Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle

dc.contributor.authorOjuka, Edward O
dc.date.accessioned2021-10-08T07:22:54Z
dc.date.available2021-10-08T07:22:54Z
dc.date.issued2004
dc.description.abstractContractile activity induces mitochondrial biogenesis and increases glucose transport capacity in muscle. There has been much research on the mechanisms responsible for these adaptations. The present paper reviews the evidence, which indicates that the decrease in the levels of high-energy phosphates, leading to activation of AMP kinase (AMPK), and the increase in cytosolic Ca(2+), which activates Ca(2+)/calmodulin-dependent protein kinase (CAMK), are signals that initiate these adaptative responses. Although the events downstream of AMPK and CAMK have not been well characterized, these events lead to activation of various transcription factors, including: nuclear respiratory factors (NRF) 1 and 2, which cause increased expression of proteins of the respiratory chain; PPAR-alpha, which up regulates the levels of enzymes of beta oxidation; mitochondrial transcription factor A, which activates expression of the mitochondrial genome; myocyte-enhancing factor 2A, the transcription factor that regulates GLUT4 expression. The well-orchestrated expression of the multitude of proteins involved in these adaptations is mediated by the rapid activation of PPAR gamma co-activator (PGC) 1, a protein that binds to various transcription factors to maximize transcriptional activity. Activating AMPK using 5-aminoimidizole-4-carboxamide-1-beta-D-riboside (AICAR) and increasing cytoplasmic Ca(2+) using caffeine, W7 or ionomycin in L6 myotubes increases the concentration of mitochondrial enzymes and GLUT4 and enhances the binding of NRF-1 and NRF-2 to DNA. AICAR and Ca-releasing agents also increase the levels of PGC-1, mitochondrial transcription factor A and myocyte-enhancing factors 2A and 2D. These results are similar to the responses seen in muscle during the adaptation to endurance exercise and show that L6 myotubes are a suitable model for studying the mechanisms by which exercise causes the adaptive responses in muscle mitochondria and glucose transport.
dc.identifier.apacitationOjuka, E. O. (2004). Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle. <i>The Proceedings of the Nutrition Society</i>, 63(2), 275 - 278. http://hdl.handle.net/11427/35025en_ZA
dc.identifier.chicagocitationOjuka, Edward O "Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle." <i>The Proceedings of the Nutrition Society</i> 63, 2. (2004): 275 - 278. http://hdl.handle.net/11427/35025en_ZA
dc.identifier.citationOjuka, E.O. 2004. Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle. <i>The Proceedings of the Nutrition Society.</i> 63(2):275 - 278. http://hdl.handle.net/11427/35025en_ZA
dc.identifier.issn0029-6651
dc.identifier.issn1475-2719
dc.identifier.ris TY - Journal Article AU - Ojuka, Edward O AB - Contractile activity induces mitochondrial biogenesis and increases glucose transport capacity in muscle. There has been much research on the mechanisms responsible for these adaptations. The present paper reviews the evidence, which indicates that the decrease in the levels of high-energy phosphates, leading to activation of AMP kinase (AMPK), and the increase in cytosolic Ca(2+), which activates Ca(2+)/calmodulin-dependent protein kinase (CAMK), are signals that initiate these adaptative responses. Although the events downstream of AMPK and CAMK have not been well characterized, these events lead to activation of various transcription factors, including: nuclear respiratory factors (NRF) 1 and 2, which cause increased expression of proteins of the respiratory chain; PPAR-alpha, which up regulates the levels of enzymes of beta oxidation; mitochondrial transcription factor A, which activates expression of the mitochondrial genome; myocyte-enhancing factor 2A, the transcription factor that regulates GLUT4 expression. The well-orchestrated expression of the multitude of proteins involved in these adaptations is mediated by the rapid activation of PPAR gamma co-activator (PGC) 1, a protein that binds to various transcription factors to maximize transcriptional activity. Activating AMPK using 5-aminoimidizole-4-carboxamide-1-beta-D-riboside (AICAR) and increasing cytoplasmic Ca(2+) using caffeine, W7 or ionomycin in L6 myotubes increases the concentration of mitochondrial enzymes and GLUT4 and enhances the binding of NRF-1 and NRF-2 to DNA. AICAR and Ca-releasing agents also increase the levels of PGC-1, mitochondrial transcription factor A and myocyte-enhancing factors 2A and 2D. These results are similar to the responses seen in muscle during the adaptation to endurance exercise and show that L6 myotubes are a suitable model for studying the mechanisms by which exercise causes the adaptive responses in muscle mitochondria and glucose transport. DA - 2004 DB - OpenUCT DP - University of Cape Town IS - 2 J1 - The Proceedings of the Nutrition Society LK - https://open.uct.ac.za PY - 2004 SM - 0029-6651 SM - 1475-2719 T1 - Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle TI - Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle UR - http://hdl.handle.net/11427/35025 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/35025
dc.identifier.vancouvercitationOjuka EO. Role of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle. The Proceedings of the Nutrition Society. 2004;63(2):275 - 278. http://hdl.handle.net/11427/35025.en_ZA
dc.language.isoeng
dc.publisher.departmentDepartment of Human Biology
dc.publisher.facultyFaculty of Health Sciences
dc.sourceThe Proceedings of the Nutrition Society
dc.source.journalissue2
dc.source.journalvolume63
dc.source.pagination275 - 278
dc.source.urihttps://dx.doi.org/10.1079/PNS2004339
dc.subject.otherAdaptation, Physiological
dc.subject.otherAdenylate Kinase
dc.subject.otherCalcium
dc.subject.otherCalcium-Calmodulin-Dependent Protein Kinases
dc.subject.otherGlucose Transporter Type 4
dc.subject.otherHumans
dc.subject.otherMitochondria, Muscle
dc.subject.otherMonosaccharide Transport Proteins
dc.subject.otherMuscle Contraction
dc.subject.otherMuscle Proteins
dc.subject.otherMuscle, Skeletal
dc.subject.otherGlucose Transporter Type 4
dc.titleRole of calcium and AMP kinase in the regulation of mitochondrial biogenesis and GLUT4 levels in muscle
dc.typeJournal Article
uct.type.publicationResearch
uct.type.resourceJournal Article
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