근수축시 해당작용에 의한 근형질 세망의 Ca2+ 변화가 미토콘드리아 Ca2+ 증가에 미치는 영향
Glycolysis Mediated Sarcoplasmic Reticulum Ca2+ Signal Regulates Mitochondria Ca2+ during Skeletal Muscle Contraction
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PURPOSE: This study was to investigate the Glycolysis mediated sarcoplasmic reticulum (SR) Ca2+ signal regulates mitochondria Ca2+ during skeletal muscle contraction by using glycolysis inhibitor. METHODS: To examine the effect of Glycolysis inhibitor on SR and mitochondria Ca2+ content, we used skeletal muscle fiber from gastrocnemius muscle. 2-deoxy glucose and 3-bromo pyruvate used as glycolysis inhibitor, it applied to electrically stimulated muscle contraction experiment. Intracellular Ca2+ content, SR, mitochondria Ca2+ level and mitochondria membrane potential (MMP) was detected by confocal microscope. Mitochondrial energy metabolism related enzyme, citric acid synthase activity also examined for mitochondrial function during the muscle contraction. RESULTS: Treatment of 2-DG and 3BP decreased the muscle contraction induced SR Ca2+ increase however the mitochondria Ca2+ level was increased by treatment of inhibitors and showed and overloading as compared with the control group. Glycolysis inhibitor and thapsigargin treatment showed a significant decrease in MPP of skeletal muscle cells compared to the control group. CS activity significantly decreased after pretreatment of glycolysis inhibitor during skeletal muscle contraction. These results suggest that regulation of mitochondrial Ca2+ levels by glycolysis is an important factor in mitochondrial energy production during skeletal muscle contraction CONCLUSIONS: These results suggest that mitochondria Ca2+ level can be regulated by SR Ca2+ level and glycolytic regulation of intraocular Ca2+ signal play pivotal role in regulation of mitochondria energy metabolism during the muscle contraction.
Abstract
PURPOSE: This study was to investigate the Glycolysis mediated sarcoplasmic reticulum (SR) Ca2+ signal regulates mitochondria Ca2+ during skeletal muscle contraction by using glycolysis inhibitor. METHODS: To examine the effect of Glycolysis inhibitor on SR and mitochondria Ca2+ content, we used skeletal muscle fiber from gastrocnemius muscle. 2-deoxy glucose and 3-bromo pyruvate used as glycolysis inhibitor, it applied to electrically stimulated muscle contraction experiment. Intracellular Ca2+ content, SR, mitochondria Ca2+ level and mitochondria membrane potential (MMP) was detected by confocal microscope. Mitochondrial energy metabolism related enzyme, citric acid synthase activity also examined for mitochondrial function during the muscle contraction. RESULTS: Treatment of 2-DG and 3BP decreased the muscle contraction induced SR Ca2+ increase however the mitochondria Ca2+ level was increased by treatment of inhibitors and showed and overloading as compared with the control group. Glycolysis inhibitor and thapsigargin treatment showed a significant decrease in MPP of skeletal muscle cells compared to the control group. CS activity significantly decreased after pretreatment of glycolysis inhibitor during skeletal muscle contraction. These results suggest that regulation of mitochondrial Ca2+ levels by glycolysis is an important factor in mitochondrial energy production during skeletal muscle contraction CONCLUSIONS: These results suggest that mitochondria Ca2+ level can be regulated by SR Ca2+ level and glycolytic regulation of intraocular Ca2+ signal play pivotal role in regulation of mitochondria energy metabolism during the muscle contraction.
