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

• 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.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Physiology (hsv//eng)

Nyckelord

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

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)