PPAR α Inhibits, Whereas PPARγ Stimulates, the Expression of 11β-Hydroxysteroid Dehydrogenase Type 2 in Human Placenta

2011 ◽  
pp. P3-160-P3-160
Author(s):  
Xin Ni ◽  
Ping He ◽  
Yuan Li ◽  
Hang Gu
Keyword(s):  
Human Placenta ◽  
Hydroxysteroid Dehydrogenase

scholarly journals Purification of 11 β-hydroxysteroid dehydrogenase type 2 from human placenta utilizing a novel affinity labelling technique

1996 ◽  
Vol 313 (3) ◽  
pp. 997-1005 ◽  
Author(s):  
Roger W. BROWN ◽  
Karen E. CHAPMAN ◽  
Parvez MURAD ◽  
Christopher R. W. EDWARDS ◽  
Jonathan R. SECKL
Keyword(s):  
Human Placenta ◽  
Pressure Control ◽  
Hydroxysteroid Dehydrogenase ◽  
Distal Nephron ◽  
Tissue Extracts ◽  
Affinity Labelling ◽  
Short Chain Alcohol ◽  
Internal Amino Acid Sequence ◽  
Dimensional Electrophoresis

11β-Hydroxysteroid dehydrogenase type 2 (11β-HSD2) efficiently inactivates potent glucocorticoid hormones (cortisol and corticosterone), leaving aldosterone unmetabolized. Abundant 11β-HSD2 activity in human placenta plays a central role in controlling fetal glucocorticoid exposure, which if excessive is harmful and may predispose to low birth weight and hypertension in adulthood. Similar 11β-HSD2 activity in the distal nephron protects mineralocorticoid receptors from glucocorticoids and appears to be important in normal blood pressure control. We have purified human placental 11β-HSD2 16000-fold, to homogeneity, and determined over 100 residues of the internal amino acid sequence. Purification was assisted by a novel technique allowing highly specific (single spot on two-dimensional electrophoresis) photoaffinity labelling of active 11β-HSD2 in crude tissue extracts by its glucocorticoid substrates. This work reveals that 11β-HSD2 is a member of the short-chain alcohol dehydrogenase superfamily (apparent monomer Mr ~40000). It is a very basic (apparent pI = 9.1) intrinsic membrane protein, requiring as yet undefined membrane constituents for full stability. Affinity chromatography and affinity labelling studies suggest that 11β-HSD2 has a compulsory ordered mechanism, with NAD+ binding first, followed by a conformational change allowing glucocorticoid binding with high affinity.

scholarly journals Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2

2015 ◽  
Vol 71 (7) ◽  
pp. 901-905 ◽  
Author(s):  
Zhong Cheng ◽  
Yao Li ◽  
Chun Sui ◽  
Xiaobo Sun ◽  
Yong Xie
Keyword(s):  
Catalytic Domain ◽  
Hydroxysteroid Dehydrogenase ◽  
Carrier Protein ◽  
Sterol Carrier Protein ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Protein Molecules

Human hydroxysteroid dehydrogenase-like protein 2 (HSDL2) is a member of the short-chain dehydrogenase/reductase (SDR) subfamily of oxidoreductases and contains an N-terminal catalytic domain and a C-termianl sterol carrier protein type 2 (SCP-2) domain. In this study, the C-terminal SCP-2 domain of human HSDL2, including residues Lys318–Arg416, was produced inEscherichia coli, purified and crystallized. X-ray diffraction data were collected to 2.10 Å resolution. The crystal belonged to the trigonal space groupP3121 (orP3221), with unit-cell parametersa=b= 70.4,c= 60.6 Å, α = β = 90, γ = 120°. Two protein molecules are present in the asymmetric unit, resulting in a Matthews coefficient of 2.16 Å3 Da−1and an approximate solvent content of 43%.

11β Hydroxysteroid Dehydrogenase Type 2 in the Adrenal Gland by Testosterone Withdrawal of Adult Rats

Folia Medica ◽  
2010 ◽  
Vol 52 (2) ◽  
Author(s):  
Yvetta Koeva ◽  
Mariana Bakalska ◽  
Elisaveta Petrova ◽  
Nina Atanassova
Keyword(s):  
Adrenal Gland ◽  
Hydroxysteroid Dehydrogenase ◽  
Adult Rats
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