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Identification of Functional Protein Regions Through Chimeric Protein Construction
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Chemerin reveals its chimeric nature.

Teizo Yoshimura1, Joost J Oppenheim

  • 1Laboratory of Molecular Immunoregulation, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA. yoshimut@mail.nih.gov

The Journal of Experimental Medicine
|September 24, 2008
PubMed
Summary
This summary is machine-generated.

Chemerin, a pro-inflammatory protein, binds to ChemR23/CMKLR1 and CCRL2 receptors, influencing immune cell movement. This protein may play a dual role in both initiating and resolving inflammation.

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Area of Science:

  • Immunology
  • Biochemistry
  • Cell Biology

Background:

  • Chemerin is a pro-inflammatory plasma protein.
  • It binds to the G protein-coupled receptor (GPCR) ChemR23/CMKLR1.
  • This interaction occurs on macrophages and plasmacytoid dendritic cells, promoting chemotaxis.

Purpose of the Study:

  • To identify additional receptors for chemerin.
  • To elucidate the role of chemerin in inflammatory processes.
  • To explore the potential dual role of chemerin in inflammation initiation and resolution.

Main Methods:

  • Receptor binding assays.
  • Cellular chemotaxis assays.
  • Analysis of chemerin-derived peptides.

Main Results:

  • CCRL2 was identified as an additional receptor for chemerin.
  • Chemerin binding to CCRL2 provides a novel mechanism for enhancing inflammation.
  • Chemerin-derived peptides exhibit anti-inflammatory properties.

Conclusions:

  • Chemerin interacts with both ChemR23/CMKLR1 and CCRL2.
  • The identification of CCRL2 expands our understanding of chemerin's role in inflammation.
  • Chemerin may be implicated in both the initiation and resolution phases of inflammation.