Class IV alcohol/retinol dehydrogenase localization in epidermal basal layer: Potential site of retinoic acid synthesis during skin development

Haselbeck, Robert J.; Ang, Hwee Luan; Duester, Gregg

doi:10.1002/(sici)1097-0177(199704)208:4<447::aid-aja1>3.0.co;2-i

Cited by 40 publications

(14 citation statements)

References 49 publications

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“…Xenopus ADH4 expression in adult tissues is found in the upper digestive tract (stomach and esophagus) and skin but is absent from the lower digestive tract (small and large intestines), liver, and mesonephros. This pattern exactly matches the adult tissue distribution for mouse ADH4 determined previously (Zgombic-Knight et al, 1995a;Ang et al, 1996b;Haselbeck and Duester, 1997;Haselbeck et al, 1997b). In addition, Xenopus ADH4 expression is localized specifically to the gastric mucosa by in situ hybridization, a property shared with mouse ADH4 (Ang et al, 1996b;Haselbeck and Duester, 1997).…”

Section: Discussionsupporting

confidence: 86%

“…In addition, Xenopus ADH4 expression is localized specifically to the gastric mucosa by in situ hybridization, a property shared with mouse ADH4 (Ang et al, 1996b;Haselbeck and Duester, 1997). On the other hand, Xenopus ADH1 expression matches that of mouse ADH1, being found in the lower digestive tract (small and large intestines), liver, and mesonephros but not in the upper digestive tract (stomach and esophagus) and skin (Zgombic-Knight et al, 1995a;Ang et al, 1996b;Haselbeck and Duester, 1997;Haselbeck et al, 1997b). Also, Xenopus ADH1 expression is first detected during embryogenesis in the developing genitourinary tract (pronephros and pronephric duct), thus conserved with mouse ADH1 which is also first expressed during embryogenesis in the developing genitourinary tract (mesonephros) (Ang et al, 1996a).…”

Section: Discussionmentioning

confidence: 99%

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

1998

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Section: Discussionsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 99%

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

1998

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“…These findings indicate that ADH3 contributes significantly to RA generation in vivo, and under these conditions makes a larger contribution than ADH4 perhaps because of its ubiquitous expression compared with the much more limited expression pattern of ADH4. ADH4 is not expressed in liver or intestine and instead is limited to epithelia of the stomach, esophagus, skin, adrenal, and reproductive tract (31,(39)(40)(41). The observed major role of ADH1 in metabolism of a dose of retinol to RA is consistent with its expression at very high levels in liver, intestine, and several other organs (31).…”

Section: ϫ/ϫmentioning

confidence: 55%

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

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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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“…These results suggest that LECs generate RA in the presence of LEDGF. It is reported that RA synthesis occurs locally in many epithelial cell types throughout the body (13). Genetic studies provide evidence that adh1-, adh3-, and adh4-null mice have defects in ethanol clearance, formaldehyde toxicity, and metabolism of retinol to RA (4).…”

Section: Discussionmentioning

confidence: 99%

LEDGF regulation of alcohol and aldehyde dehydrogenases in lens epithelial cells: stimulation of retinoic acid production and protection from ethanol toxicity

Fatma

Kubo

Chylack

et al. 2004

American Journal of Physiology-Cell Physiology

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Retinoic acid (RA) is required for the normal growth and maintenance of many cell types, including lens epithelial cells (LECs). Alcohol (ADH) and aldehyde (ALDH) dehydrogenases are implicated in cellular detoxification and conversion of vitamin A to RA. Lens epithelium-derived growth factor (LEDGF) provides cellular protection against stress by transactivating stress-associated genes. Here we show evidence that LEDGF binds and transactivates heat shock (nGAAn) and stress response (A/TGGGGA/T) elements in the promoters of ADH1, ADH4, and retinaldehyde 2 (RALDH2) genes. Electrophoretic mobility and supershift assays disclosed specific binding of LEDGF to nGAAn and A/TGGGGA/T elements in these gene promoters. Transfection experiments in LECs with promoters linked to a chloramphenicol acetyltransferase (CAT) reporter gene along with LEDGF cDNA revealed higher CAT activity. RT-PCR results confirmed that LECs overexpressing LEDGF contained increased levels of ADH1, ADH4, and RALDH2 mRNA. Notably, LECs displayed higher LEDGF mRNA and protein expression during ethanol stress. Cells overexpressing LEDGF typically exhibited elevated RA levels and survived well during ethanol stress. The present findings indicate that LEDGF is one of the transcriptional activators of these genes that facilitates cellular protection against ethanol stress and plays a role in RA production.

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Class IV alcohol/retinol dehydrogenase localization in epidermal basal layer: Potential site of retinoic acid synthesis during skin development

Cited by 40 publications

References 49 publications

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

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

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

LEDGF regulation of alcohol and aldehyde dehydrogenases in lens epithelial cells: stimulation of retinoic acid production and protection from ethanol toxicity

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