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Role of Catalase in Rat Gastric Mucosal Ethanol Metabolism In Vitro
Author(s) -
Salmela Katja S.,
Kaihovaara Pertti,
Salaspuro Mikko,
Roine Risto P.
Publication year - 1996
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1996.tb01939.x
Subject(s) - acetaldehyde , catalase , chemistry , ethanol , alcohol dehydrogenase , sodium azide , biochemistry , ethanol metabolism , metabolism , in vitro , gastric mucosa , enzyme , stomach
To evaluate the possible role of catalase in gastric ethanol metabolism in rats, we studied acetaldehyde formation from ethanol by gastric mucosal homogenate under various in vitro conditions. Homogenized rat gastric mucosa produced significant amounts of acetaldehyde in a time and ethanol concentration‐dependent manner, even in the absence of added NAD. Both acetaldehyde formation and catalase activity peaked around the physiological pH, whereas alcohol dehydrogenase (ADH) activity was in that pH range low and reached peak values only at a higher pH of 9 to 10. Catalase inhibitors sodium azide (SA) and 3‐amino‐1,2,4‐triazole (3‐AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 ± 13% of control, 5 mM of 3‐AT to 67 ± 3% of control; mean ± SE). 4‐Methylpyrazole decreased ADH activity significantly, but did not affect acetaldehyde formation. Heating of the homogenate at 60°C for 5 min decreased ADH activity only slightly, but totally abolished catalase activity and reduced acetaldehyde formation to 39 ± 3% of control. Addition of a H 2 O 2 generating system [β‐ d (+)‐glucose + glucose oxidase] increased acetaldehyde formation in a concentration‐dependent manner up to 8‐fold of the control value. Our results strongly suggest that, in addition to ADH, catalase may play a significant role in gastric ethanol metabolism in rats.