참고문헌 (49)
- Lanner JT, "Ca(2+)and insulin-mediated glucose uptake", Current Opinion in Pharmacology, 8(3), pp.339~345 (2008)
- Kuo IY, "Signaling in muscle contraction", Cold Spring Harbor Perspectives in Biology, 7(2), pp.a006023~ (2015)
- Chin ER, "Role of Ca2+", calmodulin-dependent kinases in skeletal muscle plasticity, 2005, pp.99(2), 414~423
- Eisner V, "Interactions between sarco-endoplasmic reticulum and mitochondria in cardiac and skeletal muscle-pivotal roles in Ca2+ and reactive oxygen species signaling", Journal of Cell Science, 126, pp.2965~2978 (2013)
- Hernández-Ochoa EO, "Critical Role of Intracellular RyR1 Calcium Release Channels in Skeletal Muscle Function and Disease", Frontiers in Physiology, 6, pp.420~ (2016)
- Gehlert S, "Ca2+-dependent regulations and signaling in skeletal muscle : from electro-mechanical coupling to adaptation", International Journal of Molecular Sciences, 16(1), pp.1066~1095 (2015)
- Xu KY, "Functional coupling between glycolysis and sarcoplasmic reticulum Ca2+ transport", Circulation Research, 77(1), pp.88~97 (1995)
- Marchi S, "The mitochondrial calcium uniporter complex : molecular components, structure and physiopathological implications", Journal of Physiology, 592(5), pp.829~839 (2014)
- Wan B, "Regulation of citric acid cycle by calcium", Journal of Biological Chemistry, 264(23), pp.13430~13439 (1989)
- Joiner ML, "CaMKII and stress mix it up in mitochondria", Frontiers in Pharmacology, 5, pp.67~ (2014)
- Fieni F, "Mitochondrial Ca2+uniporter and CaMKII in heart", Nature, 513(7519), pp.E1~E2 (2014)
- Shoshan-Barmatz V, "VDAC1 functions in Ca2+ homeostasis and cell life and death in health and disease", Cell Calcium, 4160(17), pp.30105~30107 (2017)
- Roberts DJ, "Hexokinase II integrates energy metabolism and cellular protection : Akting on mitochondria and TORCing to autophagy", Cell Death & Differentiation, 22(2), pp.248~257 (2015)
- Lemeshko VV, "VDAC electronics: 1. VDAC-hexo(gluco)kinase generator of the mitochondrial outer membrane potential", Biochimica et Biophysica Acta, 1838(5), pp.1362~1371 (2014)
- De Backer F, "Long-term study of Ca(2+) homeostasis and of survival in collagenase-isolated muscle fibres from normal and mdx mice", Journal of Physiology, 542(Pt 3), pp.855~865 (2002)
- Liu Y, "Activity-dependent nuclear translocation and intranuclear distribution of NFATc in adult skeletal muscle fibers", Journal of Cell Biology, 155, pp.27~39 (2001)
- Tsien RY, "T-cell mitogens cause early changes in cytoplasmic free Ca2+ and membrane potential in lymphocytes", Nature, 295, pp.68~71 (1982)
- Ghosh TK, "Persistent intracellular calcium pool depletion by thapsigargin and its influence on cell growth", Journal of Biological Chemistry, 266(36), pp.24690~24697 (1991)
- Moshal KS, "Mitochondrial MMP activation, dysfunction and arrhythmogenesis in hyperhomocysteinemia", Current Vascular Pharmacology, 6(2), pp.84~92 (2008)
- Gehlert S, "Ca2+-dependent regulations and signaling in skeletal muscle : from electro-mechanical coupling to adaptation", International Journal of Molecular Sciences, 16(1), pp.1066~1095 (2015)
- Zhou J, "Mitochondrial Ca(2+)uptake in skeletal muscle health and disease", Science China Life Sciences, 59(8), pp.770~776 (2016)
- Kohlhaas M, "Calcium release microdomains and mitochondria", Cardiovascular Research, 98(2), pp.259~268 (2013)
- Berridge MJ, "Calcium signalling : dynamics, homeostasis and remodelling", Nature Reviews Molecular Cell Biology, 4(7), pp.517~529 (2003)
- Rieusset J., "Contribution of mitochondria and endoplasmic reticulum dysfunction in insulin resistance: Distinct or interrelated roles?", Diabetes & Metabolism, 41(5), pp.358~368 (2015)
- Gomez L, "The SR", ER-mitochondria calcium crosstalk is regulated by GSK3β during reperfusion injury, 2016, pp.23(2), 313~322
- Paillusson S, "There’s Something Wrong with my MAM; the ER-Mitochondria Axis and Neurodegenerative Diseases", Trends in Neurosciences, 39(3), pp.146~157 (2016)
