Amino acids 327-350 of the human C5a-receptor are not essential for [125I]C5a binding in COS cells and signal transduction in Xenopus oocytes

A. Klos; C. Mätje; C. Rheinheimer; W. Bautsch; J. Köhl; U. Martin; M. Burg

doi:10.1016/0014-5793(94)00350-5

Amino acids 327-350 of the human C5a-receptor are not essential for [¹²⁵I]C5a binding in COS cells and signal transduction in Xenopus oocytes

A. Klos^*, C. Mätje, C. Rheinheimer, W. Bautsch, J. Köhl, U. Martin, M. Burg

^*Corresponding author for this work

Institute of Systemic Inflamation Research

Hannover Medical School

9 Citations (Scopus)

Abstract

The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a-receptor (hC5aR) mutants with truncation of its cytosolic carboxyl-terminus (C-terminus). Both mutants were analysed for C5a-binding in transiently expressing COS cells, and one mutant additionally for GTP-binding regulatory protein (G-protein) coupling in cRNA-injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C-terminus are necessary for proper receptor folding or expression and (b) the receptor C-terminus distal from position 327 is not critical for receptor expression, folding, binding and G-protein coupling.

Original language	English
Journal	FEBS Letters
Volume	344
Issue number	1
Pages (from-to)	79-82
Number of pages	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(94)00350-5
Publication status	Published - 09.05.1994

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title = "Amino acids 327-350 of the human C5a-receptor are not essential for [125I]C5a binding in COS cells and signal transduction in Xenopus oocytes",

abstract = "The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a-receptor (hC5aR) mutants with truncation of its cytosolic carboxyl-terminus (C-terminus). Both mutants were analysed for C5a-binding in transiently expressing COS cells, and one mutant additionally for GTP-binding regulatory protein (G-protein) coupling in cRNA-injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C-terminus are necessary for proper receptor folding or expression and (b) the receptor C-terminus distal from position 327 is not critical for receptor expression, folding, binding and G-protein coupling.",

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T1 - Amino acids 327-350 of the human C5a-receptor are not essential for [125I]C5a binding in COS cells and signal transduction in Xenopus oocytes

AU - Klos, A.

AU - Mätje, C.

AU - Rheinheimer, C.

AU - Bautsch, W.

AU - Köhl, J.

AU - Martin, U.

AU - Burg, M.

PY - 1994/5/9

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N2 - The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a-receptor (hC5aR) mutants with truncation of its cytosolic carboxyl-terminus (C-terminus). Both mutants were analysed for C5a-binding in transiently expressing COS cells, and one mutant additionally for GTP-binding regulatory protein (G-protein) coupling in cRNA-injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C-terminus are necessary for proper receptor folding or expression and (b) the receptor C-terminus distal from position 327 is not critical for receptor expression, folding, binding and G-protein coupling.

AB - The anaphylatoxic peptide C5a is an important inflammatory mediator of the complement system. We have generated human C5a-receptor (hC5aR) mutants with truncation of its cytosolic carboxyl-terminus (C-terminus). Both mutants were analysed for C5a-binding in transiently expressing COS cells, and one mutant additionally for GTP-binding regulatory protein (G-protein) coupling in cRNA-injected Xenopus oocytes. Our data suggest that (a) amino acids (aa) 314 to 326 as part of the C-terminus are necessary for proper receptor folding or expression and (b) the receptor C-terminus distal from position 327 is not critical for receptor expression, folding, binding and G-protein coupling.

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Amino acids 327-350 of the human C5a-receptor are not essential for [¹²⁵I]C5a binding in COS cells and signal transduction in Xenopus oocytes

Abstract

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