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Tokarz, J. ; Lintelmann, J. ; Möller, G. ; Adamski, J.

Substrate multispecificity among 20 beta-hydroxysteroid dehydrogenase type 2 members.

Mol. Cell. Endocrinol. 510:110822 (2020)
Postprint Forschungsdaten DOI PMC
Open Access Green
Steroids regulate many physiological processes. Hydroxysteroid dehydrogenases (HSDs) modulate the levels of steroids in pre- and post-receptor metabolism. The subfamily of 20 beta-HSD type 2 currently comprises six members from six different species. The zebrafish ortholog converts cortisone to 20 beta-dihydrocortisone and is involved in the catabolism of the stress hormone cortisol. Here, we elucidated the substrate preferences of all 20 beta-HSD type 2 enzymes towards a selected panel of steroids. For quantification of the substrates and their respective 20 beta-reduced products, we first developed and validated a liquid chromatography-mass spectrometry based method. Applying this method to activity assays with recombinantly expressed enzymes, our findings indicate that the 20 beta-HSD type 2 enzymes catalyze the 20 beta-reduction of a plethora of steroids of the glucocorticoid biosynthesis pathway. The observed multispecificity among the homologous 20 beta-HSD type 2 enzymes implies different physiological roles in different species.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter 20β-reduction ; Catabolism ; Cortisone ; Hsd20b2 ; Hydroxysteroid Dehydrogenase ; Lc-ms; Cortisol Metabolites; Oocyte Maturation; Human Serum; Lc-ms/ms; Identification; Progesterone; Expression; Zebrafish; Symmetry; Steroids
ISSN (print) / ISBN 0303-7207
e-ISSN 1872-8057
Zeitschrift Molecular and Cellular Endocrinology
Quellenangaben Band: 510, Heft: , Seiten: , Artikelnummer: 110822 Supplement: ,
Verlag Elsevier
Verlagsort Shannon
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Molekulare Endokrinologie und Metabolismus (MEM)