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The Role of Chemerin in Human Disease—2nd Edition

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A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Cell Biology and Pathology".

Deadline for manuscript submissions: 31 March 2025 | Viewed by 11100

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Prof. Dr. Christa Buechler

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Department of Internal Medicine I, Regensburg University Hospital, 93053 Regensburg, Germany
Interests: adipose tissue; obesity; sepsis; inflammatory bowel disease; chemerin
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Dear Colleagues,

This Special Issue, entitled “The Role of Chemerin in Human Disease”, will focus on the selection of recent research topics and up-to-date review articles focusing on the role of chemerin in disease.

Chemerin is a well-characterized adipokine which has multiple functions. Adipose tissue and serum levels are increased in the obese, and chemerin plays a significant role in adipogenesis and glucose homeostasis. The C-terminal processing of chemerin generates biologically active isoforms and, moreover, contributes to chemerin inactivation. Different chemerin isoforms have been identified, but their particular physiological functions remain mostly unknown. Chemerin isoform tissue distribution, signalling pathways, and biological activities require further investigation.

There is emerging evidence that chemerin is an important molecule in various cancers. Leukocyte recruitment via this chemoattractant mostly leads to the suppression of tumor growth, while chemerin-induced angiogenesis is one of its tumor-promoting activities. Chemerin has already been described as a major factor in various diseases, such as coronary artery disease, hypertension, Alzheimer´s disease, and chronic obstructive pulmonary disease.

With this Special Issue of Biomedicines, we aim to collect articles which clarify the pathophysiological role of chemerin in human diseases. Articles investigating chemerin’s role as a biomarker in human diseases are also welcome. Moreover, we invite authors to write review articles providing a comprehensive and critical overview of the current literature.

Prof. Dr. Christa Buechler
Guest Editor

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Keywords

biomarker
chemotaxis
cardiovascular diseases
cancer
chemerin isoforms
CMKLR1
GPR1
CCRL2

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The Role of Chemerin in Human Disease in Biomedicines (9 articles)

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Research

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16 pages, 4153 KiB

Open AccessArticle

Metabolic Activity in Human Intermuscular Adipose Tissue Directs the Response of Resident PPARγ⁺ Macrophages to Fatty Acids

by Xiaoying Chen, Sebastian Ludger Schubert, Aline Müller, Miguel Pishnamaz, Frank Hildebrand and Mahtab Nourbakhsh

Biomedicines 2025, 13(1), 10; https://doi.org/10.3390/biomedicines13010010 - 25 Dec 2024

