleic acid levels of avian uncoupling protein, avian adenine nucleotide translocator, and avian peroxisome proliferator-activated receptor-γ coactivator-1α in skeletal muscles from electrical- and gas-stunned broilers

2011 ◽  
Vol 90 (9) ◽  
pp. 2069-2075 ◽  
Author(s):  
L. Xu ◽  
S.G. Wu ◽  
H.J. Zhang ◽  
L. Zhang ◽  
H.Y. Yue ◽  
...  
Keyword(s):  
Lipid Oxidation ◽  
Ribonucleic Acid ◽  
Skeletal Muscles ◽  
Adenine Nucleotide ◽  
Uncoupling Protein ◽  
Peroxisome Proliferator ◽  
Adenine Nucleotide Translocator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Messenger Ribonucleic Acid ◽  
Avian Uncoupling Protein

scholarly journals Is the Mitochondrial Function of Keloid Fibroblasts Affected by Cytoglobin?

2021 ◽  
Vol 28 (2) ◽  
pp. 39-47
Author(s):  
Sri Widia A Jusman ◽  
Isma Nur Azzizah ◽  
Mohamad Sadikin ◽  
Novi Silvia Hardiany
Keyword(s):  
Mitochondrial Biogenesis ◽  
Mitochondrial Function ◽  
Ribonucleic Acid ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Messenger Ribonucleic Acid ◽  
Keloid Fibroblast ◽  
Excessive Proliferation ◽  
Keloid Fibroblasts

Background: A keloid is a benign skin tumour characterised by excessive proliferation of fibroblasts, a process that requires a sufficient amount of energy. The energy needs are associated with adequate oxygen (O2) flow and well-functioning mitochondria. It is known that cytoglobin (CYGB) has a function in O2 distribution. The aim of the present study was to explore whether the inhibition of CYGB expression caused impaired mitochondrial function of keloid fibroblasts. Methods: An in vitro study was conducted on a keloid fibroblast derived from our previous study. The study was carried out in the laboratory of the Biochemistry & Molecular Biology Department, Faculty of Medicine, Universitas Indonesia (FMUI), from July to December 2018. CYGB expression was inhibited by small interfering ribonucleic acid (siRNA) and CYGB. Analysis of mitochondrial function was observed through peroxisome proliferator-activated receptor gamma coactivator-1α (PGC-1α), a mitochondrial biogenesis marker and the activity of the succinate dehydrogenase (SDH) enzyme in mitochondria. Results: The CYGB gene and protein were downregulated after treatment with CYGB siRNA. Inhibition of CYGB expression with siRNA also tended to decrease the levels of PGC-1α messenger ribonucleic acid (mRNA) and protein, as well as SDH enzyme activity. Conclusion: Inhibition of CYGB expression with siRNA tended to decrease mitochondrial biogenesis and function. This may be useful for understanding the excessive proliferation of fibroblasts in keloids and for development of treatment for keloids.

scholarly journals Expression of Peroxisome Proliferator-Activated Receptor α Messenger Ribonucleic Acid and Protein in Human and Rat Testis

Endocrinology ◽  
1999 ◽  
Vol 140 (7) ◽  
pp. 2968-2975 ◽  
Author(s):  
Rüdiger Schultz ◽  
Wei Yan ◽  
Jorma Toppari ◽  
Alfred Völkl ◽  
Jan-Åke Gustafsson ◽  
...  
Keyword(s):  
Ribonucleic Acid ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Messenger Ribonucleic Acid ◽  
Rat Testis

scholarly journals Pancreatic Islet Adaptation to Fasting Is Dependent on Peroxisome Proliferator-Activated Receptor α Transcriptional Up-Regulation of Fatty Acid Oxidation

Endocrinology ◽  
2005 ◽  
Vol 146 (1) ◽  
pp. 375-382 ◽  
Author(s):  
Sandrine Gremlich ◽  
Christopher Nolan ◽  
Raphaël Roduit ◽  
Rémy Burcelin ◽  
Marie-Line Peyot ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Pancreatic Islet ◽  
Cellular Response ◽  
Uncoupling Protein ◽  
Acid Oxidation ◽  
Hyperinsulinemic Hypoglycemia ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

The cellular response to fasting and starvation in tissues such as heart, skeletal muscle, and liver requires peroxisome proliferator-activated receptor-α (PPARα)-dependent up-regulation of energy metabolism toward fatty acid oxidation (FAO). PPARα null (PPARαKO) mice develop hyperinsulinemic hypoglycemia in the fasting state, and we previously showed that PPARα expression is increased in islets at low glucose. On this basis, we hypothesized that enhanced PPARα expression and FAO, via depletion of lipid-signaling molecule(s) for insulin exocytosis, are also involved in the normal adaptive response of the islet to fasting. Fasted PPARαKO mice compared with wild-type mice had supranormal ip glucose tolerance due to increased plasma insulin levels. Isolated islets from the PPARα null mice had a 44% reduction in FAO, normal glucose use and oxidation, and enhanced glucose-induced insulin secretion. In normal rats, fasting for 24 h increased islet PPARα, carnitine palmitoyltransferase 1, and uncoupling protein-2 mRNA expression by 60%, 62%, and 82%, respectively. The data are consistent with the view that PPARα, via transcriptionally up-regulating islet FAO, can reduce insulin secretion, and that this mechanism is involved in the normal physiological response of the pancreatic islet to fasting such that hypoglycemia is avoided.

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