Brain α-adrenergic receptors: comparison of [3H]WB 4101 binding with norepinephrine-stimulated cyclic AMP accumulation in rat cerebral cortex

Davis, James N.; Arnett, Carroll D.; Hoyler, Elizabeth; Stalvey, Linda P.; Daly, John W.; Skolnick, Phil

doi:10.1016/0006-8993(78)90114-2

Cited by 43 publications

(10 citation statements)

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“…As in other tissues, activation of brain cul-adrenergic receptors increases inositol phosphate accumulation (Brown et al, 1984;Minneman and Johnson, 1984), presumably by G protein-mediated activation of the hydrolysis of phosphatidylinositol 4,5-bisphosphate. In contrast with most other tissues, however, a,-adrenergic receptor activation also increases cyclic AMP accumulation in brain slices and potentiates the cyclic AMP response to activation of other receptor types (Davis et al, 1978;Daly et al, 1981;Johnson and Minneman, 1986). Work from this laboratory has demonstrated that the inositol phosphate and cyclic AMP responses were differentially distributed in regions of rat brain Minneman, 1985, 1987).…”

Section: Discussionmentioning

confidence: 98%

Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

Wilson

Minneman

1989

Journal of Neurochemistry

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alpha 1-Adrenergic receptor subtypes were differentiated by their affinities for the competitive antagonist WB 4101 and their sensitivities to inactivation by chlorethylclonidine (CEC) in eight rat brain regions. WB 4101 showed low Hill coefficients for inhibition of specific 125I-[2-beta-(4-hydroxyphenyl)ethylaminomethyl]tetralone (125IBE) binding in all regions. Nonlinear regression analysis showed that there were two binding sites with different affinities for WB 4101 in each region. The proportions of these sites varied among regions, although the affinity of WB 4101 for each site remained constant. Thalamus and cerebral cortex had the highest proportion of low-affinity sites, whereas hippocampus and pons-medulla had the highest proportion of high-affinity sites. Pretreatment with CEC in hypotonic buffer significantly reduced the density of 125IBE binding sites in all brain regions. Cerebral cortex and cerebellum had the highest proportion of CEC-sensitive sites, whereas hippocampus and spinal cord had the highest proportion of CEC-insensitive sites. There was a significant correlation between the proportion of binding sites with a low affinity for WB 4101 and those sensitive to inactivation by CEC.

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Section: Discussionmentioning

confidence: 98%

Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

Wilson

Minneman

1989

Journal of Neurochemistry

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“…In rat cerebral cortex slices, Davis et al [1978] proposed that the a l adrenergic receptor sites labeled with WB 4101 are those involved in a adrenergic induced cyclic AMP accumulation. This ( Y I adrenergic effect is probably indirect, since it has been shown to be reduced by inhibitors of prostaglandin synthesis [Partington et al, 19801.…”

Section: Discussionmentioning

confidence: 99%

“…We suggest that the a2 adrenergic receptors described in the report on glial cells are the same as those involved in the CY adrenergic inhibition of 0 adrenergic-induced cyclic AMP accumulation reported in these cells by others [Van Calker et al, 1978;McCarthy and De Vellis, 19781. The mechanism of action of C Y ] adrenergic receptors in glial cells is completely unknown. In rat cerebral cortex slices, Davis et al [1978] proposed that the a l adrenergic receptor sites labeled with WB 4101 are those involved in a adrenergic induced cyclic AMP accumulation. This ( Y I adrenergic effect is probably indirect, since it has been shown to be reduced by inhibitors of prostaglandin synthesis [Partington et al, 19801.…”

Section: Discussionmentioning

confidence: 99%

α₁ and α₂ Adrenergic receptors in mouse brain astrocytes from primary cultures

Ebersolt

Pérez

Bockaert

1981

J of Neuroscience Research

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Mouse brain astrocytes from primary cultures were found to contain both alpha 1 and alpha 2 adrenergic receptors. 3H WB 4101 labeled one category of binding site (KD = 1.5 +/- 0.39 nM, Bmax = 64 +/- 7.9 fmoles/mg protein) with typical alpha 1 adrenergic specificity (WB 4101 greater than prazosin greater than yohimbine). The density of alpha 1 adrenergic receptors was 2-3 times higher in mouse cerebral cortex than in glial cells. Like rat brain [U'Pritchard et al, 1979; Rouot et al, 1980], mouse glial cells were found to contain two categories of 3H clonidine binding sites: high affinity sites, which were identical to the high but not to the low affinity sites found in rat brain, since 1) they displayed the same affinity for 3H clonidine (KD = 1.2 +/- 0.13 nM, n = 4) and the same typical alpha 2 adrenergic specificity (yohimbine greater than WB 4101 greater than prazosin); 2) the dissociation rate constant for clonidine binding was equal to 0.06 min-1, a value close to that found previously for the high affinity 3H clonidine binding sites in rat brain (0.05 min-1); and 3) divalent cations augmented and guanyl nucleotides reduced 3H clonidine binding as in rat brain. Na+ decreased 3H clonidine binding in a complex manner. The number of high affinity sites in glial cells (52 +/- 9.4 fmoles/mg protein, n = 4) was half the number found in mouse cerebral cortex (98 fmoles/mg protein). Low affinity 3H clonidine binding sites (KD = 81 +/- 18 nM, Bmax = 96 +/- 5.8 fmoles/mg protein, n = 3) were not fully characterized. In conclusion, glial cells contained the same alpha adrenergic receptors as those described in brain, but their physiological function is not yet known.

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“…Reference Greenberg et al, 1976Neethling et al, 1981Davis et al, 1978Lyon and Randall, 1980Weinreich and Seeman, 1981Latifpour and Bylund, 1981Yamada et al, 1980Raisman et al, 1979Bylund et al, 1982bFarley et al, 1984Farley et al, 1984Burns et al, 1983 OJ -0 ::r Bylund, 1981. bYamada et aI., 1980.…”

Section: Commentsmentioning

confidence: 99%

The alpha-1 Adrenergic Receptors

Ruffolo¹

1987

The Receptors

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All rights reservedNo part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise without written permission from the Publisher.Preface vii ology will allow alpha-l adrenergic receptors to be isolated and purified and their amino acid sequence to be identified. This will ultimately allow for the systematic subclassification of alpha-l adrenergic receptors and for their differential regulation to be studied in greater detail. These new advances are likely to take place within the next five years, and it is our intent for this review of alpha-l adrenergic receptor pharmacology to provide an accurate summary of the current state of knowledge relating to alpha-l adrenergic receptors, which we hope will serve as a foundation upon which to build a broader base of knowledge in the future.

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Brain α-adrenergic receptors: comparison of [3H]WB 4101 binding with norepinephrine-stimulated cyclic AMP accumulation in rat cerebral cortex

Cited by 43 publications

References 15 publications

Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

α₁ and α₂ Adrenergic receptors in mouse brain astrocytes from primary cultures

The alpha-1 Adrenergic Receptors

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Brain α-adrenergic receptors: comparison of [3H]WB 4101 binding with norepinephrine-stimulated cyclic AMP accumulation in rat cerebral cortex

Cited by 43 publications

References 15 publications

Regional Variations in α1‐Adrenergic Receptor Subtypes in Rat Brain

Regional Variations in α1‐Adrenergic Receptor Subtypes in Rat Brain

α1 and α2 Adrenergic receptors in mouse brain astrocytes from primary cultures

The alpha-1 Adrenergic Receptors

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Product

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Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

Regional Variations in α₁‐Adrenergic Receptor Subtypes in Rat Brain

α₁ and α₂ Adrenergic receptors in mouse brain astrocytes from primary cultures