Viewed by 3985

Abstract

Background/Objectives: Peroxisome proliferator-activated receptor gamma (PPARγ) is a fatty acid-binding transcription activator of the adipokine chemerin. The key role of PPARγ in adipogenesis was established by reports on adipose tissue-resident macrophages that express PPARγ. The present study examined PPARγ⁺ macrophages in human skeletal muscle tissues, their response to fatty acid (FA) species, and their correlations with age, obesity, adipokine expression, and an abundance of other macrophage phenotypes. Methods: An ex vivo human skeletal muscle model with surgical specimens that were maintained without or with FAs for up to 11 days was utilized. Immunofluorescence analysis was used to detect macrophage phenotypes and mitochondrial activity. Preconfigured arrays were used to detect the expression of 34 different adipokines and chemokines. Results: Data from 14 adults revealed that PPARγ⁺ macrophages exclusively reside in intermuscular adipose tissue (IMAT), and their abundance correlates with the metabolic status of surrounding adipocytes during tissue maintenance in vitro for 9–11 days. Elevated fatty acid levels lead to significant increases in PPARγ⁺ populations, which are correlated with the donor’s body mass index (BMI). Conclusions: PPARγ⁺ macrophages represent a distinctly specialized population of regulatory cells that reside within human IMATs in accordance with their metabolic status. Thus, future in-depth studies on IMAT-resident PPARγ⁺ macrophage action mechanisms will elucidate the role of skeletal muscle in the pathogenesis of human metabolic dysfunction. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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Figure 1
Representative images of skeletal muscle tissue (HE) and IMATs (IF). All images were obtained from Participant P6. (a) HE image showing the human skeletal muscle tissue comprising the areas of SMFs (red arrowhead) and IMATs (green arrowhead). The scale bar (lower right) indicates 1000 µm. (b) IF images were obtained after costaining with DAPI and secondary antibodies as negative controls (negative-488 or 594). The scale bars (upper left) indicate 50 µm. (c–i) IF images of IMATs after costaining with primary antibodies against designated human markers (white, lower left) and the corresponding secondary antibodies and DAPI. The small panels on the left side represent magnified single-cell images labeled with dashed line circles in larger images using IgG488 (green), IgG594 (red), and DAPI (blue) filters. DAPI and IgG594 or DAPI and IgG488 were merged (Merge) to determine the specificity of the detected signals. The white arrowheads indicate verified positive macrophages. The scale bars (upper left) indicate 50 µm. Full article ">Figure 2
PPARγ+ macrophages exclusively reside in IMATs. (a) Representative images from a skeletal muscle tissue slice from P2 after IF staining using a primary antibody against PPARγ, IgG488-labeled secondary antibody, and DAPI. The image of brightfield microscopy (middle panel) comprises skeletal muscle fibers (left) and intermuscular adipose tissue with adipocytes (right). Magnified IF images show the labeled areas of skeletal muscle fibers (upper left panel) and intermuscular adipose tissue (lower right panel) exposing a PPARγ+ macrophage (white arrowhead), respectively. (b) The diagram shows the mean number of PPARγ+ macrophages (y-axis) in the IMAT and SMF fields of 0.24 mm2 (x-axis) in donor tissue samples (n = 14). (c) The diagram shows the mean number of PPARγ+ macrophages (y-axis) relative to 1 mm2 of IMATs (left y-axis) or relative to the number of adipocytes in 1 mm2 of IMATs in donor tissue samples (n = 14). The Mann–Whitney test was used to assess the significance of differences in the number of PPARγ+ macrophages between SMFs and IMATs. p ≤ 0.0001 (****). Full article ">Figure 3
The numbers of CD80+ and CD11c+ macrophages correlate with adipocyte VDAC1 expression in the IMATs of donor samples. Pearson correlation analyses were employed to determine the relationships between the mean VDAC1 expression levels and the mean numbers of CD80+ (a) and CD11c+ (b) macrophages in 0.24 mm2 of IMATs from the donors (n = 14). The correlation coefficients (r) and significance levels (p) for the relationships are presented at the top right of each diagram. Full article ">Figure 4
The expression levels of IL-23 and IL-31 correlate with adipocyte VDAC1 expression in the IMATs of donor samples. Spearman’s rank correlation analyses were employed to determine the relationships between mean VDAC1 and IL-23 (a) or IL-31 (b) expression levels (n = 12). The correlation coefficients (r) and significance levels (p) for the relationships are presented at the top right of each diagram. Full article ">Figure 5
Dynamics of the PPARγ+ macrophage population in IMATs during maintenance in vitro. (a) The diagram shows the mean number of PPARγ+ macrophages (y-axis) in 0.24 mm2 of IMAT from all participants (n = 14) before (pre, white bar) and after (post, gray bars) tissue maintenance in vitro. (b) The diagram shows the mean expression of VDAC1 and COXIV (y-axis) in 0.24 mm2 of IMAT from all participants (n = 14) before (pre, white bars) and after (post, gray bars) tissue maintenance in vitro. A paired t-test or Wilcoxon signed-rank test was applied to evaluate the significance of differences before and after cultivation. p ≤ 0.01 (**). (c,d) Spearman’s rank correlation analyses were applied to determine the relationships between the mean number of PPARγ+ macrophages and the mean number of CD163+ (c) or the expression level of COXIV (d) in 0.24 mm2 of IMAT from all donors (n = 14). The correlation coefficients (r) and significance levels (p) for the relationships are presented at the top right of each diagram. Full article ">Figure 6
Dynamics of the PPARγ+ macrophage population in IMATs in response to S-FAs and U-FAs during maintenance in vitro. (a) The diagram shows the relative fold change in PPARγ+ macrophage numbers (y-axis) in 0.24 mm2 of IMAT from all participants (n = 14) in response to U-FA or S-FAs before (x-axis) in vitro culture. (b) The diagram shows the relative fold change in the expression of VDAC1 (y-axis) in 0.24 mm2 of IMAT from all participants (n = 14) in response to U-FA or S-FAs before (x-axis) in vitro culture. One-sample t-tests or Wilcoxon signed-rank tests were used to assess the significance of differences before and after cultivation. p ≤ 0.05 (*). (c,d) Pearson correlation and Spearman’s rank correlation analyses were employed to determine the relationships between the S-FA-mediated relative fold change in the number of PPARγ+ macrophages ((c), y-axis) or the relative fold change in the expression of VDAC1 ((d), y-axis) and donor BMI (n = 14). The correlation coefficients (r) and significance levels (p) for the relationships are presented at the top right of each diagram. Full article ">

17 pages, 2470 KiB

Open AccessArticle

A Cross-Sectional Study: Systematic Quantification of Chemerin in Human Cerebrospinal Fluid

by Alexandra Höpfinger, Manuel Behrendt, Andreas Schmid, Thomas Karrasch, Andreas Schäffler and Martin Berghoff

Biomedicines 2024, 12(11), 2508; https://doi.org/10.3390/biomedicines12112508 - 1 Nov 2024

Cited by 1 | Viewed by 1014

Abstract

Background: Dysregulation of adipokines is considered a key mechanism of chronic inflammation in metabolic syndrome. Some adipokines affect food intake by crossing the blood/brain barrier. The adipokine chemerin is associated with metabolic syndrome, cardiovascular diseases and immune response. Little is known about chemerin’s presence in cerebrospinal fluid (CSF) and its ability to cross the blood/CSF barrier. Methods: We quantified chemerin levels in paired serum and CSF samples of 390 patients with different neurological diagnoses via enzyme-linked immunosorbent assay (ELISA). Correlation analyses of serum and CSF chemerin levels with anthropometric, serum and CSF routine parameters were performed. Results: Overweight patients exhibited higher chemerin levels in serum and CSF. Chemerin CSF levels were higher in men. Chemerin levels in serum were associated with BMI (body mass index) and CRP (C-reactive protein). Chemerin levels in CSF were associated with age. Neurological diseases affected chemerin levels in CSF. The chemerin CSF/serum ratio was calculated as 96.3 ± 36.8 × 10⁻³ for the first time. Conclusions: Our data present a basis for the development of standard values for chemerin quantities in CSF. CSF chemerin levels are differentially regulated in neurological diseases and affected by BMI and sex. Chemerin is able to cross the blood/CSF barrier under physiological and pathophysiological conditions. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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13 pages, 1486 KiB

Open AccessArticle

Chemerin Levels in COVID-19 Are More Affected by Underlying Diseases than by the Virus Infection Itself

by Vlad Pavel, Pablo Amend, Niklas Schmidtner, Alexander Utrata, Charlotte Birner, Stephan Schmid, Sabrina Krautbauer, Martina Müller, Patricia Mester and Christa Buechler

Biomedicines 2024, 12(9), 2099; https://doi.org/10.3390/biomedicines12092099 - 14 Sep 2024

Viewed by 1050

Abstract

Background/Objectives: Chemerin is an adipokine involved in inflammatory and metabolic diseases, and its circulating levels have been associated with inflammatory parameters in various patient cohorts. Severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) infection, which causes COVID-19, triggers inflammatory pathways. However, the association between serum chemerin levels and COVID-19 disease severity and outcomes has not been definitively established. Methods: In this study, serum chemerin levels were analyzed in 64 patients with moderate COVID-19 and 60 patients with severe disease. Results: The results showed that serum chemerin levels were comparable between these two groups and slightly higher than in healthy controls. Notably, COVID-19 patients with hypertension exhibited elevated serum chemerin levels, while those with liver cirrhosis had lower levels. When patients with these comorbidities were excluded from the analyses, serum chemerin levels in COVID-19 patients were similar to those in healthy controls. Positive correlations were observed between serum chemerin levels and markers such as alkaline phosphatase, C-reactive protein, eosinophils, and lymphocytes in the entire cohort, as well as in the subgroup excluding patients with hypertension and cirrhosis. Additionally, urinary chemerin levels were comparable between COVID-19 patients and controls, and neither hypertension nor dialysis significantly affected urinary chemerin levels. Both survivors and non-survivors had similar serum and urinary chemerin levels. Conclusions: In conclusion, this study suggests that comorbidities such as arterial hypertension and liver cirrhosis do have a more significant impact on serum chemerin levels than SARS-CoV-2 infection itself. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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Review

