Human dehydrogenase/reductase (SDR family) member 8 (DHRS8): a description and evaluation of its biochemical properties

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00179906%3A_____%2F16%3A10326442" target="_blank" >RIV/00179906:_____/16:10326442 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11150/16:10326442 RIV/00216208:11160/16:10326442

Result on the web

<a href="http://link.springer.com/article/10.1007/s11010-015-2566-0" target="_blank" >http://link.springer.com/article/10.1007/s11010-015-2566-0</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11010-015-2566-0" target="_blank" >10.1007/s11010-015-2566-0</a>

Result language

angličtina

Original language name

Human dehydrogenase/reductase (SDR family) member 8 (DHRS8): a description and evaluation of its biochemical properties

Original language description

Dehydrogenase/reductase (SDR family) member 8 (DHRS8, SDR16C2) belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, one of the largest enzyme groups. In addition to the well-known members which participate in the metabolism of important eobiotics and xenobiotics, this superfamily contains many poorly characterized proteins. DHRS8 is a member of the Multisubstrate NADP(H)-dependent SDR16C family, which generally contains insufficiently described enzymes. Despite the limited knowledge about DHRS8, preliminary indicators have emerged regarding its significant function in the modulation of steroidal activity, at least in the case of 3 alpha-adiol, lipid metabolism and detoxification. The aim of this study was to describe additional biochemical properties of DHRS8 and to unify knowledge about this enzyme. The DHRS8 was prepared in recombinant form and its membrane topology in the endoplasmic reticulum as an integral protein with cytosolic orientation was demonstrated. The enzyme participates in the NAD(+)-dependent oxidation of steroid hormones as beta-estradiol and testosterone in vitro; apparent K-m and V-max values were 39.86 A mu M and 0.80 nmol x mg(-1) x min(-1) for beta-estradiol and 1207.29 A mu M and 3.45 nmol x mg(-1) x min(-1) for testosterone. Moreover, synthetic steroids (methyltestosterone and nandrolone) used as anabolics as well as all-trans-retinol were for the first time identified as substrates of DHRS8. This knowledge of its in vitro activity together with a newly described expression pattern at the protein level in tissues involved in steroidogenesis (adrenal gland and testis) and detoxification (liver, lung, kidney and small intestine) could suggest a potential role of DHRS8 in vivo.

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

Molecular and Cellular Biochemistry

ISSN

0300-8177

e-ISSN

—

Volume of the periodical

411

Issue of the periodical within the volume

1-2

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

8

Pages from-to

35-42

UT code for WoS article

000369808600004

EID of the result in the Scopus database

2-s2.0-84957432356