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

10 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.",

author = "A. Klos and C. M{\"a}tje and C. Rheinheimer and W. Bautsch and J. K{\"o}hl and U. Martin and M. Burg",

year = "1994",

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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

Y1 - 1994/5/9

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.

UR - https://www.scopus.com/pages/publications/0028267458

U2 - 10.1016/0014-5793(94)00350-5

DO - 10.1016/0014-5793(94)00350-5

M3 - Journal articles

C2 - 8181569

AN - SCOPUS:0028267458

SN - 0014-5793

VL - 344

SP - 79

EP - 82

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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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