Regional distribution of α1-adrenoceptor subtypes in rat kidney

F. Feng, W. A. Pettinger, Peter W. Abel, W. B. Jeffries

Research output: Contribution to journalArticle

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Abstract

α1-Adrenoceptors are expressed in high density in the rat kidney. Recent studies have shown that α1-adrenoceptors are heterogeneous and can be subtyped based on their affinity for the antagonists WB 4101 (α(1A) > α(1B) and chloroethylclonidine (α(1B-selective). We therefore investigated the distribution of α1-adrenoceptor subtypes using [3H]prazosin binding in membranes prepared from cortex, the outer stripe of the outer medulla (OSOM), the inner stripe of the outer medulla (ISOM) and inner medulla dissected from rat kidney. [3H]Prazosin binding was detectable in each region with the following maximum binding site values for [3H]prazosin (femtomoles per milligram of protein): cortex, 186 ± 20; OSOM, 76 ± 14; ISOM, 34 ± 2; and inner medulla, 8 ± 2. Pretreatment of membranes with chloroethylclonidine (10 μM for 10 min) reduced maximum binding sites to 41 ± 4% (75 ± 9 fmol/mg) of control in cortex, 41 ± 9% of control in OSOM (29 ± 8 fmol/mg) and 15 ± 3% of control in ISOM (5 ± 1 fmol/mg). In competition studies, WB 4101 labeled both high and low affinity sites in cortex (respective pKi values = 10.01 ± 0.3 and 8.23 ± 0.1) and OSOM (pKi values = 9.6 + 0.3 and 8.3 ± 0.5), but only low affinity sites in ISOM (pKi = 8.41 ± 0.1). The relative prevalence of high:low affinity sites revealed by WB 4101 was 53:47 for cortex, 52:48 for OSOM and virtually all low affinity for ISOM. Prior treatment with chloroethylclonidine greatly reduced the low affinity component of the WB 4101 competition curve in cortex and OSOM. We conclude that: 1) the density of α1-adrenoceptors is highest in the cortex and decreases from cortex to papilla and 2) the α(1A) and α(1B) subtypes are approximately equally distributed in the cortex and OSOM, but the α(1B) subtype predominates in ISOM.

Original languageEnglish
Pages (from-to)263-268
Number of pages6
JournalJournal of Pharmacology and Experimental Therapeutics
Volume258
Issue number1
StatePublished - 1991
Externally publishedYes

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Adrenergic Receptors
Prazosin
Kidney
Binding Sites
Membranes
(2-(2',6'-dimethoxy)phenoxyethylamino)methylbenzo-1,4-dioxane
chlorethylclonidine
Proteins

All Science Journal Classification (ASJC) codes

  • Pharmacology

Cite this

Regional distribution of α1-adrenoceptor subtypes in rat kidney. / Feng, F.; Pettinger, W. A.; Abel, Peter W.; Jeffries, W. B.

In: Journal of Pharmacology and Experimental Therapeutics, Vol. 258, No. 1, 1991, p. 263-268.

Research output: Contribution to journalArticle

Feng, F. ; Pettinger, W. A. ; Abel, Peter W. ; Jeffries, W. B. / Regional distribution of α1-adrenoceptor subtypes in rat kidney. In: Journal of Pharmacology and Experimental Therapeutics. 1991 ; Vol. 258, No. 1. pp. 263-268.
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N2 - α1-Adrenoceptors are expressed in high density in the rat kidney. Recent studies have shown that α1-adrenoceptors are heterogeneous and can be subtyped based on their affinity for the antagonists WB 4101 (α(1A) > α(1B) and chloroethylclonidine (α(1B-selective). We therefore investigated the distribution of α1-adrenoceptor subtypes using [3H]prazosin binding in membranes prepared from cortex, the outer stripe of the outer medulla (OSOM), the inner stripe of the outer medulla (ISOM) and inner medulla dissected from rat kidney. [3H]Prazosin binding was detectable in each region with the following maximum binding site values for [3H]prazosin (femtomoles per milligram of protein): cortex, 186 ± 20; OSOM, 76 ± 14; ISOM, 34 ± 2; and inner medulla, 8 ± 2. Pretreatment of membranes with chloroethylclonidine (10 μM for 10 min) reduced maximum binding sites to 41 ± 4% (75 ± 9 fmol/mg) of control in cortex, 41 ± 9% of control in OSOM (29 ± 8 fmol/mg) and 15 ± 3% of control in ISOM (5 ± 1 fmol/mg). In competition studies, WB 4101 labeled both high and low affinity sites in cortex (respective pKi values = 10.01 ± 0.3 and 8.23 ± 0.1) and OSOM (pKi values = 9.6 + 0.3 and 8.3 ± 0.5), but only low affinity sites in ISOM (pKi = 8.41 ± 0.1). The relative prevalence of high:low affinity sites revealed by WB 4101 was 53:47 for cortex, 52:48 for OSOM and virtually all low affinity for ISOM. Prior treatment with chloroethylclonidine greatly reduced the low affinity component of the WB 4101 competition curve in cortex and OSOM. We conclude that: 1) the density of α1-adrenoceptors is highest in the cortex and decreases from cortex to papilla and 2) the α(1A) and α(1B) subtypes are approximately equally distributed in the cortex and OSOM, but the α(1B) subtype predominates in ISOM.

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