Control of pyruvate kinase flux during gluconeogenesis in isolated liver cells |
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| Affiliation: | 1. Isfahan University of Technology (IUT), Isfahan, Iran;2. Swiss Federal Laboratories for Materials Science and Technology (Empa), Überlandstrasse 129, Dübendorf, 8600, Switzerland;3. University of Tehran, Tehran, Iran;1. Ph.D.’s Degree Program in Biology (International Program), Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand;2. Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand;3. Postharvest Technology Innovation Center, Ministry of Higher Education, Science, Research and Innovation, Bangkok, 10400, Thailand;4. Research Center in Bioresources for Agriculture, Industry and Medicine, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand;1. James Cook University Hospital, Marton Road, Middlesbrough, Cleveland, TS43 BW, United Kingdom;2. University Hospital of North Tees, Hardwick Rd, Hardwick, Stockton-on-Tees TS19 8PE, United Kingdom;1. Department of Brain & Cognitive Sciences, DGIST, Daegu, Republic of Korea;2. Department of New Biology, DGIST, Daegu, Republic of Korea |
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| Abstract: | - 1.1. With pyruvate as the gluconeogenic substrate, pyruvate kinase flux, estimated isotopically, and lactate formation were inhibited by glucagon, but only slightly affected by epinephrine.
- 2.2. The glucagon effect was unchanged in the absence of calcium.
- 3.3. Ethanol increased lactate formation from pyruvate, but depressed pyruvate kinase flux.
- 4.4. These results support the role of pyruvate kinase m the cyclic mechanism which transfers mitochondrial reducing hydrogen to the cytosol.
- 5.5. Glucagon and, to a lesser degree, epinephrine inhibit lactate formation from fructose or dihydroxyacetone.
- 6.6. Ethanol also inhibits lactate formation from these substrates, suggesting the possibility that NADH may in some manner regulate pyruvate kinase flux.
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