Glucagon activation of the thiol:protein disulfide oxidoreductase in isolated, rat, hepatic microsomes |
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| Authors: | D J McConkey D L Crankshaw J L Holtzman |
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| Affiliation: | 1. Southwest Oil & Gas Field Company, PetroChina, Chengdu, Sichuan 610000, China;2. ARC Research Hub for Computational Particle Technology, Department of Chemical and Biological Engineering, Monash University, Clayton, Victoria 3800, Australia;3. State Key Laboratory of Petroleum Resources and Prospecting, China University of Petroleum (Beijing), Beijing 102249, China;1. Nantes Université, Institut des Substances et Organismes de la Mer, ISOMER, UR 2160, F-44000 Nantes, France;2. Consiglio Nazionale delle Ricerche, Istituto di Scienze Marine (CNR-ISMAR), 00133, Rome, Italy;3. Ifremer, PHYTOX, Laboratoire PHYSALG, F-44000 Nantes, France;4. Ifremer, Laboratoire Environnement Ressources Normandie, Port en Bessin, France;5. Consejo Superior de Investigaciones Científicas, Instituto de Ciencias Marinas de Andalucía, Puerto Real, Spain;6. Magellium, 1 Rue Ariane, Ramonville-Saint-Agne, France |
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| Abstract: | The hepatic, microsomal, thiol:protein disulfide oxidoreductase catalyzes the glutathione (GSH) reduction of protein disulfides to sulfhydryl groups. In the presence of physiological concentrations of glucagon this activity increased from 2.3 to 6.4 fold in isolated microsomes. The stimulation had a P50 for glucagon of 7.8 X 10(-10) M which was only observed at microsomal protein concentrations of less than 100 micrograms/ml and in the presence of a GSH reducing system. This latter observation suggests that the stimulation may be inhibited by the presence of oxidized glutathione. These data support the hypothesis that glucagon may act in part by stimulating the reduction of protein disulfides by the thiol:protein disulfide oxidoreductase. |
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