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KP Minneman, C Han and PW Abel
Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322.
We showed previously that subtypes of alpha 1-adrenergic receptors can be differentiated by selective inactivation with chlorethylclonidine (CEC) [Mol. Pharmacol. 32:505-510 (1987)] or by their affinities for the competitive antagonist WB 4101 [Nature (Lond.) 329:333-335 (1987)]. Examining eight rat tissues, the proportions of 125IBE 2254-binding sites sensitive to inactivation by CEC correlated significantly (p less than 0.05) with the proportion having a low affinity for WB 4101. However, the proportion of CEC-sensitive sites was always smaller than the proportion of low affinity WB 4101 sites. Further experiments showed that repetitive pretreatment with CEC or pretreatment under hypotonic conditions caused a larger inactivation of binding sites, suggesting that CEC did not access all sites under the isotonic conditions used previously. The proportions of binding sites inactivated by 10 microM CEC under hypotonic conditions were quantitatively similar to and correlated significantly (p less than 0.01) with the proportion having a low affinity for WB 4101. Pretreatment of hippocampus and vas deferens with CEC caused a loss of all low affinity WB 4101-binding sites, leaving only high affinity sites. In vas deferens, CEC pretreatment decreased the potency of norepinephrine in stimulating 3H-inositol phosphate accumulation but not contractile responses. In rat liver slices, CEC inactivated norepinephrine-stimulated 3H-inositol phosphate accumulation in parallel with 125IBE-binding sites. These results suggest that: 1) the CEC-sensitive and -insensitive 125IBE 2254-binding sites are equivalent to those with a low and high affinity for WB 4101, respectively, and 2) the CEC-sensitive binding sites with a low affinity for WB 4101 are the alpha 1-adrenergic receptors linked to inositol phospholipid hydrolysis.
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