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A monoclonal antibody directed against an autoimmune epitope on the human beta1-adrenergic receptor recognized in idiopathic dilated cardiomyopathy.

Artikel i vetenskaplig tidskrift
Författare Reza Mobini
Michael Fu
G Wallukat
Yvonne Magnusson
Åke Hjalmarson
Johan Hoebeke
Publicerad i Hybridoma
Volym 19
Nummer/häfte 2
Sidor 135-42
ISSN 0272-457X
Publiceringsår 2000
Publicerad vid Wallenberglaboratoriet
Hjärt-kärlinstitutionen
Institutionen för invärtesmedicin
Sidor 135-42
Språk en
Länkar dx.doi.org/10.1089/0272457005003117...
Ämnesord 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
Ämneskategorier Fysiologi, Cell- och molekylärbiologi, Mikrobiologi inom det medicinska området

Sammanfattning

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.

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