scholarly journals Isatin-induced increase in the affinity of human ferrochelatase and adrenodoxin reductase interaction

2017 ◽  
Vol 26 (12) ◽  
pp. 2458-2462 ◽  
Author(s):  
Pavel Ershov ◽  
Yuri Mezentsev ◽  
Andrey Gilep ◽  
Sergey Usanov ◽  
Olga Buneeva ◽  
...  
Keyword(s):  
Adrenodoxin Reductase

scholarly journals cAMP post-transcriptionally diminishes the abundance of adrenodoxin reductase mRNA.

1992 ◽  
Vol 89 (9) ◽  
pp. 4099-4103 ◽  
Author(s):  
S. T. Brentano ◽  
S. M. Black ◽  
D. Lin ◽  
W. L. Miller
Keyword(s):  
Reductase Mrna ◽  
Adrenodoxin Reductase

The dare gene: steroid hormone production, olfactory behavior, and neural degeneration in Drosophila

Development ◽  
1999 ◽  
Vol 126 (20) ◽  
pp. 4591-4602 ◽  
Author(s):  
M.R. Freeman ◽  
A. Dobritsa ◽  
P. Gaines ◽  
W.A. Segraves ◽  
J.R. Carlson
Keyword(s):  
Nervous System ◽  
Steroid Hormones ◽  
Steroid Hormone ◽  
Larval Instar ◽  
Hormone Production ◽  
Ring Gland ◽  
Olfactory Stimuli ◽  
Steroid Hormone Signaling ◽  
Adrenodoxin Reductase ◽  
Strength Result

Steroid hormones mediate a wide variety of developmental and physiological events in insects, yet little is known about the genetics of insect steroid hormone biosynthesis. Here we describe the Drosophila dare gene, which encodes adrenodoxin reductase (AR). In mammals, AR plays a key role in the synthesis of all steroid hormones. Null mutants of dare undergo developmental arrest during the second larval instar or at the second larval molt, and dare mutants of intermediate severity are delayed in pupariation. These defects are rescued to a high degree by feeding mutant larvae the insect steroid hormone 20-hydroxyecdysone. These data, together with the abundant expression of dare in the two principal steroid biosynthetic tissues, the ring gland and the ovary, argue strongly for a role of dare in steroid hormone production. dare is the first Drosophila gene shown to encode a defined component of the steroid hormone biosynthetic cascade and therefore provides a new tool for the analysis of steroid hormone function. We have explored its role in the adult nervous system and found two striking phenotypes not previously described in mutants affected in steroid hormone signaling. First, we show that mild reductions of dare expression cause abnormal behavioral responses to olfactory stimuli, indicating a requirement for dare in sensory behavior. Then we show that dare mutations of intermediate strength result in rapid, widespread degeneration of the adult nervous system.

scholarly journals Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

FEBS Letters ◽  
1999 ◽  
Vol 443 (2) ◽  
pp. 167-169 ◽  
Author(s):  
Clemens Vonrhein ◽  
Ulrich Schmidt ◽  
Gabriele A Ziegler ◽  
Susann Schweiger ◽  
Israel Hanukoglu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Adrenodoxin Reductase

Inhibition of aldosterone biosynthesis by staurosporine

2005 ◽  
Vol 386 (7) ◽  
pp. 663-669 ◽  
Author(s):  
Matthias Bureik ◽  
Alexander Mion ◽  
Christopher J. Kenyon ◽  
Rita Bernhardt
Keyword(s):  
Kinase Inhibitor ◽  
Therapeutic Potential ◽  
Hypotensive Effect ◽  
Cytochrome P450 Enzyme ◽  
Aldosterone Synthase ◽  
Kinase C ◽  
Steroid Hydroxylase ◽  
P450 Enzyme ◽  
Adrenodoxin Reductase

Abstract Staurosporine (STS) is a very potent broad-range kinase inhibitor, and its antiproliferative properties made it a lead compound for protein kinase C (PKC) inhibitors with therapeutic potential. Because STS also causes hypotension, we investigated in this study whether it directly interferes with the terminal steps of aldosterone biosynthesis; these are catalysed by a mitochondrial steroid hydroxylase system consisting of adrenodoxin reductase, adrenodoxin, and the cytochrome P450 enzyme hCYP11B2 (aldosterone synthase). Here we demonstrate that nanomolar concentrations of STS significantly reduced aldosterone synthase activity in transiently transfected COS-1 cells and in stably transfected V79MZh11B2 cells (IC50=11 nM). However, STS did not inhibit bovine aldosterone synthase in a reconstituted steroid hydroxylation assay. In transiently transfected COS-1 cells, the protein level of adrenodoxin (but not that of adrenodoxin reductase or of hCYP11B2) was significantly reduced after treatment with 2 nM STS. Finally, we show that STS treatment (1 μg/day) of mice reduced their aldosterone/renin ratio by almost 50% (p=0.015). To the best of our knowledge, this is the first report of a direct in vivo effect of STS on the renin-angiotensin-aldosterone system. We conclude (i) that the hypotensive effect of staurosporine is at least partly due to inhibition of aldosterone biosynthesis via adrenodoxin depletion, and (ii) that aldosterone biosynthesis can be regulated in vivo at the level of adrenodoxin availability.

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