Anti-inflammatory effect of galectin-1 in a murine model of atopic dermatitis

Corrêa, Maria José Pinheiro; Andrade, F. M.; Gimenes, Alexandre Dantas; Gil, Cristiane Damas

doi:10.1007/s00109-017-1566-9

Cited by 16 publications

(28 citation statements)

References 36 publications

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“…Galectin-1 is a β-galactoside-binding mammalian lectin which has anti-inflammatory features. 44 Galectin-1 attenuates the inflammatory response by reducing neutrophil migration to sites of acute inflammation, 20,45 inhibiting production of nitric oxide by macrophages, 46 preventing adhesion of T cells to extracellular matrix and down-regulating their production of TNF-α 47 and also inducing IL-10…”

Section: Biochemical Resultsmentioning

confidence: 99%

Assessment of saliva and gingival crevicular fluid soluble urokinase plasminogen activator receptor (suPAR), galectin‐1, and TNF‐α levels in periodontal health and disease

Taşdemir

Yılmaz

Narin

et al. 2020

J of Periodontal Research

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Objective The aim of the study is to evaluate saliva and gingival crevicular fluid (GCF) levels of suPAR and galectin‐1 in different periodontal health status and relationship between these molecules and TNF‐α to understand the roles of these molecules in periodontal inflammation process. Background Soluble urokinase plasminogen activator receptor (suPAR) has been described as a biological marker of inflammation and immunological activation. Galectin‐1, a member of the galectin family, is an anti‐inflammatory cytokine. However, to date, levels of these two molecules in periodontal health and disease have not been well documented. Methods A total of 60 individuals, 20 with chronic periodontitis (group P), 20 with gingivitis (group G), and 20 with healthy periodontium (group H) were recruited for this study. Full‐mouth clinical periodontal measurements were recorded in periodontal charts. GCF and whole saliva samples were collected to determine the levels of suPAR, galectin‐1, and TNF‐α in study groups using enzymelinked immunosorbent assay (ELISA) method. Results The GCF total amount of suPAR, galectin‐1, and TNF‐α in GCF was similar in group P and G (P > .05). The GCF total amounts of these molecules in GCF were higher in the group G and P compared to the group H (P < .05), whereas the GCF concentrations of suPAR and galectin‐1 were lower in the group G and P compared to the group H (P < .05).The saliva concentration of suPAR was significantly higher in group P compared to the group G and H (P < .05). It was also higher in the group G compared to the group H but there is no significant difference between the groups (P > .05). Salivary galectin‐1 levels were similar in the study groups (P > .05). Conclusion Increased levels of GCF suPAR, galectin‐1, and saliva suPAR in periodontal disease suggest that these molecules may play a role in the periodontal inflammation. suPAR and galectin‐1 may be considered as potential biomarkers in periodontal disease.

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Section: Biochemical Resultsmentioning

confidence: 99%

Assessment of saliva and gingival crevicular fluid soluble urokinase plasminogen activator receptor (suPAR), galectin‐1, and TNF‐α levels in periodontal health and disease

Taşdemir

Yılmaz

Narin

et al. 2020

J of Periodontal Research

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“…WT and AnxA1 -/- mice were distributed in three experimental groups: Naïve, Sham and AD. On days 0 and 7, animals were immunized with a subcutaneous injection of 5 µg of ovalbumin (OVA, grade C; Sigma-Aldrich, St Louis, MO, USA) and 10 mg/mL of aluminum hydroxide adjuvant diluted in 200 µL of sterile saline according to previous studies [18]. On day 11, animals were shaved and the hair removed from the entire back.…”

Section: Methodsmentioning

confidence: 99%

Lack of Endogenous Annexin A1 Increases Mast Cell Activation and Exacerbates Experimental Atopic Dermatitis

