The Journal of Steroid Biochemistry and Molecular Biology
PaperCloning, sequencing and tissue-distribution of mouse 11β-hydroxysteroid dehydrogenase-1 cDNA
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Cited by (65)
The cortisol-activating enzyme 11β-hydroxysteroid dehydrogenase type 1 in skeletal muscle in the pathogenesis of the metabolic syndrome
2017, Journal of Steroid Biochemistry and Molecular BiologyCitation Excerpt :11β-HSD1 has shown both reductase and dehydrogenase activities in tissues homogenates, but displays predominantly reductase activity in most intact cells and in vivo due to its co-localization with H6PDH [5]. It is widely expressed with its highest levels in liver [6,7], followed by adipose tissue [8,9], vasculature [10], ovary [11], testis (human and rat, but not mouse) [7,12,13], brain [6,14,15], uterus [16], immune and inflammatory cells [17], skeletal muscle [18] and heart [10]. The reverse reaction is mediated by 11β-HSD type 2 (11β-HSD2), thereby protecting the mineralocorticoid receptor from inappropriate activation via cortisol by inactivating it to cortisone.
Prenatal corticosterone exposure programs growth, behavior, reproductive function and genes in the chicken
2016, Asian Pacific Journal of ReproductionDifferences in egg deposition of corticosterone and embryonic expression of corticosterone metabolic enzymes between slow and fast growing broiler chickens
2013, Comparative Biochemistry and Physiology - A Molecular and Integrative PhysiologyCitation Excerpt :11β-Hydroxysteroid dehydrogenase type 1 (11β-HSD1) activates, whereas 11β-HSD2 inactivates GCs (Diederich et al., 1998; Stewart and Krozowski, 1999; Harris et al., 2001; Holmes et al., 2003; Holmes and Seckl, 2006). In mammals, 11β-HSD1 is expressed predominantly in the liver, kidney and lung (Rajan et al., 1995), while 11β-HSD2 mainly exists in the kidney, colon and placenta (Albiston et al., 1994). In birds, 20α-hydroxystreroid dehydrogenase (20-HSD) is an abundantly and ubiquitously expressed enzyme, which transforms GCs to inactive 20-dihydrocorticosterone (Kucka et al., 2006).
11β-Hydroxysteroid dehydrogenases and the brain: From zero to hero, a decade of progress
2011, Frontiers in NeuroendocrinologyCitation Excerpt :This was distinct from the enzyme described by Monder, being a high affinity (low nM Km) exclusive 11β-dehydrogenase which used NAD rather than NADP(H) as co-substrate. In 1994, Krozowski’s group [6] isolated a cDNA encoding this ‘renal’ 11β-HSD from human kidney, White and colleagues found the same enzyme in sheep kidney [2], the rodent homologues were soon cloned [214] and an identical enzyme purified and its encoding cDNA cloned in the human placenta [27]. The new enzyme was called 11β-HSD type 2 to distinguish it from Monder’s 11β-HSD type 1 (Fig. 1).
2 Inhibitors of 11β-Hydroxysteroid Dehydrogenase Type 1
2008, Progress in Medicinal ChemistryCitation Excerpt :In cell-free systems, 11β-HSD1 behaves mainly as a dehydrogenase with no reductase activity being detected in the purified preparation. Subsequently, cDNAs and protein sequences were published for the human [33], mouse [34], squirrel monkey [35], sheep [36], rabbit [32], pig, cow and guinea pig [37, 38] 11β-HSD1. Human liver 11β-HSD1 was eventually purified in an active form and was postulated to exist as a dimer [39].
Leydig cells from neonatal pig testis abundantly express 11β-hydroxysteroid dehydrogenase (11β-HSD) type 2 and effectively inactivate cortisol to cortisone
2008, Journal of Steroid Biochemistry and Molecular Biology