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

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Fältnamn	Indikatorer	Metadata
000		03961naa a2200517 4500
001		oai:gup.ub.gu.se/121481
003		SwePub
008		240528s1989 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://gup.ub.gu.se/publication/1214812 URI
040		a (SwePub)gu
041		a eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Magnusson, Yvonne,d 1957u Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine4 aut0 (Swepub:gu)xmagyv
245	1 0	a Antigenic analysis of the second extra-cellular loop of the human beta-adrenergic receptors.
264	1	c 1989
520		a 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.
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Mikrobiologi inom det medicinska området0 (SwePub)301092 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Microbiology in the medical area0 (SwePub)301092 hsv//eng
653		a Antibodies
653		a immunology
653		a Cross Reactions
653		a Epitopes
653		a analysis
653		a Humans
653		a Immunoblotting
653		a Immunoenzyme Techniques
653		a Myocardium
653		a immunology
653		a Peptides
653		a immunology
653		a Receptors
653		a Adrenergic
653		a beta
653		a immunology
700	1	a Höyer, Su Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine4 aut
700	1	a Lengagne, R4 aut
700	1	a Chapot, M P4 aut
700	1	a Guillet, J G4 aut
700	1	a Hjalmarson, Agneta,d 1943u Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine4 aut0 (Swepub:gu)xhjaag
700	1	a Strosberg, A D4 aut
700	1	a Hoebeke, Johanu Gothenburg University,Göteborgs universitet,Medicinska institutionen,Department medicine4 aut
710	2	a Göteborgs universitetb Medicinska institutionen4 org
773	0	t Clinical and experimental immunologyg 78:1, s. 42-8q 78:1<42-8x 0009-9104
856	4 8	u https://gup.ub.gu.se/publication/121481

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Av författaren/redakt...: Magnusson, Yvonn ...; Höyer, S; Lengagne, R; Chapot, M P; Guillet, J G; Hjalmarson, Agne ...; visa fler...; Strosberg, A D; Hoebeke, Johan; visa färre...

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MEDICIN OCH HÄLSOVETENSKAP: MEDICIN OCH HÄLS ...; och Medicinska och f ...; och Mikrobiologi ino ...

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Av lärosätet: Göteborgs universitet

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