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Göteborgs universitets publikationer

Characterization of anti-peptide antibodies directed against an extracellular immunogenic epitope on the human alpha 1-adrenergic receptor.

Författare och institution:
Michael Fu (Wallenberglaboratoriet); G Wallukat (-); Åke Hjalmarson (Wallenberglaboratoriet); Johan Hoebeke (-)
Publicerad i:
Clinical and experimental immunology, 97 ( 1 ) s. 146-51
Artikel, refereegranskad vetenskaplig
Sammanfattning (abstract):
A synthetic peptide corresponding to amino acids 192-218 of the second extracellular loop of the human alpha 1A-adrenergic receptor was used to raise antibodies in rabbits. Affinity-purified antibodies specifically recognized main bands with a molecular weight of about 68, 40 and 37 kD on the electrotransferred membrane proteins of rat ventricle membranes. The incubation of these antibodies with rat myocardial membranes resulted in a decrease in the number of binding sites for the specific radiolabelled alpha 1-antagonist prazosin. These antibodies were also able to mimic the effects of agonist stimulation as demonstrated by a positive chronotropic effect on cultured cardiomyocytes. These results constitute the first immunochemical evidence of the presence of both the A and B subtypes of the alpha 1-adrenergic receptor in the heart. They also confirm that the second extracellular loop of the alpha 1-adrenergic receptors is an immunologically and functionally important domain.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
Medicinska grundvetenskaper ->
Amino Acid Sequence, Animals, Antibodies, isolation & purification, Cells, Cultured, Cricetinae, Epitopes, chemistry, genetics, Heart Rate, immunology, Humans, Immunochemistry, Membrane Proteins, chemistry, genetics, immunology, Molecular Sequence Data, Myocardium, immunology, metabolism, Peptide Fragments, chemical synthesis, genetics, immunology, Protein Conformation, Rabbits, Rats, Receptors, Adrenergic, alpha-1, chemistry, genetics, immunology, Sequence Homology, Amino Acid, Species Specificity
Postens nummer:
Posten skapad:
2007-10-31 21:35
Posten ändrad:
2011-01-20 09:59

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