Correction: Chemerin Is an Antimicrobial Agent in Human Epidermis

Banas, Magdalena; Zabieglo, Katarzyna; Kasetty, Gopinath; Kapińska-Mrowiecka, Monika; Borowczyk, Julia; Drukała, Justyna; Murzyn, Krzysztof; Zabel, Brian A.; Butcher, Eugene C.; Schroeder, Johann O.; Schmidtchen, Artur; Cichy, Joanna

doi:10.1371/annotation/4dfd522c-f0fd-40db-aadc-44cbef367a40

Cited by 18 publications

(11 citation statements)

References 16 publications

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“…Consistent with its role as an adipokine, evidence from clinical and animal studies have firmly established that secretion and circulating levels of chemerin increase with adiposity and decline after bariatric surgery, diet, and exercise-based weight loss [26,27,28,29,30,31,32,33,34,35]. In addition to adipose tissue, chemerin is highly expressed in many other human tissues including the adrenals, liver, female reproductive organs, mammary tissue, and lung (Data Source: GTEx Analysis Release V7 (dbGaP, Accession phs000424.v7.p2, accessed on 29 July 2019)) as well as cell types such as intestinal epithelial cells, platelets, keratinocytes, synovial fibroblasts, and vascular endothelial cells [36,37,38,39,40]. Therefore, when assessing a role for this adipokine in cancer, the impact of chemerin produced locally within the affected tissue and/or tumor microenvironment must be considered in addition to systemic levels of circulating chemerin.…”

Section: Chemerinmentioning

confidence: 99%

More Than an Adipokine: The Complex Roles of Chemerin Signaling in Cancer

Goralski

Jackson

McKeown

et al. 2019

IJMS

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Chemerin is widely recognized as an adipokine, with diverse biological roles in cellular differentiation and metabolism, as well as a leukocyte chemoattractant. Research investigating the role of chemerin in the obesity–cancer relationship has provided evidence both for pro- and anti-cancer effects. The tumor-promoting effects of chemerin primarily involve direct effects on migration, invasion, and metastasis as well as growth and proliferation of cancer cells. Chemerin can also promote tumor growth via the recruitment of tumor-supporting mesenchymal stromal cells and stimulation of angiogenesis pathways in endothelial cells. In contrast, the majority of evidence supports that the tumor-suppressing effects of chemerin are immune-mediated and result in a shift from immunosuppressive to immunogenic cell populations within the tumor microenvironment. Systemic chemerin and chemerin produced within the tumor microenvironment may contribute to these effects via signaling through CMKLR1 (chemerin1), GPR1 (chemerin2), and CCLR2 on target cells. As such, inhibition or activation of chemerin signaling could be beneficial as a therapeutic approach depending on the type of cancer. Additional studies are required to determine if obesity influences cancer initiation or progression through increased adipose tissue production of chemerin and/or altered chemerin processing that leads to changes in chemerin signaling in the tumor microenvironment.

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Section: Chemerinmentioning

confidence: 99%

More Than an Adipokine: The Complex Roles of Chemerin Signaling in Cancer

Goralski

Jackson

McKeown

et al. 2019

IJMS

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“…Chemerin is secreted as prochemerin from various cell types and then cleaved into bioactive isoforms by specific proteases [2]. Chemerin is also considered to function as an antimicrobial agent in the epidermis, an angiogenic factor in endothelial cells, and an adipokine that regulates adipogenesis and energy metabolism in adipocytes [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Chemerin Treatment Inhibits the Growth and Bone Invasion of Breast Cancer Cells

Kim

Lee

Song

et al. 2020

IJMS

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Chemerin is secreted as prochemerin from various cell types and then cleaved into the bioactive isoform by specific proteases. In various cancer types, chemerin exhibits pro- or antitumor effects. In the present study, chemerin treatment significantly inhibited the viability and invasion of breast cancer cells in the absence or presence of transforming growth factor (TGF)-β and insulin-like growth factor (IGF)-1. The expression levels of E-cadherin and vimentin were reduced in chemerin-treated breast cancer cells. However, chemerin treatment recovered the reduced E-cadherin expression level in breast cancer cells treated with TGF-β or IGF-1. Chemerin treatment inhibited nuclear β-catenin levels in breast cancer cells stimulated with or without TGF-β or IGF-1. In addition, chemerin treatment blocked the increase in the receptor activator of nuclear factor kappa-Β ligand (RANKL)/osteoprotegerin (OPG) ratio in osteoblastic cells exposed to metastatic breast cancer cell-derived conditioned medium. Chemerin treatment inhibited RANKL-induced osteoclast formation and bone resorption by reducing the secretion of matrix metalloproteinase (MMP)-2, MMP-9, and cathepsin K. Intraperitoneal administration of chemerin inhibited tumor growth in MCF-7 breast cancer cell-injected mice and reduced the development of osteolytic lesions resulting from intratibial inoculation of MDA-MB-231 cells. Taken together, chemerin inhibits the growth and invasion of breast cancer cells and prevents bone loss resulting from breast cancer cells by inhibiting finally osteoclast formation and activity.

