Literature DB >> 2650803

Distribution and possible metabolic role of class III alcohol dehydrogenase in the human brain.

P R Giri1, M Linnoila, J B O'Neill, D Goldman.   

Abstract

In human brain, the sole alcohol dehydrogenase (ADH) present in significant quantity has been shown to be Class III (chi) ADH and this ADH is ineffective in generating potentially toxic and reactive acetaldehyde from ethanol at concentrations attainable in living brain tissue. We have extended this finding to show that Class I ADH potentially present is undetectable even when concentrated several hundred-fold. Purified Class III ADH from human brain is identical in its pattern of tryptic peptides and in other properties to Class III ADH from human liver. Immunohistochemical staining and western immunoblots using polyclonal antibodies reveal that Class III ADH is widely distributed in brian and most concentrated in the subependymal layer and perivascular areas. Class III ADH closely resembles omega-hydroxyfatty acid dehydrogenase and a possible role for the brain enzyme is in the oxidation of long chain fatty alcohols and omega-hydroxyfatty acids.

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Year:  1989        PMID: 2650803     DOI: 10.1016/0006-8993(89)90493-9

Source DB:  PubMed          Journal:  Brain Res        ISSN: 0006-8993            Impact factor:   3.252


  3 in total

1.  Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation.

Authors:  K Engeland; J O Höög; B Holmquist; M Estonius; H Jörnvall; B L Vallee
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-15       Impact factor: 11.205

2.  Ventilatory responses during and following exposure to a hypoxic challenge in conscious mice deficient or null in S-nitrosoglutathione reductase.

Authors:  Lisa A Palmer; Walter J May; Kimberly deRonde; Kathleen Brown-Steinke; James N Bates; Benjamin Gaston; Stephen J Lewis
Journal:  Respir Physiol Neurobiol       Date:  2012-11-24       Impact factor: 1.931

3.  The activity of alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) in the sera of patients with brain cancer.

Authors:  Wojciech Jelski; Magdalena Laniewska-Dunaj; Karolina Orywal; Jan Kochanowicz; Robert Rutkowski; Maciej Szmitkowski
Journal:  Neurochem Res       Date:  2014-10-10       Impact factor: 3.996

  3 in total

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