Alcohol dehydrogenases inXenopus development: Conserved expression of ADH1 and ADH4 in epithelial retinoid target tissues

Hoffmann, Ines; Ang, Hwee Luan; Duester, Gregg

doi:10.1002/(sici)1097-0177(199811)213:3<261::aid-aja3>3.0.co;2-v

Cited by 16 publications

(7 citation statements)

References 51 publications

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“…Because evolutionary data suggest that ADH1 diverged from ADH3 during the advent of bony fishes (32,46), and that ADH4 diverged from ADH1 during emergence of amphibians (47,48), ADH1 and ADH4 cannot be responsible for RA synthesis in present-day primitive fishes and their ancestors where retinoid signaling is believed to have originated (1). Instead, our data indicate that ADH3 initially evolved to perform this function, and its relatively low activity with retinol may have actually been advantageous in that it would have spared retinol, particularly important during VAD commonly encountered in the wild, while still making sufficient RA for development.…”

mentioning

confidence: 76%

Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3

Molotkov

Fan

Deltour

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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Influence of vitamin A (retinol) on growth depends on its sequential oxidation to retinal and then to retinoic acid (RA), producing a ligand for RA receptors essential in development of specific tissues. Genetic studies have revealed that aldehyde dehydrogenases function as tissue-specific catalysts for oxidation of retinal to RA. However, enzymes catalyzing the first step of RA synthesis, oxidation of retinol to retinal, remain unclear because none of the present candidate enzymes have expression patterns that fully overlap with those of aldehyde dehydrogenases during development. Here, we provide genetic evidence that alcohol dehydrogenase (ADH) performs this function by demonstrating a role for Adh3, a ubiquitously expressed form. Adh3 null mutant mice exhibit reduced RA generation in vivo, growth deficiency that can be rescued by retinol supplementation, and completely penetrant postnatal lethality during vitamin A deficiency. ADH3 was also shown to have in vitro retinol oxidation activity. Unlike the second step, the first step of RA synthesis is not tissue-restricted because it is catalyzed by ADH3, a ubiquitous enzyme having an ancient origin.

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mentioning

confidence: 76%

Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3

Molotkov

Fan

Deltour

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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130

123

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“…Expression pattern of amphibian class I in adult and embryonic tissues resembles that of other vertebrates, and transcripts of ADH1B are abundant in the developing tadpole (Table 3 and [22]).…”

Section: Discussionmentioning

confidence: 99%

“…Substrate preferences may be large substrates rather than ethanol, but probably not steroids. Northern blot studies detect ADH9 transcripts in adult stomach, esophagus and skin, while discard the expression of the enzyme at embryonic stages (Figure 1 and [22]). Colocalization with ADH8, in spite of their sequence divergence and different cofactor specificity, may obey to the common regulatory elements found in their gene promoters, and it is consistent with the adjacent chromosomal location of their genes.…”

Section: Discussionmentioning

confidence: 99%

“…For X. laevis , results of expression experiments from our group (in bold) and other sources, are also included. 1 Partial sequence, probably another allele of this gene; 2 Hoffmann et al [22]; 3 Partial sequence, containing frameshift mutations; n.a. : not available.…”

Section: Methodsmentioning

confidence: 99%

“…The cloning of the cDNA of R. perezi ADH8 [15] allowed to perform mutagenesis studies on coenzyme specificity [19] and to obtain the crystal structure of the enzyme [20,21]. Partial cDNAs of X. laevis ADH1 and an ADH4-like form were cloned and used for expression analysis in embryonic and adult tissues [22]. Later, two reviews on MDR-ADH evolution [4,23], which included genomic data, provided some partial information on the amphibian ADH system.…”

Section: Introductionmentioning

confidence: 99%

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The Xenopusalcohol dehydrogenase gene family: characterization and comparative analysis incorporating amphibian and reptilian genomes

et al. 2014

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BackgroundThe alcohol dehydrogenase (ADH) gene family uniquely illustrates the concept of enzymogenesis. In vertebrates, tandem duplications gave rise to a multiplicity of forms that have been classified in eight enzyme classes, according to primary structure and function. Some of these classes appear to be exclusive of particular organisms, such as the frog ADH8, a unique NADP+-dependent ADH enzyme. This work describes the ADH system of Xenopus, as a model organism, and explores the first amphibian and reptilian genomes released in order to contribute towards a better knowledge of the vertebrate ADH gene family.ResultsXenopus cDNA and genomic sequences along with expressed sequence tags (ESTs) were used in phylogenetic analyses and structure-function correlations of amphibian ADHs. Novel ADH sequences identified in the genomes of Anolis carolinensis (anole lizard) and Pelodiscus sinensis (turtle) were also included in these studies. Tissue and stage-specific libraries provided expression data, which has been supported by mRNA detection in Xenopus laevis tissues and regulatory elements in promoter regions. Exon-intron boundaries, position and orientation of ADH genes were deduced from the amphibian and reptilian genome assemblies, thus revealing syntenic regions and gene rearrangements with respect to the human genome. Our results reveal the high complexity of the ADH system in amphibians, with eleven genes, coding for seven enzyme classes in Xenopus tropicalis. Frogs possess the amphibian-specific ADH8 and the novel ADH1-derived forms ADH9 and ADH10. In addition, they exhibit ADH1, ADH2, ADH3 and ADH7, also present in reptiles and birds. Class-specific signatures have been assigned to ADH7, and ancestral ADH2 is predicted to be a mixed-class as the ostrich enzyme, structurally close to mammalian ADH2 but with class-I kinetic properties. Remarkably, many ADH1 and ADH7 forms are observed in the lizard, probably due to lineage-specific duplications. ADH4 is not present in amphibians and reptiles.ConclusionsThe study of the ancient forms of ADH2 and ADH7 sheds new light on the evolution of the vertebrate ADH system, whereas the special features showed by the novel forms point to the acquisition of new functions following the ADH gene family expansion which occurred in amphibians.

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Environmentally induced limb malformations in mink frogs (Rana septentrionalis)

Gardiner

Hoppe

1999

J. Exp. Zool.

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Alcohol dehydrogenases inXenopus development: Conserved expression of ADH1 and ADH4 in epithelial retinoid target tissues

Cited by 16 publications

References 51 publications

Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3

Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3

The Xenopusalcohol dehydrogenase gene family: characterization and comparative analysis incorporating amphibian and reptilian genomes

Environmentally induced limb malformations in mink frogs (Rana septentrionalis)

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