Evidence That the Human Gene for Prostate Short-chain Dehydrogenase/Reductase (PSDR1) Encodes a Novel Retinal Reductase (RalR1)

Kedishvili, Natalia Y.; Чумакова, О. В.; Chetyrkin, Sergei V.; Belyaeva, Olga V.; Лапшина, Е. А.; Lin, Daniel W.; Matsumura, Masazumi; Nelson, Peter S.

doi:10.1074/jbc.m202588200

Cited by 63 publications

(76 citation statements)

References 46 publications

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“…This study and others (3)(4)(5)7) showed that mRDH11 is expressed in ocular and extraocular tissues, suggesting multiple functions. A possible role of mRDH11 in intestinal absorption of ␤-carotene has been discussed (7).…”

Section: Discussionmentioning

confidence: 99%

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Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo

Kasus‐Jacobi

Ou²,

Birch

et al. 2005

Journal of Biological Chemistry

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We previously cloned mouse RDH11 (mRDH11) as a gene regulated by the transcription factor sterol regulatory element-binding proteins and showed that it is a retinol dehydrogenase expressed in non-ocular tissues such as the liver and testis and in the retina We show by immunoblot analysis that mRDH11 is associated with retinal membranes purified from a non-outer segment fraction of the retina. No obvious retinal defect was found during development and aging of RDH11-deficient mice. The functional consequences of mRDH11 disruption were investigated by electroretinography. Dark adaptation was delayed by a factor of 2.5-3 compared with wild-type mice. However, the kinetics of 11-cis-retinal recycling during dark adaptation was not affected, suggesting that mRDH11 is not involved in the visual cycle. We propose that mRDH11 disruption affects retinoid metabolism in photoreceptor inner segments and delays the kinetics of dark adaptation through modulation of calcium homeostasis.

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Section: Discussionmentioning

confidence: 99%

“…The reverse reaction, oxidation of all-trans-retinol, is not catalyzed by mRDH11 (3). hRDH11 is able to catalyze this reaction, however, at a lower catalytic efficiency compared with all-trans-retinal reduction (5,7). In addition to retinaldehydes, mRDH11 catalyzes the reduction of short-chain aldehydes such as nonanal with K m ϭ 30 M (3).…”

mentioning

confidence: 99%

Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo

Kasus‐Jacobi

Ou²,

Birch

et al. 2005

Journal of Biological Chemistry

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“…DHRS3 is a known retinoic acid-inducible gene (Cerignoli et al, 2002) that encodes a retinal reductase (Kedishvili et al, 2002). Retinol regeneration by DHRS3 depends on the presence of the cellular retinoic acid binding protein CRABP2 (Cerignoli et al, 2002), a gene that was concordantly upregulated in ATRA-treated Wilms tumor cells.…”

Section: Retinoid Signalingmentioning

confidence: 99%

All-trans retinoic acid treatment of Wilms tumor cells reverses expression of genes associated with high risk and relapse in vivo

Zirn

Samans

Spangenberg³

et al. 2005

Oncogene

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“…However, because of the high concentrations of RBP2 in the intestine, it was suggested that the microsomal enzyme that utilizes retinal-RBP2 is likely a more physiologically relevant enzyme. From the literature, we have identified a microsomal retinal reductase RalR1 that is expressed in intestine and uses retinal in the presence of high concentrations of RBP1 [28]. However, the effects of RBP2, the major intracellular retinolbinding protein present in the intestine, on this enzyme had not been studied.…”

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confidence: 99%

In vitro and in vivo characterization of retinoid synthesis from β-carotene

Fierce

Vieira

Piantedosi

et al. 2008

Archives of Biochemistry and Biophysics

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Retinoids are indispensable for the health of mammals, which cannot synthesize retinoids de novo. Retinoids are derived from dietary provitamin A carotenoids, like β-carotene, through the actions β-carotene 15,15′ monooxygenase (BCMO1). As the substrates for retinoid metabolizing enzymes are water insoluble, they must be transported intracellularly bound to cellular retinol-binding proteins. Our studies suggest that cellular retinol binding protein, type I (RBP1) acts as an intracellular sensor of retinoid status that, when present as apo-RBP1, stimulates BCMO1 activity and the conversion of carotenoids to retinoids. Cellular retinol binding protein, type II (RBP2), which is 56% identical to RBP1 does not influence BCMO1 activity. Studies of mice lacking BCMO1 demonstrate that BCMO1 is responsible for metabolically limiting the amount of intact β-carotene that can be absorbed by mice from their diet. Our studies provide new insights into the regulation of BCMO1 activity and the physiological role of BCMO1 in living organisms. Keywordsβ-carotene; cleavage; β-carotene 15; 15′ monooxygenase; retinoid; metabolism; cellular retinol binding protein Retinoids (vitamin A, its natural metabolites and synthetic analogs) are required for survival of mammals and are needed to support vision, normal cell differentiation and proliferation, embryonic development, normal immune function and reproduction [1]. Aside from in vision, all of the essential actions of retinoids within the body are thought to involve the transcriptional activity of retinoic acid [1]. Retinoic acid is a potent transcriptional regulator whose effects are mediated by two families of nuclear receptors, the retinoic acid receptors (RARs) and the retinoid X receptors (RXRs) [2][3][4]. When retinoic acid is not available, RAR/RXR heterodimers bind to retinoic acid response elements in promoter of genes and form complexes with transcriptional corepressors resulting in chromatin condensation and transcriptional silencing. In the presence of retinoic acid, corepressors are released from the RAR/RXR heterodimer which is now free to recruit and bind coactivators resulting in chromatin *Corresponding author: Jisun Paik, Department of Comparative Medicine, Raitt Hall, 324, Seattle, WA 98195. Phone: 206-221-2682; Fax: 206-685-1696; E-mail: jpaik@u.washington.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript decondensation and transcriptional activation. In excess of 500 genes may be responsive to retinoic acid [5].Since ani...

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Evidence That the Human Gene for Prostate Short-chain Dehydrogenase/Reductase (PSDR1) Encodes a Novel Retinal Reductase (RalR1)

Cited by 63 publications

References 46 publications

Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo

Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo

All-trans retinoic acid treatment of Wilms tumor cells reverses expression of genes associated with high risk and relapse in vivo

In vitro and in vivo characterization of retinoid synthesis from β-carotene

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