- Panfili E, "The role of hexokinase as a possible modulator of Ca2+ movements in isolated rat brain mitochondria", Biochemical and Biophysical Research Communications, 131(1), pp.6~12 (1985)
- Nogueira L, "Ca2+-pumping impairment during repetitive fatiguing contractions in single myofibers:role of cross-bridge cycling", American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, 305(2), pp.R118~R125 (2013)
- Baskin RJ, "A membrane-bound creatine phosphokinase in fragmented sarcoplasmic reticulum", Journal of Biological Chemistry, 245, pp.1345~1347 (1970)
- Korge P, "Local ATP regeneration is important for sarcoplasmic reticulum Ca2+ pump function", American Journal Of Physiology-Cell Physiology, 267, pp.C357~C366 (1994)
- Csordás G, "Sorting of calcium signals at the junctions of endoplasmic reticulum and mitochondria", Cell Calcium, 29(4), pp.249~262 (2001)
- Li S, "Intracellular alkalinization induces cytosolic Ca2+ increases by inhibiting sarco", endoplasmic reticulum Ca2+-ATPase (SERCA), 2012, pp.7(2), e31905~
- Ravera S, "Evaluation of energy metabolism and calcium homeostasis in cells affected by Shwachman-Diamond syndrome", Scientific Reports, 6, pp.25441~ (2016)
- Nguyen MH, "Mitochondrial calcium signaling and energy metabolism", Annals of the New York Academy of Sciences, 1047, pp.127~137 (2005)
- Bianchi K, "Calcium and mitochondria: mechanisms and functions of a troubled relationship", Biochimica et Biophysica Acta, 1742(1-3), pp.119~131 (2004)
- Madreiter-Sokolowski CT, "Resveratrol Specifically Kills Cancer Cells by a Devastating Increase in the Ca2+ Coupling Between the Greatly Tethered Endoplasmic Reticulum and Mitochondria", Cellular Physiology and Biochemistry, 39(4), pp.1404~1420 (2016)
- Malli R, "The role of mitochondria for Ca2+ refilling of the endoplasmic reticulum", Journal of Biological Chemistry, 280(13), pp.12114~12122 (2005)
- Waldeck-Weiermair M, "Molecularly distinct routes of mitochondrial Ca2+uptake are activated depending on the activity of the sarco", endoplasmic reticulum Ca2+ ATPase(SERCA), 2013, pp.288(21), 15367~15379
- Bechara LR, "NADPH oxidase hyperactivity induces plantaris atrophy in heart failure rats", International Journal of Cardiology, 175(3), pp.499~507 (2014)
- Zhang Q, "Hexokinase II inhibitor, 3-BrPA induced autophagy by stimulating ROS formation in human breast cancer cells", Genes and Cancer, 5(3-4), pp.100~112 (2014)
- Mailloux RJ, "Glucose regulates enzymatic sources of mitochondrial NADPH in skeletal muscle cells; a novel role for glucose-6-phosphate dehydrogenase", Federation of American Societies for Experimental Biology J, 24(7), pp.2495~2506 (2010)
- Potter M, "The Warburg effect : 80 years on", Biochemical Society Transactions, 44(5), pp.1499~1505 (2016)
- Anderson NM, "The emerging role and targetability of the TCA cycle in cancer metabolism", Protein & Cell (2017)[DOI]
- Lis P, "The HK2 Dependent “Warburg Effect” and Mitochondrial Oxidative Phosphorylation in Cancer: Targets for Effective Therapy with 3-Bromopyruvate", Molecules, 21(12), pp.pii: E1730~ (2016)
- Woessner S, "Nonspherocytic congenital hemolytic anemia induced by a pyruvate kinase deficiency. Presentation of a clinical case", Sangre (Barc), 13(1), pp.61~66 (1968)
- Sureira TM, "Influence of artistic gymnastics on iron nutritional status and exercise-induced hemolysis in female athletes", International Journal of Sport Nutrition and Exercise Metabolism, 22(4), pp.243~250 (2012)
- Baker JS, "Interaction among Skeletal Muscle Metabolic Energy Systems during Intense Exercise", Journal of Nutrition and Metabolism, 2010, pp.905612~ (2010)
- Sommese L, "Ryanodine receptor phosphorylation by CaMKII promotes spontaneous Ca(2+)release events in a rodent model of early stage diabetes : The arrhythmogenic substrate", International Journal of Cardiology, 202, pp.394~406 (2016)
- Jiang D, "Letm1, the mitochondrial Ca2+", H+ antiporter, is essential for normal glucose metabolism and alters brain function in Wolf-Hirschhorn syndrome, 2013, pp.110(24), E2249~E2254
