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Probing the immunological properties of the extracellular domains of the human beta(1)-adrenoceptor.

Artikel i vetenskaplig tidskrift
Författare Reza Mobini
Yvonne Magnusson
G Wallukat
M Viguier
Agneta Hjalmarson
Johan Hoebeke
Publicerad i Journal of autoimmunity
Volym 13
Nummer/häfte 2
Sidor 179-86
ISSN 0896-8411
Publiceringsår 1999
Publicerad vid Wallenberglaboratoriet
Hjärt-kärlinstitutionen
Sidor 179-86
Språk en
Länkar dx.doi.org/10.1006/jaut.1999.0310
Ämnesord Adrenergic beta-Agonists, Amino Acid Sequence, Animals, Animals, Newborn, Antibody Specificity, Autoantibodies, Cardiovascular Diseases, etiology, immunology, Cell Polarity, Cells, Cultured, Humans, Models, Molecular, Molecular Sequence Data, Myocardial Contraction, drug effects, Myocardium, cytology, Peptide Fragments, immunology, Rats, Receptors, Adrenergic, beta-1, immunology, T-Lymphocytes, immunology
Ämneskategorier Mikrobiologi inom det medicinska området

Sammanfattning

The human beta(1)-adrenoceptor is an immune target for autoantibodies with functional activity in cardiovascular diseases. Different epitopes on the extracellular domains of the receptor are involved. To study the immunological and pharmacological properties of these epitopes, rabbits were immunized with peptides corresponding to a large domain in the N-terminal part of the receptor and to its first and second extracellular loops. In contrast to the two other peptides, the first extracellular loop did not have immunogenic properties but acted as a hapten. Antibodies affinity-purified with the three synthetic peptides were able to significantly immunoprecipitate the solubilized receptor, confirming that they recognized the target receptor. While antibodies against the N-terminal domain did not inhibit the binding of a radiolabelled antagonist to the receptor, those against the first and second extracellular loop showed non-competitive inhibition. Similarly, only the two latter antibodies exerted a specific agonist-like effect on the receptor, as assessed on neonatal rat cardiomyocytes in culture. Our results are in accordance with those found for human anti-receptor autoantibodies with functional effects. We conclude that not all extracellular epitopes give rise to functional autoantibodies with potential physiopathological relevance in cardiac diseases with an autoimmune component.

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