Abstract
A human cytochrome P-450 with aldosterone synthase activity was purified from the mitochondria of an aldosterone-producing adenoma. It was recognized by an anti-bovine cytochrome P-450(11β) IgG and by a specific antibody raised against a portion of the CYP11B2 gene product, one of the two putative proteins encoded by human cytochrome P-450(11β)-related genes (Mornet, E., Dupont, J., Vitek, A., and White, P. C. (1989) J. Biol. Chem. 264, 20961-20967). A similar and probably the same aldosterone synthase cytochrome P-450 was detected in the adrenal of a patient with idiopathic hyperaldosteronism. These aldosterone synthases were distinguishable from cytochrome P-450(11β), the product of another cytochrome P-450(11β)-related gene, i.e. CYP11B1, by their catalytic, molecular, and immunological properties and also by their localization. The latter enzyme was unable to produce aldosterone and did not react with the specific antibody against the CYP11B2 gene product. It was present both in tumor and non-tumor portions of the adrenals carrying the adenoma and in normal adrenal cortex. On the other hand, aldosterone synthase cytochrome P-450 localized in the tumor portion of the adrenals or in the adrenal of a patient with idiopathic hyperaldosteronism. Thus aldosterone synthase cytochrome P-450, a distinct species from cytochrome P-450(11β), is responsible for the biosynthesis of aldosterone in the human, at least in patients suffering from primary aldosteronism.
| Original language | English |
|---|---|
| Pages (from-to) | 10731-10734 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 266 |
| Issue number | 17 |
| Publication status | Published - Sep 6 1991 |
| Externally published | Yes |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Aldosterone synthase cytochrome P-450 expressed in the adrenals of patients with primary aldosteronism. / Ogishima, Tadashi; Shibata, H.; Shimada, H.; Mitani, F.; Suzuki, H.; Saruta, T.; Ishimura, Y.
In: Journal of Biological Chemistry, Vol. 266, No. 17, 06.09.1991, p. 10731-10734.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Aldosterone synthase cytochrome P-450 expressed in the adrenals of patients with primary aldosteronism
AU - Ogishima, Tadashi
AU - Shibata, H.
AU - Shimada, H.
AU - Mitani, F.
AU - Suzuki, H.
AU - Saruta, T.
AU - Ishimura, Y.
PY - 1991/9/6
Y1 - 1991/9/6
N2 - A human cytochrome P-450 with aldosterone synthase activity was purified from the mitochondria of an aldosterone-producing adenoma. It was recognized by an anti-bovine cytochrome P-450(11β) IgG and by a specific antibody raised against a portion of the CYP11B2 gene product, one of the two putative proteins encoded by human cytochrome P-450(11β)-related genes (Mornet, E., Dupont, J., Vitek, A., and White, P. C. (1989) J. Biol. Chem. 264, 20961-20967). A similar and probably the same aldosterone synthase cytochrome P-450 was detected in the adrenal of a patient with idiopathic hyperaldosteronism. These aldosterone synthases were distinguishable from cytochrome P-450(11β), the product of another cytochrome P-450(11β)-related gene, i.e. CYP11B1, by their catalytic, molecular, and immunological properties and also by their localization. The latter enzyme was unable to produce aldosterone and did not react with the specific antibody against the CYP11B2 gene product. It was present both in tumor and non-tumor portions of the adrenals carrying the adenoma and in normal adrenal cortex. On the other hand, aldosterone synthase cytochrome P-450 localized in the tumor portion of the adrenals or in the adrenal of a patient with idiopathic hyperaldosteronism. Thus aldosterone synthase cytochrome P-450, a distinct species from cytochrome P-450(11β), is responsible for the biosynthesis of aldosterone in the human, at least in patients suffering from primary aldosteronism.
AB - A human cytochrome P-450 with aldosterone synthase activity was purified from the mitochondria of an aldosterone-producing adenoma. It was recognized by an anti-bovine cytochrome P-450(11β) IgG and by a specific antibody raised against a portion of the CYP11B2 gene product, one of the two putative proteins encoded by human cytochrome P-450(11β)-related genes (Mornet, E., Dupont, J., Vitek, A., and White, P. C. (1989) J. Biol. Chem. 264, 20961-20967). A similar and probably the same aldosterone synthase cytochrome P-450 was detected in the adrenal of a patient with idiopathic hyperaldosteronism. These aldosterone synthases were distinguishable from cytochrome P-450(11β), the product of another cytochrome P-450(11β)-related gene, i.e. CYP11B1, by their catalytic, molecular, and immunological properties and also by their localization. The latter enzyme was unable to produce aldosterone and did not react with the specific antibody against the CYP11B2 gene product. It was present both in tumor and non-tumor portions of the adrenals carrying the adenoma and in normal adrenal cortex. On the other hand, aldosterone synthase cytochrome P-450 localized in the tumor portion of the adrenals or in the adrenal of a patient with idiopathic hyperaldosteronism. Thus aldosterone synthase cytochrome P-450, a distinct species from cytochrome P-450(11β), is responsible for the biosynthesis of aldosterone in the human, at least in patients suffering from primary aldosteronism.
UR - http://www.scopus.com/inward/record.url?scp=0025859698&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025859698&partnerID=8YFLogxK
M3 - Article
VL - 266
SP - 10731
EP - 10734
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 17
ER -