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Title: Mammalian. beta. /sub 1/- and. beta. /sub 2/-adrenergic receptors: immunological and structural comparison

Abstract

..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors, pharmacologically distinct proteins, have been reported to be structurally dissimilar. In the present study three techniques were employed to compare the nature of mammalian ..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors. Antibodies against each of the receptor subtypes were raised separately. Polyclonal antisera against ..beta../sub 1/-receptors of rat fat cells were raised in mice, and antisera against ..beta../sub 2/-receptors of guinea pig lung were raised in rabbits. Receptors purified from rat fat cells (..beta../sub 1/-), S49 mouse lymphoma cells (..beta../sub 2/-), and rat liver (..beta../sub 2/-) were probed with these antisera. Each anti-receptor antisera demonstrated the ability to immunoprecipitate purified receptors of both ..beta../sub 1/- and ..beta../sub 2/-subtypes. The mobility of ..beta..-receptors subjected to polyacrylamide gel electrophoresis was probed using antireceptor antibodies and nitrocellulose blots of the gels. Fat cell ..beta../sub 1/-adrenergic receptors display M/sub r/ = 67,000 under reducing conditions and M/sub r/ = 54,000 under nonreducing conditions, as previously reported. Both ..beta../sub 1/- and ..beta../sub 2/-receptors displayed this same shift in electrophoretic mobility observed in the presence as compared to the absence of disulfide bridge-reducing agents, as detected both by autoradiography of the radiolabeled receptors and by immunoblotting of native receptors. Finally, isoelectricmore » focusing of purified radioiodinated ..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors revealed identical isoelectric points. These data are the first to provide analyses of immunological, structural, and biochemical features of ..beta../sub 1/- and ..beta../sub 2/-subtypes in tandem and underscore the structural similarities that exist between these pharmacologically distinct receptors.« less

Authors:
; ; ; ;
Publication Date:
Research Org.:
State Univ. of New York, Stony Brook
OSTI Identifier:
6934304
Resource Type:
Journal Article
Journal Name:
J. Biol. Chem.; (United States)
Additional Journal Information:
Journal Volume: 261:31
Country of Publication:
United States
Language:
English
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; 59 BASIC BIOLOGICAL SCIENCES; FAT CELLS; ENZYME IMMUNOASSAY; RADIORECEPTOR ASSAY; RECEPTORS; AUTORADIOGRAPHY; MOLECULAR STRUCTURE; ELECTROPHORESIS; GUINEA PIGS; IMMUNE SERUMS; IODINE 125; LIVER; LUNGS; MICE; MOLECULAR WEIGHT; PROTEINS; RABBITS; TUMOR CELLS; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; BODY; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DIGESTIVE SYSTEM; ELECTRON CAPTURE RADIOISOTOPES; GLANDS; IMMUNOASSAY; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MAMMALS; MEMBRANE PROTEINS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANS; RADIOISOTOPES; RESPIRATORY SYSTEM; RODENTS; SOMATIC CELLS; TRACER TECHNIQUES; VERTEBRATES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics; 550201 - Biochemistry- Tracer Techniques

Citation Formats

Moxham, C P, George, S T, Graziano, M P, Brandwein, H J, and Malbon, C C. Mammalian. beta. /sub 1/- and. beta. /sub 2/-adrenergic receptors: immunological and structural comparison. United States: N. p., 1986. Web.
Moxham, C P, George, S T, Graziano, M P, Brandwein, H J, & Malbon, C C. Mammalian. beta. /sub 1/- and. beta. /sub 2/-adrenergic receptors: immunological and structural comparison. United States.
Moxham, C P, George, S T, Graziano, M P, Brandwein, H J, and Malbon, C C. 1986. "Mammalian. beta. /sub 1/- and. beta. /sub 2/-adrenergic receptors: immunological and structural comparison". United States.
@article{osti_6934304,
title = {Mammalian. beta. /sub 1/- and. beta. /sub 2/-adrenergic receptors: immunological and structural comparison},
author = {Moxham, C P and George, S T and Graziano, M P and Brandwein, H J and Malbon, C C},
abstractNote = {..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors, pharmacologically distinct proteins, have been reported to be structurally dissimilar. In the present study three techniques were employed to compare the nature of mammalian ..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors. Antibodies against each of the receptor subtypes were raised separately. Polyclonal antisera against ..beta../sub 1/-receptors of rat fat cells were raised in mice, and antisera against ..beta../sub 2/-receptors of guinea pig lung were raised in rabbits. Receptors purified from rat fat cells (..beta../sub 1/-), S49 mouse lymphoma cells (..beta../sub 2/-), and rat liver (..beta../sub 2/-) were probed with these antisera. Each anti-receptor antisera demonstrated the ability to immunoprecipitate purified receptors of both ..beta../sub 1/- and ..beta../sub 2/-subtypes. The mobility of ..beta..-receptors subjected to polyacrylamide gel electrophoresis was probed using antireceptor antibodies and nitrocellulose blots of the gels. Fat cell ..beta../sub 1/-adrenergic receptors display M/sub r/ = 67,000 under reducing conditions and M/sub r/ = 54,000 under nonreducing conditions, as previously reported. Both ..beta../sub 1/- and ..beta../sub 2/-receptors displayed this same shift in electrophoretic mobility observed in the presence as compared to the absence of disulfide bridge-reducing agents, as detected both by autoradiography of the radiolabeled receptors and by immunoblotting of native receptors. Finally, isoelectric focusing of purified radioiodinated ..beta../sub 1/- and ..beta../sub 2/-adrenergic receptors revealed identical isoelectric points. These data are the first to provide analyses of immunological, structural, and biochemical features of ..beta../sub 1/- and ..beta../sub 2/-subtypes in tandem and underscore the structural similarities that exist between these pharmacologically distinct receptors.},
doi = {},
url = {https://www.osti.gov/biblio/6934304}, journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 261:31,
place = {United States},
year = {Wed Nov 05 00:00:00 EST 1986},
month = {Wed Nov 05 00:00:00 EST 1986}
}