Molecular identity and gene expression of aldosterone synthase cytochrome P450

doi:10.1016/J.BBRC.2005.0

Title: Molecular identity and gene expression of aldosterone synthase cytochrome P450

Full Record
Other Related Research

Abstract

11{beta}-Hydroxylase (CYP11B1) of bovine adrenal cortex produced corticosterone as well as aldosterone from 11-deoxycorticosterone in the presence of the mitochondrial P450 electron transport system. CYP11B1s of pig, sheep, and bullfrog, when expressed in COS-7 cells, also performed corticosterone and aldosterone production. Since these CYP11B1s are present in the zonae fasciculata and reticularis as well as in the zona glomerulosa, the zonal differentiation of steroid production may occur by the action of still-unidentified factor(s) on the enzyme-catalyzed successive oxygenations at C11- and C18-positions of steroid. In contrast, two cDNAs, one encoding 11{beta}-hydroxylase and the other encoding aldosterone synthase (CYP11B2), were isolated from rat, mouse, hamster, guinea pig, and human adrenals. The expression of CYP11B1 gene was regulated by cyclic AMP (cAMP)-dependent signaling, whereas that of CYP11B2 gene by calcium ion-signaling as well as cAMP-signaling. Salt-inducible protein kinase, a cAMP-induced novel protein kinase, was one of the regulators of CYP11B2 gene expression.

Authors:

Okamoto, Mitsuhiro ^[1]; Nonaka, Yasuki ^[2]; Takemori, Hiroshi ^[3]; Doi, Junko ^[4]

Laboratories for Biomolecular Networks, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871 (Japan) and Department of Molecular Physiological Chemistry, Graduate School of Medicine (H-1), Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871 (Japan). E-mail: mokamoto@mr-mbio.med.osaka-u.ac.jp
College of Nutrition, Koshien University, Takarazuka, Hyogo 665-0006 (Japan)
Department of Molecular Physiological Chemistry, Graduate School of Medicine (H-1), Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871 (Japan)
Department of Food and Nutrition, Faculty of Human Life Sciences, Senri Kinran University, Suita, Osaka 565-0873 (Japan)

Publication Date:: Fri Dec 09 00:00:00 EST 2005

OSTI Identifier:: 20793199

Resource Type:: Journal Article

Resource Relation:: Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 338; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2005.07.187; PII: S0006-291X(05)01690-6; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; ALDOSTERONE; AMP; CALCIUM IONS; CARBON 11; CARBON 18; CATTLE; CORTICOSTERONE; GENES; GUINEA PIGS; HAMSTERS; HYDROXYLASES; MICE; RATS; SHEEP; SWINE

Citation Formats


                    Okamoto, Mitsuhiro, Nonaka, Yasuki, Takemori, Hiroshi, and Doi, Junko. Molecular identity and gene expression of aldosterone synthase cytochrome P450.  United States: N. p., 2005. 
        Web.  doi:10.1016/J.BBRC.2005.0.

Copy to clipboard


                    Okamoto, Mitsuhiro, Nonaka, Yasuki, Takemori, Hiroshi, & Doi, Junko. Molecular identity and gene expression of aldosterone synthase cytochrome P450.  United States.  doi:10.1016/J.BBRC.2005.0.

Copy to clipboard


                    Okamoto, Mitsuhiro, Nonaka, Yasuki, Takemori, Hiroshi, and Doi, Junko. Fri .  
        "Molecular identity and gene expression of aldosterone synthase cytochrome P450".  United States.  
        doi:10.1016/J.BBRC.2005.0.

Copy to clipboard


                    
@article{osti_20793199,

  title        = {Molecular identity and gene expression of aldosterone synthase cytochrome P450},

  author       = {Okamoto, Mitsuhiro and Nonaka, Yasuki and Takemori, Hiroshi and Doi, Junko},

  abstractNote = {11{beta}-Hydroxylase (CYP11B1) of bovine adrenal cortex produced corticosterone as well as aldosterone from 11-deoxycorticosterone in the presence of the mitochondrial P450 electron transport system. CYP11B1s of pig, sheep, and bullfrog, when expressed in COS-7 cells, also performed corticosterone and aldosterone production. Since these CYP11B1s are present in the zonae fasciculata and reticularis as well as in the zona glomerulosa, the zonal differentiation of steroid production may occur by the action of still-unidentified factor(s) on the enzyme-catalyzed successive oxygenations at C11- and C18-positions of steroid. In contrast, two cDNAs, one encoding 11{beta}-hydroxylase and the other encoding aldosterone synthase (CYP11B2), were isolated from rat, mouse, hamster, guinea pig, and human adrenals. The expression of CYP11B1 gene was regulated by cyclic AMP (cAMP)-dependent signaling, whereas that of CYP11B2 gene by calcium ion-signaling as well as cAMP-signaling. Salt-inducible protein kinase, a cAMP-induced novel protein kinase, was one of the regulators of CYP11B2 gene expression.},

  doi          = {10.1016/J.BBRC.2005.0},

  journal      = {Biochemical and Biophysical Research Communications},

  number       = 1,

  volume       = 338,

  place        = {United States},

  year         = {Fri Dec 09 00:00:00 EST 2005},

  month        = {Fri Dec 09 00:00:00 EST 2005}

}

Copy to clipboard

Journal Article:

