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Genetics of alcohol dehydrogenase and aldehyde dehydrogenase from Monodelphis domestica cornea: further evidence for identity of corneal aldehyde dehydrogenase with a major soluble protein

Published online by Cambridge University Press:  14 April 2009

Roger S. Holmes ,
Roland A. H. van Oorschot  and
John L. Vandeberg
Roger S. Holmes*
Affiliation:
Department of Genetics, Southwest Foundation for Biomedical Research, P.O. Box 28147, San Antonio, TX 78284, USA Division of Science and Technology, Griffith University, Nathan, Brisbane 4111, Queensland, Australia
Roland A. H. van Oorschot
Affiliation:
Department of Genetics, Southwest Foundation for Biomedical Research, P.O. Box 28147, San Antonio, TX 78284, USA
John L. Vandeberg
Affiliation:
Department of Genetics, Southwest Foundation for Biomedical Research, P.O. Box 28147, San Antonio, TX 78284, USA
*
Dr R. S. Holmes, Division of Science and Technology, Griffith University, Nathan, Brisbane 4111, Queensland, Australia.
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A didelphid marsupial, the gray short-tailed opossum (Monodelphis domestica), was used as a model species to study the biochemical genetics of alcohol dehydrogenases (ADHs) and aldehyde dehydrogenase (ALDH) in corneal tissue. Isoelectric point variants of corneal ALDH (designated ALDH3) and a major soluble protein in corneal extracts were observed among eight families of animals used in studying the genetics of these proteins. Both phenotypes exhibited identical patterns following PAGE-IEF and were inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression. The data provided evidence for genetic identity of corneal ALDH with this major soluble protein, and supported biochemical evidence, recently reported for purified bovine corneal ALDH, that this enzyme constitutes a major portion of soluble corneal protein (Abedinia et al. 1990). Isoelectric point variants for corneal ADH were also observed, with patterns for the two major forms (ADH3 and ADH4) and one minor form (ADH5) being consistent with the presence of two ADH subunits (designated γ and δ), and variant phenotypes existing for the γ subunit. The genetics of this enzyme was studied in the eight families, and the results were consistent with codominant expression of two alleles at a single locus (designated ADH3). It is relevant that a major detoxification function has been proposed for corneal ADH and ALDH, in the oxidoreduction of peroxidic aldehydes induced by available oxygen and UV-B light (Holmes & VandeBerg, 1986a). In addition, a direct role for corneal ALDH as a UV-B photoreceptor in this anterior eye tissue has also been proposed (Abedinia et al. 1990).

Type
Research Article
Information
Genetics Research , Volume 56 , Issue 2-3 , October 1990 , pp. 259 - 265
Copyright
Copyright © Cambridge University Press 1990

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