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Chemerin – exploring a versatile adipokine

  • Tobias F. Fischer and Annette G. Beck-Sickinger ORCID logo EMAIL logo
Published/Copyright: January 18, 2022

Abstract

Chemerin is a small chemotactic protein and a key player in initiating the early immune response. As an adipokine, chemerin is also involved in energy homeostasis and the regulation of reproductive functions. Secreted as inactive prochemerin, it relies on proteolytic activation by serine proteases to exert biological activity. Chemerin binds to three distinct G protein-coupled receptors (GPCR), namely chemokine-like receptor 1 (CMKLR1, recently named chemerin1), G protein-coupled receptor 1 (GPR1, recently named chemerin2), and CC-motif chemokine receptor-like 2 (CCRL2). Only CMKLR1 displays conventional G protein signaling, while GPR1 only recruits arrestin in response to ligand stimulation, and no CCRL2-mediated signaling events have been described to date. However, GPR1 undergoes constitutive endocytosis, making this receptor perfectly adapted as decoy receptor. Here, we discuss expression pattern, activation, and receptor binding of chemerin. Moreover, we review the current literature regarding the involvement of chemerin in cancer and several obesity-related diseases, as well as recent developments in therapeutic targeting of the chemerin system.


Corresponding author: Annette G. Beck-Sickinger, Institute of Biochemistry, University of Leipzig, Brüderstraße 34, D-04103 Leipzig, Germany, E-mail:

Award Identifier / Grant number: 209933838 – SFB1052 – Z05

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: This study was financially supported by the Deutsche Forschungsgemeinschaft (DFG), German Research Foundation, project number 209933838 – SFB1052 – Z05.

  3. Conflict of interest statement: The authors declare no competing financial interests.

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Received: 2021-11-06
Accepted: 2021-12-23
Published Online: 2022-01-18
Published in Print: 2022-06-27

© 2022 Walter de Gruyter GmbH, Berlin/Boston

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