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29 pages, 673 KiB

Open AccessReview

Chemerin and Polycystic Ovary Syndrome: A Comprehensive Review of Its Role as a Biomarker and Therapeutic Target

by Stefano Palomba, Giuseppe Seminara, Flavia Costanzi, Donatella Caserta and Antonio Aversa

Biomedicines 2024, 12(12), 2859; https://doi.org/10.3390/biomedicines12122859 - 16 Dec 2024

Viewed by 1087

Abstract

Background: Chemerin, an adipokine implicated in inflammatory, metabolic, and adipogenic processes, has been detected in high serum concentration in women with polycystic ovary syndrome (PCOS) and seems to play a role in PCOS pathogenesis. Moreover, at present, no comprehensive and critical document is available in the literature on this topic. The aim of the current study was to comprehensively review the latest available data to confirm the evidence about the association between chemerin and PCOS, highlighting its potential role as an upcoming biomarker and therapeutic target. Methods: A search in the literature of studies published between 2019 and 2024 was conducted using PubMed, Cochrane Library, and Web of Science, focusing on research related to chemerin, PCOS, and PCOS-related features, comorbidities, and complications. A qualitative structured synthesis of key findings was performed according to the specific thematic areas selected, including and discussing clinical data on women with PCOS and experimental studies in humans and animal models of PCOS. Results: Available data confirm increased serum levels of chemerin in women with PCOS compared with controls, independent of obesity and body mass index. Chemerin is associated with insulin resistance, hyperandrogenism, and ovarian dysfunction in PCOS individuals, inhibiting folliculogenesis and steroidogenesis. Experimental animal models underscore chemerin’s regulatory roles through its receptors within the hypothalamic–pituitary–ovarian axis and peripheral tissues. High systemic levels of chemerin in PCOS may also be related to the increased risk of pregnancy complications, especially gestational diabetes mellitus and preeclampsia. Conclusions: The current review study highlights the role of chemerin in PCOS pathophysiology, severity, and associated comorbidities and complications, assessing its value as a future biomarker and foreshadowing its potential as a therapeutic target. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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17 pages, 3415 KiB

Open AccessReview

Structural Basis for Chemerin Recognition and Signaling Through Its Receptors

by Yezhou Liu, Aijun Liu and Richard D. Ye

Biomedicines 2024, 12(11), 2470; https://doi.org/10.3390/biomedicines12112470 - 28 Oct 2024