Parisi

Corrêa

Gil

2019

Cells

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Annexin A1 (AnxA1) is a protein with potent anti-inflammatory actions and an interesting target that has been poorly explored in skin inflammation. This work evaluated the lack of endogenous AnxA1 in the progression of ovalbumin (OVA)-induced atopic dermatitis (AD)-like skin lesions. OVA/Alum-immunized C57BL/6 male wild-type (WT) and AnxA1 null (AnxA1-/-) mice were challenged with drops containing OVA on days 11, 14–18 and 21–24. The AnxA1-/- AD group exhibited skin with intense erythema, erosion and dryness associated with increased skin thickness compared to the AD WT group. The lack of endogenous AnxA1 also increased IgE relative to WT animals, demonstrating exacerbation of the allergic response. Histological analysis revealed intense eosinophilia and mast-cell activation in AD animals, especially in AnxA1-/-. Both AD groups increased skin interleukin (IL)-13 levels, while IL-17A was upregulated in AnxA1-/- lymph nodes and mast cells. High levels of phosphorylated ERK were detected in keratinocytes from AD groups. However, phospho-ERK levels were higher in the AnxA1-/- when compared to the respective control groups. Our results suggest AnxA1 as an important therapeutic target for inflammatory skin diseases.

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“…In view of the multifaceted immunoregulatory properties of Gal 1, Correa et al (38) evaluated the possible therapeutic efficacy of intraperitoneally applied recombinant Gal 1 on an ovalbumininduced atopic dermatitis model in BALB/c mice. In Gal 1-treated mice they found that Gal 1 was as effective as dexamethasone in causing clinically evident improvement of skin lesions, reduction in local eotaxin and interferon-gamma levels, suppression of eosinophil and mast cell infiltration, decrease of interleukin 17 plasma levels, activation of signal-regulated kinase, and downregulation of endogenous Gal 1.…”

Section: B Atopic Dermatitismentioning

confidence: 99%

Galectin 1 in dermatology: current knowledge and perspectives

Pasmatzi

Papadionysiou

Monastirli

et al. 2019

Acta Dermatovenerologica Alpina Pannonica Et Adriatica

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Gal 1, the first identified and best-studied prototypical member of the galectin family, is encoded in humans by the LGALS1 gene, which is located on chromosome 22 (q12) (10). It is a noncovalent homodimeric protein with a 14 kDa monomer that contains one CRD and preferentially recognizes galactose-β1-4-N-acetyl-glucosamine sequences on N-or O-linked glycans (11). AbstractGalectins are a family of soluble proteins that are widely distributed in nature and bind to a variety of glycoproteins and glycolipids bearing β-galactoside residues. They are involved in highly important processes at the molecular and cellular level in human cutaneous and extracutaneous tissues, and they exert biological effects of paramount importance through their interaction with cytoplasmic and nuclear proteins and the components of the cell surface and extracellular matrix. Galectin 1 (Gal 1), the first galectin isolated, is a noncovalent homodimeric protein with a 14 kDa monomer that contains one carbohydrate-recognition domain (CRD) and preferentially recognizes galactose-β1-4-N-acetyl-glucosamine sequences on N-or O-linked glycans. Gal 1 occurs intracellularly, extracellularly, and on the cell surface. In the last few years Gal 1 has emerged as a multifaceted protein that exerts a wide spectrum of regulatory effects in diverse normal and abnormal tissues and conditions, indicating a tremendous therapeutic potential. This review summarizes current knowledge on the expression of Gal 1 in normal and diseased human skin, its implications in the pathogenesis, diagnosis, and prognosis of cutaneous disorders, and the novel approach to the treatment of these disorders offered by the use of Gal 1 or its inhibitors/antagonists.

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Anti-inflammatory effect of galectin-1 in a murine model of atopic dermatitis

Cited by 16 publications

References 36 publications

Assessment of saliva and gingival crevicular fluid soluble urokinase plasminogen activator receptor (suPAR), galectin‐1, and TNF‐α levels in periodontal health and disease

Assessment of saliva and gingival crevicular fluid soluble urokinase plasminogen activator receptor (suPAR), galectin‐1, and TNF‐α levels in periodontal health and disease

Lack of Endogenous Annexin A1 Increases Mast Cell Activation and Exacerbates Experimental Atopic Dermatitis

Galectin 1 in dermatology: current knowledge and perspectives

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