DOI: 10.1016/J.BBRC.2005.0

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

DHA down-regulates phenobarbital-induced cytochrome P450 2B1 gene expression in rat primary hepatocytes by attenuating CAR translocation

Journal Article Li, C.-C. ; Lii, C.-K. ; Liu, K.-L. ; ... - Toxicology and Applied Pharmacology

The constitutive androstane receptor (CAR) plays an important role in regulating the expression of detoxifying enzymes, including cytochrome P450 2B (CYP 2B). Phenobarbital (PB) induction of human CYP 2B6 and mouse CYP 2b10 has been shown to be mediated by CAR. Our previous study showed that PB-induced CYP 2B1 expression in rat primary hepatocytes is down-regulated by both n-6 and n-3 polyunsaturated fatty acids (PUFAs), especially docosahexaenoic acid (DHA); however, the mechanism for this down-regulation by DHA was previously unknown. The objective of the present study was to determine whether change in CAR translocation is involved in the down-regulation bymore »« less
DOI: 10.1016/j.taap.2007.08.009
The cytochrome P450 2AA gene cluster in zebrafish (Danio rerio): Expression of CYP2AA1 and CYP2AA2 and response to phenobarbital-type inducers

Journal Article Kubota, Akira ; Bainy, Afonso C.D. ; Departamento de Bioquímica, CCB, Universidade Federal de Santa Catarina, Florianopolis, SC 88040-900 ; ... - Toxicology and Applied Pharmacology

The cytochrome P450 (CYP) 2 gene family is the largest and most diverse CYP gene family in vertebrates. In zebrafish, we have identified 10 genes in a new subfamily, CYP2AA, which does not show orthology to any human or other mammalian CYP genes. Here we report evolutionary and structural relationships of the 10 CYP2AA genes and expression of the first two genes, CYP2AA1 and CYP2AA2. Parsimony reconstruction of the tandem duplication pattern for the CYP2AA cluster suggests that CYP2AA1, CYP2AA2 and CYP2AA3 likely arose in the earlier duplication events and thus are most diverged in function from the other CYP2AAs.more »« less
DOI: 10.1016/J.TAAP.2013.05.017
Structure and function of NADPH-cytochrome P450 reductase and nitric oxide synthase reductase domain

Journal Article Iyanagi, Takashi - Biochemical and Biophysical Research Communications

NADPH-cytochrome P450 reductase (CPR) and the nitric oxide synthase (NOS) reductase domains are members of the FAD-FMN family of proteins. The FAD accepts two reducing equivalents from NADPH (dehydrogenase flavin) and FMN acts as a one-electron carrier (flavodoxin-type flavin) for the transfer from NADPH to the heme protein, in which the FMNH {sup {center_dot}}/FMNH{sub 2} couple donates electrons to cytochrome P450 at constant oxidation-reduction potential. Although the interflavin electron transfer between FAD and FMN is not strictly regulated in CPR, electron transfer is activated in neuronal NOS reductase domain upon binding calmodulin (CaM), in which the CaM-bound activated form canmore »« less
DOI: 10.1016/J.BBRC.2005.0
Crystallization and preliminary X-ray analysis of allene oxide synthase, cytochrome P450 CYP74A2, from Parthenium argentatum

Journal Article Chang, Zhenzhan ; Li, Lenong ; Pan, Zhiqiang, E-mail: zpan@ars.usda.gov ; ... - Acta Crystallographica. Section F

Allene oxide synthase, an atypical cytochrome P450 from Parthenium argentatum, was crystallized and diffraction data were collected to 2.4 Å resolution. Oxylipins are oxygenated derivatives of fatty acids and pivotal signaling molecules in plants and animals. Allene oxide synthase (AOS) is a key cytochrome P450 CYP74 enzyme involved in the biosynthesis of plant oxylipin jasmonates to convert 13(S)-hydroperoxide to allene oxide. Guayule (Parthenium argentatum) AOS, CYP74A2, was expressed in Escherichia coli. Protein was purified using affinity chromatography and size exclusion chromatography, and then crystallized. Two different crystal forms were obtained from 0.2 M (NH{sub 4})H{sub 2}PO{sub 4}, 50% MPD, 0.1more »« less
DOI: 10.1107/S1744309108017545
Cytochrome P450 expression and activities in human tongue cells and their modulation by green tea extract

Journal Article Yang, S.-P. ; Raner, Gregory M. - Toxicology and Applied Pharmacology

The expression, inducibility, and activities of several cytochrome P450 (CYP) enzymes were investigated in a human tongue carcinoma cell model, CAL 27, and compared with the human liver model HepG2 cells. The modulation effects of green tea on various CYP isoforms in both cell lines were also examined. RT-PCR analysis of CAL 27 cells demonstrated constitutive expression of mRNA for CYPs 1A1, 1A2, 2C, 2E1, 2D6, and 4F3. The results were negative for CYP2A6, 2B6/7, 3A3/4, and 3A7. Both cell lines displayed identical expression and induction profiles for all of the isoforms examined in this study except 3A7 and 2B6/7,more »« less
DOI: 10.1016/j.taap.2004.06.014

Similar Records