Human DHRS7, promising enzyme in metabolism of steroids and retinoids?

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00179906%3A_____%2F16%3A10326443" target="_blank" >RIV/00179906:_____/16:10326443 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11150/16:10326443 RIV/00216208:11160/16:10326443

Result on the web

<a href="http://www.sciencedirect.com/science/article/pii/S0960076015300984" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0960076015300984</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jsbmb.2015.09.041" target="_blank" >10.1016/j.jsbmb.2015.09.041</a>

Result language

angličtina

Original language name

Human DHRS7, promising enzyme in metabolism of steroids and retinoids?

Original language description

The metabolism of steroids and retinoids has been studied in detail for a long time, as these compounds are involved in a broad spectrum of physiological processes. Many enzymes participating in the conversion of such compounds are members of the short-chain dehydrogenase/reductase (SDR) superfamily. Despite great effort, there still remain a number of poorly characterized SDR proteins. According to various bioinformatics predictions, many of these proteins may play a role in the metabolism of steroids and retinoids. Dehydrogenase/reductase (SDR family) member 7 (DHRS7) is one such protein. In a previous study, we determined DHRS7 to be an integral membrane protein of the endoplasmic reticulum facing the lumen which has shown at least in vitro NADPH-dependent reducing activity toward several eobiotics and xenobiotics bearing a carbonyl moiety. In the present paper pure DHRS7 was used for a more detailed study of both substrate screening and an analysis of kinetics parameters of the physiologically important substrates androstene-3,17-dione, cortisone and all-trans-retinal. Expression patterns of DHRS7 at the mRNA as well as protein level were determined in a panel of various human tissue samples, a procedure that has enabled the first estimation of the possible biological function of this enzyme. DHRS7 is expressed in tissues such as prostate, adrenal glands, liver or intestine, where its activity could be well exploited. Preliminary indications show that DHRS7 exhibits dual substrate specificity recognizing not only steroids but also retinoids as potential substrates and could be important in the metabolism of these signalling molecules.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

FR - Pharmacology and apothecary chemistry

OECD FORD branch

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Project

<a href="/en/project/EE2.3.20.0235" target="_blank" >EE2.3.20.0235: Establishment of Research Team Focused on Experimental and Applied Biopharmacy</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Steroid Biochemistry and Molecular Biology

ISSN

0960-0760

e-ISSN

—

Volume of the periodical

155

Issue of the periodical within the volume

January

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

112-119

UT code for WoS article

000367424000014

EID of the result in the Scopus database

2-s2.0-84945299747