ISSN:
0730-2312
Keywords:
neurotransmitter receptors
;
monoclonal antibodies
;
muscarinic acetylcholine receptors
;
receptor purification
;
receptor subunits
;
target size analysis
;
autoantibodies
;
alpha-adrenergic receptors
;
beta-adrenergic receptors
;
dopamine receptors
;
immunoaffinity chromatography
;
isoelectric focusing
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
The combination of immunological advances with membrane receptor research has promoted rapid progress in the molecular characterization of neurotransmitter receptor molecules. We have to date produced monoclonal antibodies to β1-, β2-, and β1-adrenergic, D2-dopaminergic, and muscarinic receptors. In addition we have discovered that some allergic respiratory disease patients possess circulating autoantibodies to β2-adrenergic receptors. These antireceptor antibodies in conjunction with specific receptor affinity reagents have allowed us to isolate, purify, and begin to characterize α- and β-adrenergic, dopaminergic, and muscarinic receptors. For example, immunoprecipitation of turkey erythrocyte β1 receptors with monoclonal antibodies yields a single polypeptide Mr 65-70 K. In contrast, purification of β2-adrenergic receptors using either autoantibodies or monoclonal antibodies yields a receptor species with a subunit of Mr 55-59 K. Autoantibodies to β2 receptors demonstrate a 50-100% homology among β2 receptors from humans to rats, whereas monoclonal antibody FV-104 recognizes a determinant in the ligand binding site of all β1 and β2 receptors tested to date. These data suggest that β1- and β2-adrenergic receptors may have evolved from a common ancestor, perhaps by gene duplication.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jcb.240210304
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