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Antigenic analysis of the second extra-cellular loop of the human beta-adrenergic receptors.

Magnusson, Yvonne, 1957 (författare)
Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine
Höyer, S (författare)
Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine
Lengagne, R (författare)
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Chapot, M P (författare)
Guillet, J G (författare)
Hjalmarson, Agneta, 1943 (författare)
Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine
Strosberg, A D (författare)
Hoebeke, Johan (författare)
Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine
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 (creator_code:org_t)
1989
1989
Engelska.
Ingår i: Clinical and experimental immunology. - 0009-9104. ; 78:1, s. 42-8
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • Polyclonal antibodies were raised in rabbits by immunization with free peptides corresponding to positions 197-222 of the human beta 1-adrenergic receptor (beta 1 peptide) and the corresponding sequence (172-197) of the human beta 2-adrenergic receptor (beta 2 peptide). While the beta 2 peptide yielded antibodies that cross-reacted with the beta 1 peptide, the antibodies against the beta 1 peptide did not cross-react with the beta 2 sequence. Cross-reactivity of the anti-beta 2 peptide antibodies and the selectivity of the anti-beta 1 peptide antibodies were also revealed in the recognition by immunoblots of the beta 1- and beta 2-adrenergic receptors of different species or of the receptor gene products expressed in a bacterial vector. These antibodies could be used immunohistochemically to visualize the beta-adrenergic receptors on rabbit heart. The anti-beta 2 peptide antibodies did not show any functional effect on the beta-adrenergic receptors; the anti-beta 1 peptide antibodies were able to displace agonist affinity to higher values. Recognition of truncated peptides by the anti-beta 1 and anti-beta 2 peptide antibodies suggested that the cross-reaction of the anti-beta 2 peptide antibodies was due to the recognition of a common epitope on the C-terminal part of the peptides. The anti-beta 1 peptide antibodies recognized the N-terminal part of the peptide better than the C-terminal part. These results suggest that the second extracellular loop postulated in the structure of the human beta-adrenergic receptor contains the T and B cell epitopes necessary for induction of an immune response. The selectivity and the functional properties of the antibodies raised against that loop in the beta 1 adrenergic receptor could have relevance in induction of auto antibodies in certain cardiomyopathic conditions.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Nyckelord

Antibodies
immunology
Cross Reactions
Epitopes
analysis
Humans
Immunoblotting
Immunoenzyme Techniques
Myocardium
immunology
Peptides
immunology
Receptors
Adrenergic
beta
immunology

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ref (ämneskategori)
art (ämneskategori)

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