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“…Furthermore, experimental evidence suggests that inflammatory mediators such as interleukin 1β (IL-1β), tumor necrosis factor alpha (TNFα), interferon γ (IFNγ) and lipopolysaccharide (LPS) induce chemerin expression by adipocytes, hepatocytes and epithelial cells [ 9 , 18 , 19 ]. Finally, chemerin has been shown to exert antimicrobial properties, inhibiting bacterial growth after activation by host-derived, as well as pathogen-derived proteases [ 20 , 21 , 22 , 23 , 24 ].…”

Section: Introductionmentioning

confidence: 99%

Circulating Chemerin and Its Kinetics May Be a Useful Diagnostic and Prognostic Biomarker in Critically Ill Patients with Sepsis: A Prospective Study

et al. 2022

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Chemerin, a novel adipokine, is a potent chemoattractant molecule with antimicrobial properties, implicated in immune responses. Our aim was to investigate circulating chemerin and its kinetics, early in sepsis in critically ill patients and its association with severity and prognosis. Serum chemerin was determined in a cohort of 102 critically ill patients with sepsis during the first 48 h from sepsis onset and one week later, and in 102 age- and gender-matched healthy controls. Patients were followed for 28 days and their outcomes were recorded. Circulating chemerin was significantly higher in septic patients at onset compared to controls (342.3 ± 108.1 vs. 200.8 ± 40.1 μg/L, p < 0.001). Chemerin decreased significantly from sepsis onset to one week later (342.3 ± 108.1 vs. 308.2 ± 108.5 μg/L, p < 0.001), but remained higher than in controls. Chemerin was higher in patients presenting with septic shock than those with sepsis (sepsis onset: 403.2 ± 89.9 vs. 299.7 ± 99.5 μg/L, p < 0.001; one week after: 374.9 ± 95.3 vs. 261.6 ± 91.9 μg/L, p < 0.001), and in nonsurvivors than survivors (sepsis onset: 427.2 ± 96.7 vs. 306.9 ± 92.1 μg/L, p < 0.001; one week after: 414.1 ± 94.5 vs. 264.2 ± 79.9 μg/L, p < 0.001). Moreover, patients with septic shock and nonsurvivors, presented a significantly lower absolute and relative decrease in chemerin one week after sepsis onset compared to baseline (p < 0.001). Based on ROC curve analyses, the diagnostic performance of chemerin (AUC 0.78, 95% CI 0.69–0.87) was similar to C-reactive protein (CRP) (AUC 0.78, 95% CI 0.68–0.87) in discriminating sepsis severity. However, increased chemerin at sepsis onset and one week later was an independent predictor of 28-day mortality (sepsis onset: HR 3.58, 95% CI 1.48–8.65, p = 0.005; one week after: HR 10.01, 95% CI 4.32–23.20, p < 0.001). Finally, serum chemerin exhibited significant correlations with the severity scores, white blood cells, lactate, CRP and procalcitonin, as well as with biomarkers of glucose homeostasis, but not with cytokines and soluble urokinase-type plasminogen activator receptor (suPAR). Circulating chemerin is increased early in sepsis and its kinetics may have diagnostic and prognostic value in critically ill patients. Further studies are needed to shed light on the role of chemerin in sepsis.

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Correction: Chemerin Is an Antimicrobial Agent in Human Epidermis

Cited by 18 publications

References 16 publications

More Than an Adipokine: The Complex Roles of Chemerin Signaling in Cancer

More Than an Adipokine: The Complex Roles of Chemerin Signaling in Cancer

Chemerin Treatment Inhibits the Growth and Bone Invasion of Breast Cancer Cells

Circulating Chemerin and Its Kinetics May Be a Useful Diagnostic and Prognostic Biomarker in Critically Ill Patients with Sepsis: A Prospective Study

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