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A monoclonal antibo...
A monoclonal antibody directed against an autoimmune epitope on the human beta1-adrenergic receptor recognized in idiopathic dilated cardiomyopathy.
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- Mobini, Reza, 1965 (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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- Fu, Michael, 1963 (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Institutionen för invärtesmedicin,Wallenberg Laboratory,Institute of Internal Medicine
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Wallukat, G (author)
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- Magnusson, Yvonne, 1957 (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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- Hjalmarson, Åke, 1937 (author)
- Gothenburg University,Göteborgs universitet,Hjärt-kärlinstitutionen,Wallenberglaboratoriet,Cardiovascular Institute,Wallenberg Laboratory
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- Hoebeke, Johan (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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(creator_code:org_t)
- Mary Ann Liebert Inc, 2000
- 2000
- English.
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In: Hybridoma. - : Mary Ann Liebert Inc. - 0272-457X. ; 19:2, s. 135-42
- Related links:
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https://doi.org/10.1...
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Abstract
Subject headings
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- A monoclonal antibody (MAb M16) was obtained by immunizing Balb/C mice with free peptide H26R, corresponding to the second extracellular loop of the human beta1-adrenergic receptor (beta1AR), against which functional autoantibodies have been detected in patients with idiopathic dilated cardiomyopathy. The MAb was found to be of IgG2b type and directed against a conformational epitope, encompassing the sequence recognized by the human autoantibodies. BIAcore measurements yielded an equilibrium constant of 6.5 X 10(7) M1 with an association rate constant (kon) of 6.5 X 10(4) M(-1) sec(-1) and a dissociation rate constant (koff) of 1.0 X 10(-3) sec(-1). It immunoprecipitated only poorly the solubilized beta1AR of Sf9 cell membranes. Functionally, the MAb was capable of not only reducing the number of the maximal binding sites to the beta1-adrenergic receptor of transfected Sf9 cell membranes, but also of displaying a positive chronotropic effect on cultured neonatal rat cardiomyocytes. These properties, which the MAb shares with the human autoantibodies, makes it an interesting tool for passive transfer studies in mice.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
- 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)
Keyword
- Amino Acid Sequence
- Animals
- Animals
- Newborn
- Antibodies
- Monoclonal
- chemistry
- immunology
- Antibody Affinity
- Autoantigens
- immunology
- Cardiomyopathy
- Dilated
- immunology
- Cells
- Cultured
- Epitope Mapping
- Heart Rate
- Humans
- Hybridomas
- Immunoglobulin G
- analysis
- Mice
- Mice
- Inbred BALB C
- immunology
- Molecular Sequence Data
- Myocardium
- cytology
- Peptides
- immunology
- Precipitin Tests
- Rats
- Rats
- Wistar
- Receptors
- Adrenergic
- beta-1
- genetics
- immunology
- Spodoptera
- genetics
- Transfection
Publication and Content Type
- ref (subject category)
- art (subject category)
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