Acetaldehyde inhibition of protein synthesis in isolated rat pancreatic acini |
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| Authors: | A P Majumdar M J Haiman B A Zylbert H T Billy G D Vesenka M C Geokas |
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| Affiliation: | 1. Enzymology Research Laboratory, Department of Medicine, VA Medical Center, Martinez, California 94553 USA;2. Department of Medicine, University of California, Davis, California 95616 USA;1. School of Chemistry and Environmental Engineering, Key Laboratory for Green Chemical Process of Ministry of Education, Hubei Key Lab of Novel Reactor & Green Chemical Technology, Wuhan Institute of Technology, Wuhan 430073, China;2. Institute of Materials Engineering, University of Siegen, 57076 Siegen, Germany;1. LSPM–CNRS UPR 3407, Université Paris 13, Sorbonne Paris Cité, 99 Avenue Jean Baptiste Clément Villetaneuse 93430, France;2. Chemistry Department, Royal University of Phnom Penh, Russian Federation Boulevard, Toul Kork, Phnom Penh, Cambodia;1. School of Environmental and Chemical Engineering, Shanghai University, Shanghai, 200444, China;2. School of Instrument Science and Opto-electronics Engineering, Hefei University of Technology, Hefei, 230009, China;3. Kunshan Hexin Mass Spectrometry Technology Co., Ltd., Kunshan, 215311, China;1. School of Pharmacy, Anhui Medical University, Mei Shan Road, Hefei, Anhui Province, China;2. Institute for Liver Disease of Anhui Medical University, Mei Shan Road, Hefei, Anhui Province, China;3. Department of Pharmacy, The Second Hospital of Anhui Medical University, Hefei, Anhui Province, China |
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| Abstract: | Exposure of isolated dispersed pancreatic acini to increasing concentrations of ethanol (5 to 500 mM) or acetaldehyde (0.5 to 100 mM) produced a progressive inhibition of [3H]leucine incorporation into both "cellular" (those remaining in the cell) and "secretory" (those released into the medium) proteins. Whereas 500 mM ethanol caused 90-95% inhibition in the synthesis of "cellular" and "secretory" proteins, the concentration of acetaldehyde needed to produce a similar inhibition was found to be 50 mM. All subsequent experiments were performed with 12.5 mM acetaldehyde, a concentration that consistently inhibited acinar protein synthesis by about 50%. The acetaldehyde-mediated inhibition of acinar protein synthesis was partially normalized when this metabolite was removed after 30 min during a 90-min incubation period. In the presence of acetaldehyde, the secretion of 3H-pulse-labeled proteins, but not amylase, trypsinogen, or chymotrypsinogen, was greatly depressed. Acetaldehyde also caused a marked reduction in [3H]uridine incorporation into acinar RNA. The entry of [3H]uridine, [3H]leucine, and [3H]aminoisobutyric acid into isolated acini was found to be slightly (15-25%) decreased by acetaldehyde. It is concluded that acetaldehyde exerts a direct toxic effect on isolated dispersed pancreatic acini as evidenced by diminution of both protein and RNA synthesis and decreased secretion of the newly synthesized proteins. This inhibitory effect of acetaldehyde could be partially reversed. |
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