Abstract
Zonal distribution of aldosterone synthase cytochrome P-450 and cytochrome P-45011β in rat adrenocortex was investigated immunochemically using specific antibodies to these enzymes. Localization of aldosterone synthase cytochrome P-450 (cytochrome P-450aldo), a recently identified enzyme that converts deoxycorticosterone to aldosterone in rat adrenocortex was strictly confined to two or three outermost cell layers in the zona glomerulosa. In contrast, cytochrome P-45011β, which forms corticosterone, but not aldosterone, from deoxycorticosterone, was localized in the zona fasciculata-reticularis and not in the zona glomerulosa. Neither enzyme was detected in the medulla or the capsule. The functional zonation of adrenocortex with respect to aldosterone and corticosterone syntheses is, thus, ascribable to the localization of cytochromes P-450aldo and P- 45011β in the respective zones. When rats were maintained under Na-depleted conditions for 10 days, the zona glomerulosa cells containing cytochrome P-450aldo proliferated to 10-15layers, the thickness of which was 5-7-fold that in the nonstimulated rats. Proliferation of the cytochrome P-450aldo-positive cells into the zona fasciculata-reticularis was also observed along with arterial walls. Under these conditions, no significant change in the distribution of cytochrome P-45011β was noted. These results indicate that the angiotensin-II stimuli, which had been elicited by the low Na treatment, promoted proliferation of the glomerulosa cells, resulting in increased expression of cytochrome P-450aldo in rat adrenocortex.
| Original language | English |
|---|---|
| Pages (from-to) | 2971-2977 |
| Number of pages | 7 |
| Journal | Endocrinology |
| Volume | 130 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - Jan 1 1992 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Endocrinology
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Zone-specific expression of aldosterone synthase cytochrome p-450 and cytochrome p-45011β in rat adrenal cortex : Histochemical basis for the functional zonation. / Ogishima, Tadashi; Suzuki, Hiroshi; Hata, Jun Ichi; Mitani, Fumiko; Ishimura, Yuzuru.
In: Endocrinology, Vol. 130, No. 5, 01.01.1992, p. 2971-2977.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Zone-specific expression of aldosterone synthase cytochrome p-450 and cytochrome p-45011β in rat adrenal cortex
T2 - Histochemical basis for the functional zonation
AU - Ogishima, Tadashi
AU - Suzuki, Hiroshi
AU - Hata, Jun Ichi
AU - Mitani, Fumiko
AU - Ishimura, Yuzuru
PY - 1992/1/1
Y1 - 1992/1/1
N2 - Zonal distribution of aldosterone synthase cytochrome P-450 and cytochrome P-45011β in rat adrenocortex was investigated immunochemically using specific antibodies to these enzymes. Localization of aldosterone synthase cytochrome P-450 (cytochrome P-450aldo), a recently identified enzyme that converts deoxycorticosterone to aldosterone in rat adrenocortex was strictly confined to two or three outermost cell layers in the zona glomerulosa. In contrast, cytochrome P-45011β, which forms corticosterone, but not aldosterone, from deoxycorticosterone, was localized in the zona fasciculata-reticularis and not in the zona glomerulosa. Neither enzyme was detected in the medulla or the capsule. The functional zonation of adrenocortex with respect to aldosterone and corticosterone syntheses is, thus, ascribable to the localization of cytochromes P-450aldo and P- 45011β in the respective zones. When rats were maintained under Na-depleted conditions for 10 days, the zona glomerulosa cells containing cytochrome P-450aldo proliferated to 10-15layers, the thickness of which was 5-7-fold that in the nonstimulated rats. Proliferation of the cytochrome P-450aldo-positive cells into the zona fasciculata-reticularis was also observed along with arterial walls. Under these conditions, no significant change in the distribution of cytochrome P-45011β was noted. These results indicate that the angiotensin-II stimuli, which had been elicited by the low Na treatment, promoted proliferation of the glomerulosa cells, resulting in increased expression of cytochrome P-450aldo in rat adrenocortex.
AB - Zonal distribution of aldosterone synthase cytochrome P-450 and cytochrome P-45011β in rat adrenocortex was investigated immunochemically using specific antibodies to these enzymes. Localization of aldosterone synthase cytochrome P-450 (cytochrome P-450aldo), a recently identified enzyme that converts deoxycorticosterone to aldosterone in rat adrenocortex was strictly confined to two or three outermost cell layers in the zona glomerulosa. In contrast, cytochrome P-45011β, which forms corticosterone, but not aldosterone, from deoxycorticosterone, was localized in the zona fasciculata-reticularis and not in the zona glomerulosa. Neither enzyme was detected in the medulla or the capsule. The functional zonation of adrenocortex with respect to aldosterone and corticosterone syntheses is, thus, ascribable to the localization of cytochromes P-450aldo and P- 45011β in the respective zones. When rats were maintained under Na-depleted conditions for 10 days, the zona glomerulosa cells containing cytochrome P-450aldo proliferated to 10-15layers, the thickness of which was 5-7-fold that in the nonstimulated rats. Proliferation of the cytochrome P-450aldo-positive cells into the zona fasciculata-reticularis was also observed along with arterial walls. Under these conditions, no significant change in the distribution of cytochrome P-45011β was noted. These results indicate that the angiotensin-II stimuli, which had been elicited by the low Na treatment, promoted proliferation of the glomerulosa cells, resulting in increased expression of cytochrome P-450aldo in rat adrenocortex.
UR - http://www.scopus.com/inward/record.url?scp=0026748962&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026748962&partnerID=8YFLogxK
U2 - 10.1210/endo.130.5.1572304
DO - 10.1210/endo.130.5.1572304
M3 - Article
C2 - 1572304
AN - SCOPUS:0026748962
VL - 130
SP - 2971
EP - 2977
JO - Endocrinology
JF - Endocrinology
SN - 0013-7227
IS - 5
ER -