{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T05:12:13Z","timestamp":1773292333666,"version":"3.50.1"},"reference-count":46,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":5454,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1990,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Changes in the mRNA levels during mammalian myogenesis were compared for seven polypeptides of mitochondrial respiration (the mitochondrial DNA\u2010encoded cytochrome oxidase subunit III, ATP synthase subunit 6, NADH dehydrogenase subunits 1 and 2, and 16S ribosomal RNA; the nuclear encoded ATP synthase \u03b2 subunit and the adenine nucleotide translocase) and three polypeptides of glycolysis (glyceraldehyde\u20103\u2010phosphate dehydrogenase, pyruvate kinase, and triose\u2010phosphate isomerase). Progressive changes during the conversion from myoblasts to myotubes were monitored under both atmospheric oxygen (nor\u2010moxic) and hypoxic environments. Northern analyses revealed coordinate, biphasic, and reciprocal expression of the respiratory and glycolytic mRNAs during myogenesis. In normoxic cells the mitochondrial respiratory enzymes were highest in myoblasts, declined 3\u2010 to 5\u2010fold during commitment and exit from the cell cycle, and increased progressively as the myotubes matured. By contrast, the glycolytic enzyme mRNAs rose 3\u2010 to 6\u2010fold on commitment and then progressively declined. When partially differentiated myotubes were switched to hypoxic conditions, the glycolytic enzyme mRNAs increased and the respiratory mRNAs declined. Hence, the developmental regulation of muscle bioenergetic metabolism appears to be regulated at the pretranslational level and is modulated by oxygen tension.<\/jats:p>","DOI":"10.1002\/jcp.1041420316","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T09:56:21Z","timestamp":1109411781000},"page":"566-573","source":"Crossref","is-referenced-by-count":87,"title":["Coordinate reciprocal trends in glycolytic and mitochondrial transcript accumulations during the in vitro differentiation of human myoblasts"],"prefix":"10.1002","volume":"142","author":[{"given":"Keith A.","family":"Webster","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"Gunning","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edna","family":"Hardeman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Douglas C.","family":"Wallace","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Larry","family":"Kedes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(80)90264-8"},{"key":"e_1_2_1_3_1","first-page":"177","article-title":"Mitochondrial DNA D\u2010loop structure and mitochondrial DNA polymerase activity in mammalian striated muscles of differing oxidative capacity","volume":"13","author":"Annex B. H.","year":"1989","journal-title":"J. Cell. Biochem. [Suppl.]"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.78.9.5623"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-4827(81)90008-2"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4781(87)90029-7"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.83.17.6277"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.8.10.4502"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.53.070184.003041"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0012-1606(79)90286-0"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(87)90220-0"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.7.2.925"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(85)90216-1"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.7.11.4100"},{"key":"e_1_2_1_15_1","first-page":"1","volume-title":"The Enzymes","author":"Harris J. I.","year":"1976"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1152\/jappl.1984.56.4.831"},{"key":"e_1_2_1_17_1","doi-asserted-by":"crossref","unstructured":"Horlick R. A. andBenfield P. A.(1989)The upstream muscle\u2010specific enhancer of the rat muscle creatine kinase gene is composed of multiple","DOI":"10.1128\/mcb.9.6.2396-2413.1989"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(85)90216-1"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.7.11.4100"},{"key":"e_1_2_1_20_1","first-page":"1","volume-title":"The Enzymes","author":"Harris J. I.","year":"1976"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1152\/jappl.1984.56.4.831"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.9.6.2396"},{"key":"e_1_2_1_23_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.6.8.2855"},{"key":"e_1_2_1_24_1","doi-asserted-by":"crossref","unstructured":"Li K. Warner C. K. Hodge J. A. Minoshima S. Kudoh J. Fukuyama R. Maekawa M. Shimizu Y. Shimizu N. andWallace D. C.(1989)A human muscle adenine nucleotide translocator gene has four exons is located on chromosome 4 and is differentially expressed. J. Biol. Chem. (in press).","DOI":"10.1016\/S0021-9258(18)71632-3"},{"key":"e_1_2_1_25_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1475-4754.1982.tb01001.x"},{"key":"e_1_2_1_26_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.21.7580"},{"key":"e_1_2_1_27_1","doi-asserted-by":"crossref","unstructured":"Neckelmann N. Warner C. Chung A. Kudoh J. Minoshima S. Fukuyama R. Maekawa M. Shimizu Y. Shimizu N. andWallace D. C.(1989)The human ATP synthase \u03b2 subunit gene: Sequence analysis chromosome assignment and differential expression. (submitted to Genomics).","DOI":"10.1016\/0888-7543(89)90125-0"},{"key":"e_1_2_1_28_1","doi-asserted-by":"publisher","DOI":"10.1038\/290470a0"},{"key":"e_1_2_1_29_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00714a032"},{"key":"e_1_2_1_30_1","first-page":"847","volume-title":"Handbook of Physiology: The Cardiovascular System III","author":"Pappenheimer J. R.","year":"1981"},{"key":"e_1_2_1_31_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00428a069"},{"key":"e_1_2_1_32_1","first-page":"555","volume-title":"In: Handbook of Physiology: Skeletal Muscle. 1983","author":"Saltin B.","year":"1983"},{"key":"e_1_2_1_33_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.74.12.5463"},{"key":"e_1_2_1_34_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00517a027"},{"key":"e_1_2_1_35_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF01534741"},{"key":"e_1_2_1_36_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.8.7.2896"},{"issue":"3","key":"e_1_2_1_37_1","first-page":"137","article-title":"Medical and Experimental Mammalian Genetics: A Perspective","volume":"23","author":"Wallace D. C.","year":"1987","journal-title":"Birth Defects"},{"key":"e_1_2_1_38_1","doi-asserted-by":"publisher","DOI":"10.1159\/000132809"},{"key":"e_1_2_1_39_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00434661"},{"key":"e_1_2_1_40_1","first-page":"19","article-title":"Regulation of glycolytic enzyme transcriptional rates by oxygen availability in skeletal muscle cells","volume":"17","author":"Webster K. A.","year":"1987","journal-title":"Mol. Cell. Biochem."},{"key":"e_1_2_1_41_1","doi-asserted-by":"publisher","DOI":"10.1139\/z88-155"},{"key":"e_1_2_1_42_1","first-page":"102","article-title":"Reciprocal regulation of glycolytic and mitochondrial enzyme mRNA transcript levels by O2 tension in beating heart cell cultures","volume":"13","author":"Webster K. A.","year":"1989","journal-title":"J. Cell. Biochem. [Suppl.]"},{"key":"e_1_2_1_43_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.6.12.4539"},{"key":"e_1_2_1_44_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)67252-7"},{"key":"e_1_2_1_45_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.1987.253.6.C866"},{"key":"e_1_2_1_46_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)42482-3"},{"key":"e_1_2_1_47_1","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1016\/S0021-9258(18)61572-8","article-title":"Adaptation of skeletal muscle to increased contractile activity","volume":"262","author":"Williams R. S.","year":"1987","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Cellular Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjcp.1041420316","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/jcp.1041420316","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,22]],"date-time":"2023-10-22T18:17:11Z","timestamp":1697998631000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/jcp.1041420316"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,3]]},"references-count":46,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1990,3]]}},"alternative-id":["10.1002\/jcp.1041420316"],"URL":"https:\/\/doi.org\/10.1002\/jcp.1041420316","archive":["Portico"],"relation":{},"ISSN":["0021-9541","1097-4652"],"issn-type":[{"value":"0021-9541","type":"print"},{"value":"1097-4652","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,3]]}}}