Viewed by 1527

Abstract

Chemerin is a chemotactic adipokine that participates in a multitude of physiological processes, including adipogenesis, leukocyte chemotaxis, and neuroinflammation. Chemerin exerts biological functions through binding to one or more of its G protein-coupled receptors (GPCRs), namely chemokine-like receptor 1 (CMKLR1), G protein-coupled receptor 1 (GPR1), and CC-motif receptor-like 2 (CCRL2). Of these receptors, CMKLR1 and GPR1 have been confirmed as signaling receptors of chemerin, whereas CCRL2 serves as a chemerin-binding protein without transmembrane signaling. High-resolution structures of two chemerin receptors are now available thanks to recent advancements in structure biology. This review focuses on the structural perspectives of the chemerin receptors with an emphasis on the structure–activity correlation, including key components of the two receptors for ligand recognition and conformational changes induced by chemerin and its derivative peptides for G protein activation. There are also comparisons between the two chemerin receptors and selected GPCRs with peptide ligands for better appreciation of the shared and distinct features of the chemerin receptors in ligand recognition and transmembrane signaling, and in the evolution of this subclass of GPCRs. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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Figure 1
Chemerin, chemerin-derived peptides, and their receptors. Upper panel, chemerin and its derived C-terminal peptides. The N-terminal signal peptide (a.a. −21 to −1) is marked in orange. The mature form of chemerin (a.a. 1–137) is marked in teal blue. The selected C-terminal peptides of chemerin are listed. Lower panel, schematic illustration of the 3 chemerin receptors and their downstream signaling pathways. Chemerin binding to CMKLR1 elicits balanced responses of the G protein and β-arrestin signaling pathways. The C-terminal nonapeptide of chemerin (C9) induces G protein-dependent signaling through CMKLR1. GPR1 is activated by chemerin and its C9 peptide with a β-arrestin bias. Chemerin ligands bind to CCRL2 but do not induce downstream signaling. Full article ">Figure 2
CMKLR1 recognition of chemerin and its C9 peptide. (A) Superimposed structures of the two solved C9-CMKLR1 complexes (PDB ID: 7YKD and 8SG1). The C9 peptide and CMKLR1 in the 7YKD structure are shown as yellow and cyan, respectively. The C9 peptide and CMKLR1 in the 8SG1 structure are shown as orange and blue, respectively. (B) Enlarged view of the ligand binding pocket and the interactions with the C9 peptide in the two solved structures shown above. CMKLR1 residues interacting with the ligand are marked using the Ballesteros–Weinstein numbering scheme [<a href="#B46-biomedicines-12-02470" class="html-bibr">46</a>]. The C9 peptide (Y129-S137) corresponds to the last 9 residues of the mature chemerin. (C) Comparison of the heterotrimeric Gi protein binding poses in the two C9-CMKLR1-Gi complexes. The G⍺i, Gβ, and Gγ subunits in the 7YKD structure are colored as grass green, blue-grey and purple, respectively. The G⍺i, Gβ, and Gγ subunits in the 8SG1 structure are colored as yellow, sky blue and pink, respectively. A red arrow indicates a downward movement of the heterotrimeric Gi proteins in the 8SG1 structure compared to the 7YKD structure. (D) The interaction between the full-length mature chemerin and GPR1. The full-length mature chemerin (numbered as 1-137, shown in dark pink) uses its C-terminus to insert into the transmembrane binding pocket of GPR1 (shown in purple blue). Interacting residues are shown as sticks and labeled. The 5 interaction sites (IS1-IS5) are highlighted in red boxes with dashed lines in the left panel. The panels in the right depict details of IS1 (chemerin N-terminal core interacting with GPR1 N-terminus), IS2 (chemerin interacting with ECL2 of GPR1) and IS3 (chemerin interacting with ECL3 of GPR1). (E) IS4 indicates chemerin Y129-A135 interacting with residues at the opening of the transmembrane pocket of GPR1. (F) IS5 depicts interactions of F136-S137 of chemerin with residues at the bottom of the GPR1 ligand binding pocket. Full article ">Figure 3
Agonist-induced activation of chemerin receptors. (A) Overall structural comparison between C9-bound active state CMKLR1 (PDB ID: 7YKD, blue) and inactive C5aR (PDB ID: 6C1R, light yellow) structures. Receptor conformational changes of CMKLR1 to an active state are marked with red arrows. (B) Upon agonist binding, the “toggle switch” W6.48 shows a downward orientation, further resulting in an outward movement of TM6 for an active receptor conformation. (C) Conformational changes at the P5.50-I/V3.40-F6.44 motif towards an active state GPCR conformation. Orientations of residue conformations are highlighted by red arrows. (D) Conformational changes at the D3.49-R3.50-Y3.51 motif for G protein activation. An upward rotation of R3.50 is highlighted by a red arrow. The red dashed line indicates the polar interaction between R3.50 and Y5.58 that secures the active receptor conformation for G protein binding. (E) C9-bound CMKLR1 (blue) interacting with the α subunit (teal) of the heterotrimeric Gi protein. Interacting residues are shown as sticks. (F) Comparison of the extent of W6.48 downward movement. C5aR in its inactive state is shown in pale yellow, GPR1 bound to chemerin (PDB ID: 8XGM) is shown in cyan, and CMKLR1 binding to C9 is shown in purple blue. W6.48 orients downwards to a greater extent in CMKLR1 than in GPR1. (G) C9-bound GPR1 (cyan) interacting with the α subunit (teal) of the heterotrimeric Gi protein (PDB ID: 8JJP). Interacting residues are shown as sticks. (H) Binding of C9 to CMKLR1 (blue) and GPR1 (cyan), respectively. The C9 bound to CMKLR1 is shown in orange, and C9 bound to GPR1 is shown in lime yellow. C9 binds deeper in the transmembrane binding pocket of CMKLR1 than in GPR1. Full article ">Figure 4
Phylogenetic analysis of the chemerin receptors, complement receptors, formyl peptide receptors, and chemokine receptors. Chemerin receptors are highlighted with blue color. The phylogenetic tree is rooted at C3aR. The graphical illustration of the tree was created using iTOL v6.9.1 [<a href="#B52-biomedicines-12-02470" class="html-bibr">52</a>]. Full article ">Figure 5
Comparison of ligand recognition of the chemerin receptors and other GPCRs. (A) Schematic illustration of the binding of chemerin to GPR1 (left, PDB ID: 8XGM) and chemokine CXCL12 to CXCR4 (right, PDB ID: 8K3Z, receptor N-terminus is reconstructed using AlphaFold and MD simulations). (B) The binding mode of C-terminus-in ligands, C9 to CMKLR1 (left, PDB ID: 7YKD), C3a to C3aR (middle, PDB ID: 8HK2) and C5a to C5aR (right, PDB ID: 7Y64), respectively. The C-terminal ends of the ligands show an “S” shape binding pose in the receptor transmembrane binding pocket. (C) Ligand recognition modes of peptide agonists to GPCRs. The C9 peptide bound to CMKLR1 is colored in light green (PDB ID: 7YKD) as a reference for comparison. Angiotensin II bound to AT1R is colored in dark forest green (left, PDB ID: 6OS0), bradykinin bound to the type 2 bradykinin receptor is colored in pink (middle, PDB ID: 7F2O) and α-MSH bound to melanocortin-1 receptor is colored in purple (right, PDB ID: 7F4D). Full article ">

16 pages, 506 KiB

Open AccessReview

Chemerin in the Spotlight: Revealing Its Multifaceted Role in Acute Myocardial Infarction

by Andreas Mitsis, Elina Khattab, Michael Myrianthefs, Stergios Tzikas, Nikolaos P. E. Kadoglou, Nikolaos Fragakis, Antonios Ziakas and George Kassimis

Biomedicines 2024, 12(9), 2133; https://doi.org/10.3390/biomedicines12092133 - 20 Sep 2024

Cited by 2 | Viewed by 1284

Abstract

Chemerin, an adipokine known for its role in adipogenesis and inflammation, has emerged as a significant biomarker in cardiovascular diseases, including acute myocardial infarction (AMI). Recent studies have highlighted chemerin’s involvement in the pathophysiological processes of coronary artery disease (CAD), where it modulates inflammatory responses, endothelial function, and vascular remodelling. Elevated levels of chemerin have been associated with adverse cardiovascular outcomes, including increased myocardial injury, left ventricular dysfunction, and heightened inflammatory states post-AMI. This manuscript aims to provide a comprehensive review of the current understanding of chemerin’s role in AMI, detailing its molecular mechanisms, clinical implications, and potential as a biomarker for diagnosis and prognosis. Additionally, we explore the therapeutic prospects of targeting chemerin pathways to mitigate myocardial damage and improve clinical outcomes in AMI patients. By synthesizing the latest research findings, this review seeks to elucidate the multifaceted role of chemerin in AMI and its promise as a target for innovative therapeutic strategies. Full article

(This article belongs to the Special Issue The Role of Chemerin in Human Disease—2nd Edition)

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