Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0848237 (acute stress)
 4,619 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies suggest that protein synthesis in the liver may be influenced by alterations in hepatic proteolysis and gluconeogenesis. Since proteolysis and gluconeogenesis are accelerated in acute stress states (especially when associated with nutrient deprivation), these alterations may substantially affect hepatic protein synthesis, the integrity of which is important for host survival. In the present study, we have investigated albumin secretion and glucose production in primary cultures of rat hepatocytes in response to nutrient-limiting conditions, including amino acid depletion, proteolysis inhibition, and augmented gluconeogenesis. In nonlimiting nutrient culture medium containing 10 times the normal plasma amino acid concentrations, hepatocytes produced 8.05 +/- 1.62 micrograms/plate-hr of albumin. Short-term (5 hr) inhibition of cellular protein degradation with the lysosomal protease inhibitor leupeptin did not influence albumin production, but caused a profound reduction (17-41%) when amino acid supply was reduced to the physiologic range (1.5-0.5 times, respectively). This indicates the need for active proteolysis for the maintenance of secretory protein production during nutrient limitation. Similarly, leupeptin inhibited glucose production by 22-30% at physiologic (1.5 times and 0.5 times, respectively) amino acid concentrations. Additionally, hepatocyte glucose production could be augmented 168% by epinephrine (2 microM) in 10 times medium, but this response was markedly depressed by leupeptin. Similar catecholamine-mediated effects, but of a smaller magnitude, were noted at lower medium amino acid concentrations. These findings indicate that hepatocyte albumin and glucose production are associated with the common factor of active cellular proteolysis, probably through the regulation of amino acid supply. However, protein synthesis exhibits a higher priority, since stimulated hepatocyte glucose production did not substantially alter albumin secretion.
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PMID:Factors affecting secretory protein production in primary cultures of rat hepatocytes. 847 37

Glucocorticoid actions in the brain, particularly in the hippocampus and the hypothalamus, are critically involved in the response of the organism to stress. The key molecules in this process are the corticosteroid receptors, which upon activation, migrate and act in the nucleus. We have investigated the effect of stress on the activated form of the cytosolic glucocorticoid receptor from the above brain areas, using anion exchange chromatography. Exposure of rats to chronic stress resulted in the disappearance of the chromatographic peak, which corresponds to the activated form (DE II) of the hormone-receptor complex. For this phenomenon to occur, 1) the animal must be exposed to chronic, and not to acute stress, and 2) the adrenals of the animal must be intact. The disappearance of the activated form of the hormone-receptor complex (DE II) following chronic stress is most probably due to proteolysis of the receptor molecule, since it is specifically inhibited by the protease inhibitor leupeptin. This phenomenon may represent an adaptive mechanism which helps the organism cope with a repeated stressor.
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PMID:Stress affects the activated form of the corticosteroid-receptor complex in the rat brain. 2155 71