Literature DB >> 3366301

Intralobular distribution of rat liver aldehyde dehydrogenase and alcohol dehydrogenase.

H Yamazaki1, K Nishiguchi, K Inoue, T Yasuyama, S Nakanishi.   

Abstract

1. The activity of liver microsomal high Km-ALDH and mitochondrial low Km-ALDH, which may be primarily responsible for the oxidation of acetaldehyde after ethanol administration was found to be predominantly distributed in the centrilobular area. 2. The activities of other ALDH isozymes in mitochondrial and soluble fractions were evenly distributed in periportal and perivenous regions. 3. The activity of ADH which is involved in production of acetaldehyde was predominantly located in the periportal area. 4. From these results it seems unlikely that a concentration of acetaldehyde after ethanol ingestion is higher in perivenous hepatocytes than in periportal ones. Additional data would be needed to understand fully the mechanism by which ethanol induces predominantly centrilobular liver injury.

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Year:  1988        PMID: 3366301     DOI: 10.1016/0020-711x(88)90212-1

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  2 in total

1.  Nitric oxide and hypoxia exacerbate alcohol-induced mitochondrial dysfunction in hepatocytes.

Authors:  Blake R Zelickson; Gloria A Benavides; Michelle S Johnson; Balu K Chacko; Aparna Venkatraman; Aimee Landar; Angela M Betancourt; Shannon M Bailey; Victor M Darley-Usmar
Journal:  Biochim Biophys Acta       Date:  2011-09-24

2.  Heterogenic response of the liver parenchyma to ethanol studied in the bivascularly perfused rat liver.

Authors:  Carlos Henrique Lopez; Jorgete Constantin; Daniele Gimenes; Fumie Suzuki-Kemmelmeier; Adelar Bracht
Journal:  Mol Cell Biochem       Date:  2004-03       Impact factor: 3.396

  2 in total

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