An anti-inflammatory function for the complement anaphylatoxin C5a-binding protein, C5L2

Norma P. Gerard, Bao Lu, Pixu Liu, Stewart Craig, Yuko Fujiwara, Shoji Okinaga, Craig Gerard

Research output: Contribution to journalArticle

144 Citations (Scopus)

Abstract

C5L2 is an enigmatic serpentine receptor that is co-expressed with the C5a receptor on many cells including polymorphonuclear neutrophils. The apparent absence of coupling of C5L2 with G proteins suggests that this receptor may modulate the biological activity of C5a, perhaps by acting as a decoy receptor. Alternatively, C5L2 may affect C5a function through formation of a heteromeric complex with the C5aR, or it may utilize a G protein-independent signaling pathway. Here we show that in mice bearing a targeted deletion of C5L2, the biological activity of C5a/C5adesArg is enhanced both in vivo and in vitro. The biological role of C5L2 thus appears to be limiting to the pro-inflammatory response to the anaphylatoxin. Accordingly, up-regulation of C5L2 may be of benefit in inflammatory states driven by C5a, including sepsis, asthma, cystic fibrosis, and chronic obstructive lung disease.

Original languageEnglish
Pages (from-to)39677-39680
Number of pages4
JournalJournal of Biological Chemistry
Volume280
Issue number48
DOIs
Publication statusPublished - 2005 Dec 2

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Gerard, N. P., Lu, B., Liu, P., Craig, S., Fujiwara, Y., Okinaga, S., & Gerard, C. (2005). An anti-inflammatory function for the complement anaphylatoxin C5a-binding protein, C5L2. Journal of Biological Chemistry, 280(48), 39677-39680. https://doi.org/10.1074/jbc.C500287200