Disease relevance of RDH11

• This study identified a novel gene that we have designated prostate short-chain dehydrogenase/reductase 1 (PSDR1), that exhibits increased expression on exposure to androgens in the LNCaP prostate cancer cell line [1].

High impact information on RDH11

• 3. In situ hybridization localizes PSDR1 expression to normal and neoplastic prostate epithelium [1].
• We used a radiation-hybrid panel to map the PSDR1 gene to chromosome 14q23-24 [1].
• Cloning and analysis of the putative PSDR1 promoter region identified a potential androgen-response element [1].
• RDH11-14 fill the gap in our understanding of 11-cis-retinal and all-trans-retinal transformations in photoreceptor (RDH12) and retinal pigment epithelial cells (RDH11) [2].
• As shown by immunostaining of human prostate and LNCaP cells with monoclonal anti-RalR1 antibodies, the enzyme is highly expressed in the epithelial cell layer of human prostate and localizes to the endoplasmic reticulum [3].

Biological context of RDH11

• The enzymatic properties and expression pattern of RalR1 in prostate epithelium suggest that it might play a role in the regulation of retinoid homeostasis in human prostate [3].
• The coenzyme and substrate specificity of ADH8, that has 50-65% sequence identity with vertebrate NAD(H)-dependent ADHs, suggest a role in aldehyde reduction probably as a retinal reductase [4].

Anatomical context of RDH11

• In the present study, we purified the recombinant enzyme from the microsomal membranes of insect Sf9 cells, determined its catalytic efficiency for the reduction of retinal and the oxidation of retinol, established its transmembrane topology, and examined the distribution of RalR1 in human tissues and cell lines [5].
• Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues [6].
• Psdr1 was cloned as a 3.2 kbp transcript from mouse testis cDNA based on the sequence of the recently described androgen-regulated human PSDR1 gene (Cancer Res. 61 (2001) 1611) [7].

Associations of RDH11 with chemical compounds

• ADHs appear to be more effective retinol dehydrogenases than SDRs because of their higher kcat values, whereas RDH11 and AKR1B10 are efficient retinaldehyde reductases [8].
• Prostate short-chain dehydrogenase reductase 1 (PSDR1): a new member of the short-chain steroid dehydrogenase/reductase family highly expressed in normal and neoplastic prostate epithelium [1].
• We demonstrate that RalR1 exhibits an oxidoreductive catalytic activity toward retinoids, but not steroids, with at least an 800-fold lower apparent K(m) values for NADP+ and NADPH versus NAD+ and NADH as cofactors [3].

Other interactions of RDH11

• Importantly, RalR1 reduces all-trans-retinal in the presence of a 10-fold molar excess of cellular retinol-binding protein type I, which is believed to sequester all-trans-retinal from nonspecific enzymes [3].
• CONCLUSIONS: Scald injuries are now the major cause of burns in those with epilepsy, and the proportion of such patients admitted to a regional burns unit has reduced [9].

Analytical, diagnostic and therapeutic context of RDH11

• Western blot analysis revealed that RalR1 is expressed in a wide variety of normal human tissues and cancer cell lines [5].

References