Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)

Dasmahapatra, Asok K.; Doucet, Herman L.; Bhattacharyya, Champa; Carvan, Michael J.

doi:10.1006/bbrc.2001.5511

Cited by 38 publications

(26 citation statements)

References 15 publications

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“…Indeed, from our data, the widespread expression during zebrafish development was not ubiquitous, but consistent with spatio-temporal regulation (Dasmahapatra et al, 2001;Cañ estro et al, 2003). At the subcellular level, in contrast to other ADHs of strictly cytosolic localization, ADH3 has also been reported in the cell nucleus (Iborra et al, 1992;Fernández et al, 2003), presumably related to DNA protection.…”

Section: Evolution Of the Mdr-adh Familysupporting

confidence: 85%

Merging protein, gene and genomic data: the evolution of the MDR-ADH family

Gonzàlez‐Duarte

Albalat

2005

Heredity

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Multiple members of the MDR-ADH (MDR: Medium-chain dehydrogenases/reductases; ADH: alcohol dehydrogenase) family are found in vertebrates, although the enzymes that belong to this family have also been isolated from bacteria, yeast, plant and animal sources. Initial understanding of the physiological roles and evolution of the family relied on biochemical studies, protein alignments and protein structure comparisons. Subsequently, studies at the genetic level yielded new information: the expression pattern, exon-intron distribution, in silico-derived protein sequences and murine knockout phenotypes. More recently, genomic and EST databases have revealed new family members and the chromosomal location and position in the cluster of both the first and new forms. The data now available provide a comprehensive scenario, from which a reliable picture of the evolutionary history of this family can be made.

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Section: Evolution Of the Mdr-adh Familysupporting

confidence: 85%

Merging protein, gene and genomic data: the evolution of the MDR-ADH family

Gonzàlez‐Duarte

Albalat

2005

Heredity

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“…First, several alcohol dehydrogenases have been identified in zebrafish, adh5, adh8a , and adh8b , all three of which can process ethanol (Dasmahapatra, Doucet, Bhattacharyya, & Carvan, 2001; Reimers, Hahn, & Tanguay, 2004). In addition, other enzymes such as the cytochrome P450, Cyp2E1, may play a role in ethanol metabolism (Passeri, Cinaroglu, Gao, & Sadler, 2009).…”

Section: Discussionmentioning

confidence: 99%

Developmental age strengthens barriers to ethanol accumulation in zebrafish

Lovely¹,

Nobles²,

Eberhart³

2014

Alcohol

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Fetal Alcohol Spectrum Disorders (FASD) describes a wide range of phenotypic defects affecting facial and neurological development associated with ethanol teratogenicity. It affects approximately 1 in 100 children born in the United States each year. Genetic predisposition along with timing and dosage of ethanol exposure are critical in understanding the prevalence and variability of FASD. The zebrafish attributes of external fertilization, genetic tractability, and high fecundity make it a powerful tool for FASD studies. However, a lack of consensus of ethanol treatment paradigms has limited the interpretation of these various studies. Here we address this concern by examining ethanol tissue concentrations across timing and genetic background. We utilize headspace gas chromatography to determine ethanol concentration in the AB, fli1:EGFP, and Tu backgrounds. In addition, we treated these embryos with ethanol over two different developmental time windows, 6–24 hours post fertilization (hpf) and 24–48 hpf. Our analysis demonstrates that embryos rapidly equilibrate to a sub-media level of ethanol. Embryos then maintain this level of ethanol for the duration of exposure. The ethanol tissue concentration level is independent of genetic background, but is timing-dependent. Embryos exposed from 6–24 hpf were 2.7–4.2-fold lower than media levels, while embryos were 5.7–6.2-fold lower at 48 hpf. This suggests that embryos strengthen one or more barriers to ethanol as they develop. In addition, both the embryo and, to a lesser extent, the chorion, surrounding the embryo are barriers to ethanol. Overall, this work will help tighten ethanol treatment regimens and strengthen zebrafish as a model of FASD.

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“…Expression of amphibian ADH3 is detected in every stage and tissue studied, although it is more abundant in some organs such as the ovary, suggesting that oocytes may store large amounts of maternal ADH3 for its later use during the embryonic development. The maternal origin of ADH3 mRNA has been previously described in Drosophila [74] and zebrafish [75] embryos.…”

Section: Discussionmentioning

confidence: 99%

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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Developmental Expression of Alcohol Dehydrogenase (ADH3) in Zebrafish (Danio rerio)

Cited by 38 publications

References 15 publications

Merging protein, gene and genomic data: the evolution of the MDR-ADH family

Merging protein, gene and genomic data: the evolution of the MDR-ADH family

Developmental age strengthens barriers to ethanol accumulation in zebrafish

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

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