The lysine derivative aminoadipic acid, a biomarker of protein oxidation and diabetes-risk, induces production of reactive oxygen species and impairs trypsin secretion in mouse pancreatic acinar cells.

Autor: Estaras M; Institute of Molecular Pathology Biomarkers, University of Extremadura, Cáceres, Spain., Ameur FZ; Laboratoire de Physiologie de la Nutrition et de Sécurité Alimentaire, Université d'Oran1 Ahmed BenBella, Algeria., Estévez M; IPROCAR Research Institute, TECAL Research Group, University of Extremadura, 10003, Cáceres, Spain., Díaz-Velasco S; IPROCAR Research Institute, TECAL Research Group, University of Extremadura, 10003, Cáceres, Spain., Gonzalez A; Institute of Molecular Pathology Biomarkers, University of Extremadura, Cáceres, Spain. Electronic address: agmateos@unex.es.
Jazyk: angličtina
Zdroj: Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association [Food Chem Toxicol] 2020 Nov; Vol. 145, pp. 111594. Date of Electronic Publication: 2020 Jul 30.
DOI: 10.1016/j.fct.2020.111594
Abstrakt: We have examined the effects of α-aminoadipic acid, an oxidized derivative from the amino acid lysine, on the physiology of mouse pancreatic acinar cells. Changes in intracellular free-Ca 2+ concentration, the generation of reactive oxygen species, the levels of carbonyls and thiobarbituric-reactive substances, cellular metabolic activity and trypsin secretion were studied. Stimulation of mouse pancreatic cells with cholecystokinin (1 nM) evoked a transient increase in [Ca 2+ ] i . In the presence of α-amoniadipic acid increases in [Ca 2+ ] i were observed. In the presence of the compound, cholecystokinin induced a Ca 2+ response that was smaller compared with that observed when cholecystokinin was applied alone. Stimulation of cells with cholecystokinin in the absence of Ca 2+ in the extracellular medium abolished further mobilization of Ca 2+ by α-aminoadipic acid. In addition, potential pro-oxidant conditions, reflected as increases in ROS generation, oxidation of proteins and lipids, were noted in the presence of α-aminoadipic acid. Finally, the compound impaired trypsin secretion induced by the secretagogue cholecystokinin. We conclude that the oxidized derivative from the amino acid lysine induces pro-oxidative conditions and the impairment of enzyme secretion in pancreatic acinar cells. α-aminoadipic acid thus creates a situation that could potentially lead to disorders in the physiology of the pancreas.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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