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C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor

C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor The molecular cloning of the C5a receptor places this molecule in the superfamily of G-protein coupled receptors. This superfamily is charac­ terized by the presence of signature motifs including seven hydrophobic domains which span the cell membrane and impart a predicted serpentine topology to the receptor proteins. The identification of other members of this family, including receptors for the chemokines IL-8 and Mip-l /Rantes, thrombin, formyl peptide, and platelet activating factor, provide new tools for understanding structure­ function relationships relevant to the inflammatory process. This review focuses on the recent biological studies concerning the ligand C5a and its cellular receptor, the structure/activity relationships so far discerned, signal transduction mechanisms, progress toward identification of receptor antagonists, and some likely directions for future studies. Where appro­ priate, relevant work on related seven transmembrane segment receptors is discussed. PERSPECTIVES tegies Complex organisms have evolved a number of cellular and humoral stra­ of host defense (1, 2). Conceptually, these strategies each include 775 0732-0582/94/0410-0775$05.00 GERARD & GERARD ligand molecules which reflect a change in state and receptor/effector molecules that initiate local or global responses to the signal. Ligand molecules advertising a change in state may be derived from the host (e.g. cytokines, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

C5A Anaphylatoxin and Its Seven Transmembrane-Segment Receptor

Gerard, C; Gerard, N P
Annual Review of Immunology , Volume 12 (1) – Apr 1, 1994
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Publisher
Annual Reviews
Copyright
Copyright 1994 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev.iy.12.040194.004015
pmid
8011297
Publisher site
See Article on Publisher Site

Abstract

The molecular cloning of the C5a receptor places this molecule in the superfamily of G-protein coupled receptors. This superfamily is charac­ terized by the presence of signature motifs including seven hydrophobic domains which span the cell membrane and impart a predicted serpentine topology to the receptor proteins. The identification of other members of this family, including receptors for the chemokines IL-8 and Mip-l /Rantes, thrombin, formyl peptide, and platelet activating factor, provide new tools for understanding structure­ function relationships relevant to the inflammatory process. This review focuses on the recent biological studies concerning the ligand C5a and its cellular receptor, the structure/activity relationships so far discerned, signal transduction mechanisms, progress toward identification of receptor antagonists, and some likely directions for future studies. Where appro­ priate, relevant work on related seven transmembrane segment receptors is discussed. PERSPECTIVES tegies Complex organisms have evolved a number of cellular and humoral stra­ of host defense (1, 2). Conceptually, these strategies each include 775 0732-0582/94/0410-0775$05.00 GERARD & GERARD ligand molecules which reflect a change in state and receptor/effector molecules that initiate local or global responses to the signal. Ligand molecules advertising a change in state may be derived from the host (e.g. cytokines,

Journal

Annual Review of Immunology – Annual Reviews

Published: Apr 1, 1994

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