Characterization of the C5a Receptor on Guinea Pig Platelets

Titus Kretzschmar; Kai Kahl; Katja Rech; Wilfried Bautsch; Jörg Köhl; Dieter Bitter-Suermann

doi:10.1016/S0171-2985(11)80526-7

Characterization of the C5a Receptor on Guinea Pig Platelets

Titus Kretzschmar^*, Kai Kahl, Katja Rech, Wilfried Bautsch, Jörg Köhl, Dieter Bitter-Suermann

^*Corresponding author for this work

Hannover Medical School

15 Citations (Scopus)

Abstract

Guinea pig (gp) platelets react to nanomolar doses of the complement-derived anaphylatoxin C5a with a shape change, aggregation and release of biogenic amines and nucleotides from their granules. We have investigated the specific receptor for C5a on gp platelets which mediates these biological effects. Competitive binding studies with ¹²⁵I-labeled guinea pig C5a ¹²⁵I-gpC5a) revealed approx. 4000 binding sites/cell with K_d = 6 x 10^-9 M. The more than 60-fold higher biological activity (ATP-release from gp platelets) of gpC5a versus recombinant human C5a (rhuC5a) and the different binding behavior of gpC5a and rhuC5a point to a species restriction in the gp platelet system. Cross-linking of ¹²⁵I-gpC5a to gp platelets (250 μM DSS) and analysis by SDS-PAGE under reducing conditions resulted in labeling of a single band with a molecular mass of 32 kDa (ligand-receptor complex). Because of these characteristics, the C5a receptor on gp platelets clearly differs from all previously described C5a receptors.

Original language	English
Journal	Immunobiology
Volume	183
Issue number	5
Pages (from-to)	418-432
Number of pages	15
ISSN	0171-2985
DOIs	https://doi.org/10.1016/S0171-2985(11)80526-7
Publication status	Published - 01.11.1991

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title = "Characterization of the C5a Receptor on Guinea Pig Platelets",

abstract = "Guinea pig (gp) platelets react to nanomolar doses of the complement-derived anaphylatoxin C5a with a shape change, aggregation and release of biogenic amines and nucleotides from their granules. We have investigated the specific receptor for C5a on gp platelets which mediates these biological effects. Competitive binding studies with 125I-labeled guinea pig C5a 125I-gpC5a) revealed approx. 4000 binding sites/cell with Kd = 6 x 10-9 M. The more than 60-fold higher biological activity (ATP-release from gp platelets) of gpC5a versus recombinant human C5a (rhuC5a) and the different binding behavior of gpC5a and rhuC5a point to a species restriction in the gp platelet system. Cross-linking of 125I-gpC5a to gp platelets (250 μM DSS) and analysis by SDS-PAGE under reducing conditions resulted in labeling of a single band with a molecular mass of 32 kDa (ligand-receptor complex). Because of these characteristics, the C5a receptor on gp platelets clearly differs from all previously described C5a receptors.",

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AU - Kretzschmar, Titus

AU - Kahl, Kai

AU - Rech, Katja

AU - Bautsch, Wilfried

AU - Köhl, Jörg

AU - Bitter-Suermann, Dieter

PY - 1991/11/1

Y1 - 1991/11/1

N2 - Guinea pig (gp) platelets react to nanomolar doses of the complement-derived anaphylatoxin C5a with a shape change, aggregation and release of biogenic amines and nucleotides from their granules. We have investigated the specific receptor for C5a on gp platelets which mediates these biological effects. Competitive binding studies with 125I-labeled guinea pig C5a 125I-gpC5a) revealed approx. 4000 binding sites/cell with Kd = 6 x 10-9 M. The more than 60-fold higher biological activity (ATP-release from gp platelets) of gpC5a versus recombinant human C5a (rhuC5a) and the different binding behavior of gpC5a and rhuC5a point to a species restriction in the gp platelet system. Cross-linking of 125I-gpC5a to gp platelets (250 μM DSS) and analysis by SDS-PAGE under reducing conditions resulted in labeling of a single band with a molecular mass of 32 kDa (ligand-receptor complex). Because of these characteristics, the C5a receptor on gp platelets clearly differs from all previously described C5a receptors.

AB - Guinea pig (gp) platelets react to nanomolar doses of the complement-derived anaphylatoxin C5a with a shape change, aggregation and release of biogenic amines and nucleotides from their granules. We have investigated the specific receptor for C5a on gp platelets which mediates these biological effects. Competitive binding studies with 125I-labeled guinea pig C5a 125I-gpC5a) revealed approx. 4000 binding sites/cell with Kd = 6 x 10-9 M. The more than 60-fold higher biological activity (ATP-release from gp platelets) of gpC5a versus recombinant human C5a (rhuC5a) and the different binding behavior of gpC5a and rhuC5a point to a species restriction in the gp platelet system. Cross-linking of 125I-gpC5a to gp platelets (250 μM DSS) and analysis by SDS-PAGE under reducing conditions resulted in labeling of a single band with a molecular mass of 32 kDa (ligand-receptor complex). Because of these characteristics, the C5a receptor on gp platelets clearly differs from all previously described C5a receptors.

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Characterization of the C5a Receptor on Guinea Pig Platelets

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