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

FEBS Letters

Mätje, C.¹  Rheinheimer, C.¹  Burg, M.¹  Martin, U.¹  Bautsch, W.¹  Klos, A.¹  Köhl, J.¹ 

[1] Institut für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Konstanty-Gutschowstr. 8, D-30625 Hannover, Germany

关键词: C5a;    C5a-receptor;    Anaphylatoxin;    Complement;    G-protein;    Xenopus;   

DOI  :  10.1016/0014-5793(94)00350-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown