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Cancers
Special Issues
Chemerin Signaling in Cancer
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Chemerin Signaling in Cancer

A special issue of Cancers (ISSN 2072-6694). This special issue belongs to the section "Molecular Cancer Biology".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 14710

Special Issue Editors

Prof. Dr. Oliver Treeck

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Guest Editor
Department of Gynecology and Obstetrics I, Molecular Gynecologic Oncology, University Medical Center Regensburg, Caritas KH St. Josef, 93053 Regensburg, Germany
Interests: hormone-dependent cancer; tumors of the breast; ovary and endometrium; estrogen receptor signaling; estrogen receptor; G-protein coupled estrogen receptor 1; transcriptome analysis
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Christa Büchler

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Guest Editor
Department of Internal Medicine I, University Hospital Regensburg, Regensburg, Germany
Interests: adipose tissue; obesity; non-alcoholic fatty liver disease; adiponectin; chemerin
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues,

Increasing evidence demonstrates a role of the adipokine chemerin in cancer. Chemerin has been reported to exert both antitumoral and tumor-promoting effects. In the majority of tumor diseases, present data suggest a tumor-suppressing function of chemerin, whereas in other cancer types, this adipokine was reported to exert adverse effects. Chemerin blocks tumor growth by recruiting innate immune cells and inactivation of tumor promoting signaling molecules. Activation of these molecules by chemerin contributes to tumor growth. Chemerin binds to the receptors CMKLR1, GPR1, and CCRL2. To date, few studies have addressed downstream signaling of these receptors in cancer cells. Thus, further attempts are needed to elucidate the molecular mechanisms underlying the role of chemerin and its receptors in different cancer types, which would also be able to explain the presence of tissue-specific effects. With this Special Issue, we would like to shed light on novel findings on chemerin signaling in cancer. To address this topic, we will welcome original publications or state-of the art reviews on signaling pathways affected by chemerin in cancer cells of different origin.

Prof. Dr. Oliver Treeck
Prof. Dr. Christa Büchler
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cancers is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • cancer
  • chemerin
  • chemerin receptors
  • signaling

Published Papers (6 papers)

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Editorial

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3 pages, 186 KiB  
Editorial
Chemerin Signaling in Cancer
by Oliver Treeck and Christa Buechler
Cancers 2020, 12(11), 3085; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers12113085 - 22 Oct 2020
Cited by 6 | Viewed by 1805
Abstract
The multifunctional adipokine chemerin exerts key functions in inflammation, adipogenesis and glucose homeostasis [...] Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)

Research

Jump to: Editorial

21 pages, 4607 KiB  
Article
Anti-Tumoral Effect of Chemerin on Ovarian Cancer Cell Lines Mediated by Activation of Interferon Alpha Response
by Meike Schmitt, Johanna Gallistl, Susanne Schüler-Toprak, Jürgen Fritsch, Christa Buechler, Olaf Ortmann and Oliver Treeck
Cancers 2022, 14(17), 4108; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers14174108 - 25 Aug 2022
Cited by 7 | Viewed by 1765
Abstract
The pleiotropic adipokine chemerin affects tumor growth primarily as anti-tumoral chemoattractant inducing immunocyte recruitment. However, little is known about its effect on ovarian adenocarcinoma. In this study, we examined chemerin actions on ovarian cancer cell lines in vitro and intended to elucidate involved [...] Read more.
The pleiotropic adipokine chemerin affects tumor growth primarily as anti-tumoral chemoattractant inducing immunocyte recruitment. However, little is known about its effect on ovarian adenocarcinoma. In this study, we examined chemerin actions on ovarian cancer cell lines in vitro and intended to elucidate involved cell signaling mechanisms. Employing three ovarian cancer cell lines, we observed differentially pronounced effects of this adipokine. Treatment with chemerin (huChem-157) significantly reduced OVCAR-3 cell numbers (by 40.8% on day 6) and decreased the colony and spheroid growth of these cells by half. The spheroid size of SK-OV-3 ovarian cancer cells was also significantly reduced upon treatment. Transcriptome analyses of chemerin-treated cells revealed the most notably induced genes to be interferon alpha (IFNα)-response genes like IFI27, OAS1 and IFIT1 and their upstream regulator IRF9 in all cell lines tested. Finally, we found this adipokine to elevate IFNα levels about fourfold in culture medium of the employed cell lines. In conclusion, our data for the first time demonstrate IFNα as a mediator of chemerin action in vitro. The observed anti-tumoral effect of chemerin on ovarian cancer cells in vitro was mediated by the notable activation of IFNα response genes, resulting from the chemerin-triggered increase of secreted levels of this cytokine. Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)
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17 pages, 3683 KiB  
Article
A Chemerin Peptide Analog Stimulates Tumor Growth in Two Xenograft Mouse Models of Human Colorectal Carcinoma
by Justa Friebus-Kardash, Petra Schulz, Sandy Reinicke, Cordula Karthaus, Quirino Schefer, Sebastian Bandholtz and Carsten Grötzinger
Cancers 2022, 14(1), 125; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers14010125 - 28 Dec 2021
Cited by 6 | Viewed by 2321
Abstract
Background: Chemerin plasma concentration has been reported to be positively correlated with the risk of colorectal cancer. However, the potential regulation of CRC tumorigenesis and progression has not yet been investigated in an experimental setting. This study addresses this hypothesis by investigating proliferation, [...] Read more.
Background: Chemerin plasma concentration has been reported to be positively correlated with the risk of colorectal cancer. However, the potential regulation of CRC tumorigenesis and progression has not yet been investigated in an experimental setting. This study addresses this hypothesis by investigating proliferation, colony formation, and migration of CRC cell lines in vitro as well as in animal models. Methods: In vitro, microscopic assays to study proliferation, as well as a scratch-wound assay for migration monitoring, were applied using the human CRC cell lines HCT116, HT29, and SW620 under the influence of the chemerin analog CG34. The animal study investigated HCT116-luc and HT29-luc subcutaneous tumor size and bioluminescence during treatment with CG34 versus control, followed by an ex-vivo analysis of vessel density and mitotic activity. Results: While the proliferation of the three CRC cell lines in monolayers was not clearly stimulated by CG34, the chemerin analog promoted colony formation in three-dimensional aggregates. An effect on cell migration was not observed. In the treatment study, CG34 significantly stimulated both growth and bioluminescence signals of HCT116-luc and HT29-luc xenografts. Conclusions: The results of this study represent the first indication of a tumor growth-stimulating effect of chemerin signaling in CRC. Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)
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23 pages, 9599 KiB  
Article
Expression of CCRL2 Inhibits Tumor Growth by Concentrating Chemerin and Inhibiting Neoangiogenesis
by Diana Al Delbany, Virginie Robert, Ingrid Dubois-Vedrenne, Annalisa Del Prete, Maxime Vernimmen, Ayoub Radi, Anne Lefort, Frédérick Libert, Valérie Wittamer, Silvano Sozzani and Marc Parmentier
Cancers 2021, 13(19), 5000; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers13195000 - 05 Oct 2021
Cited by 10 | Viewed by 2544
Abstract
CCRL2 belongs to the G protein-coupled receptor family and is one of the three chemerin receptors. It is considered as a non-signaling receptor, presenting chemerin to cells expressing the functional chemerin receptor ChemR23/CMKLR1 and possibly GPR1. In the present work, we investigate the [...] Read more.
CCRL2 belongs to the G protein-coupled receptor family and is one of the three chemerin receptors. It is considered as a non-signaling receptor, presenting chemerin to cells expressing the functional chemerin receptor ChemR23/CMKLR1 and possibly GPR1. In the present work, we investigate the role played by CCRL2 in mouse cancer models. Loss of function of Ccrl2 accelerated the development of papillomas in a chemical model of skin carcinogenesis (DMBA/TPA), whereas the growth of B16 and LLC tumor cell grafts was delayed. Delayed tumor growth was also observed when B16 and LLC cells overexpress CCRL2, while knockout of Ccrl2 in tumor cells reversed the consequences of Ccrl2 knockout in the host. The phenotypes associated with CCRL2 gain or loss of function were largely abrogated by knocking out the chemerin or Cmklr1 genes. Cells harboring CCRL2 could concentrate bioactive chemerin and promote the activation of CMKLR1-expressing cells. A reduction of neoangiogenesis was observed in tumor grafts expressing CCRL2, mimicking the phenotype of chemerin-expressing tumors. This study demonstrates that CCRL2 shares functional similarities with the family of atypical chemokine receptors (ACKRs). Its expression by tumor cells can significantly tune the effects of the chemerin/CMKLR1 system and act as a negative regulator of tumorigenesis. Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)
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15 pages, 3032 KiB  
Article
Cyclic Derivatives of the Chemerin C-Terminus as Metabolically Stable Agonists at the Chemokine-like Receptor 1 for Cancer Treatment
by Tobias F. Fischer, Anne S. Czerniak, Tina Weiß, Tristan Zellmann, Lina Zielke, Sylvia Els-Heindl and Annette G. Beck-Sickinger
Cancers 2021, 13(15), 3788; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers13153788 - 27 Jul 2021
Cited by 8 | Viewed by 2369
Abstract
Chemerin is a small chemotactic protein and a modulator of the innate immune system. Its activity is mainly mediated by the chemokine-like receptor 1 (CMKLR1), a receptor expressed by natural killer cells, dendritic cells, and macrophages. Downregulation of chemerin is part of the [...] Read more.
Chemerin is a small chemotactic protein and a modulator of the innate immune system. Its activity is mainly mediated by the chemokine-like receptor 1 (CMKLR1), a receptor expressed by natural killer cells, dendritic cells, and macrophages. Downregulation of chemerin is part of the immune evasion strategy exploited by several cancer types, including melanoma, breast cancer, and hepatocellular carcinoma. Administration of chemerin can potentially counteract these effects, but synthetically accessible, metabolically stable analogs are required. Other tumors display overexpression of CMKLR1, offering a potential entry point for targeted delivery of chemotherapeutics. Here, we present cyclic derivatives of the chemerin C-terminus (chemerin-9), the minimal activation sequence of chemerin. Chemerin-9 derivatives that were cyclized through positions four and nine retained activity while displaying full stability in blood plasma for more than 24 h. Therefore, these peptides could be used as a drug shuttle system to target cancer cells as demonstrated here by methotrexate conjugates. Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)
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16 pages, 2700 KiB  
Article
Chemerin Is Induced in Non-Alcoholic Fatty Liver Disease and Hepatitis B-Related Hepatocellular Carcinoma
by Elisabeth M. Haberl, Susanne Feder, Rebekka Pohl, Lisa Rein-Fischboeck, Kerstin Dürholz, Laura Eichelberger, Josef Wanninger, Thomas S. Weiss and Christa Buechler
Cancers 2020, 12(10), 2967; https://0-doi-org.brum.beds.ac.uk/10.3390/cancers12102967 - 13 Oct 2020
Cited by 15 | Viewed by 2283
Abstract
Chemerin is protective in experimental models of hepatocellular carcinoma (HCC). Noteworthy, chemerin mRNA and protein were reduced in HCC tissues of Asian patients with mostly hepatitis B disease etiology. The current study nevertheless showed that chemerin protein was induced in tumor tissues of [...] Read more.
Chemerin is protective in experimental models of hepatocellular carcinoma (HCC). Noteworthy, chemerin mRNA and protein were reduced in HCC tissues of Asian patients with mostly hepatitis B disease etiology. The current study nevertheless showed that chemerin protein was induced in tumor tissues of European HCC patients with non-alcoholic fatty liver disease (NAFLD) and patients with unclear disease etiology. A similar regulation was observed in hepatitis B virus (HBV), but not in hepatitis C virus (HCV), related HCC. The apparent discrepancy between the regulation of chemerin in HBV-HCC obtained from our study and recent reports led us to use the chemerin antibodies applied in the previous assays. These antibodies could not equally detect different chemerin isoforms, which were overexpressed in HepG2 cells. Higher chemerin protein in HCC was nevertheless confirmed by the use of all antibodies. Chemerin protein was low in Huh7 and PLC/PRF/5 cells whereas HepG2 and Hep3B cells had chemerin protein similar as primary human hepatocytes. Besides, the anti-tumor effects of retinoids in hepatocyte cell lines did not enclose upregulation of chemerin, which was initially discovered as a tazarotene induced protein in the skin. Finally, protein levels of the chemerin receptor, chemokine-like receptor 1 (CMKLR1), declined in non-viral, and tended to be lower in HBV-HCC tissues suggesting reduced chemerin activity in the tumors. To sum up, our work showed an opposite regulation of chemerin and CMKLR1 in NAFLD and HBV associated HCC. In HCV-HCC neither chemerin nor its receptor were changed in the tumor tissues. Current findings do not support a critical role of total chemerin protein levels in HCC of non-viral and viral etiology. Accordingly, tumor-localized chemerin protein was not associated with tumor-node-metastasis classification. Full article
(This article belongs to the Special Issue Chemerin Signaling in Cancer)
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