Galectin-7 in Epithelial Homeostasis and Carcinomas

Advedissian, Tamara; Deshayes, Frédérique; Viguier, Mireille

doi:10.3390/ijms18122760

Cited by 42 publications

(35 citation statements)

References 122 publications

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“…This difference in structural arrangement suggests that galactin-7 glycoconjugate binding activity may differ from other prototypical ones. So galectin-7 participates in diverse processes such as the susceptibility to apoptosis, cell migration, and cell adhesion and has been in stratified epithelia where it favors epithelial homeostasis [22, 23]. To date, there are no studies demonstrating galectin-7 function in RA.…”

Section: Introductionmentioning

confidence: 99%

Galectin-1, -4, and -7 Were Associated with High Activity of Disease in Patients with Rheumatoid Arthritis

Vilar

Pereira

Dantas

et al. 2019

Autoimmune Diseases

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Background. Due to the variety of functions that galectins (Gal) possess, it is clear that they participate in the pathogenesis of rheumatoid arthritis (RA). Although some studies demonstrate their functions, there is still no correlation with the clinical data of the disease, having the physiological meaning still unknown. Objectives. To compare serum levels of Gal-1, -4, and -7 in patients with RA and healthy controls and to correlate them with clinical parameters. Methods. Serum samples were collected from patients with RA and healthy donors to determine the serum levels of Gal-1, -4, and -7. Results. Serum levels of Gal-1, -4, and -7 were significantly higher in RA patients compared to controls. We evaluated disease activity (CDAI) with serum levels of galectins and found that patients who were high in disease activity had high levels of galectin compared to the moderate activity group. Galectin-4 had higher levels in patients who were in high activity when compared to the group in remission or low activity. Evaluating the activity of the individual disease (DAS28), patients in high individual activity had high levels of Gal-4 when compared to the group in remission or low activity. We also found an association between positive rheumatoid factor and Gal-1 and Gal-4 levels. Conclusion. Our results show for the first time the relationship between serum levels of galectin and the clinical parameters of patients with RA. Demonstrating their role in pathogenesis, new studies with galectins are needed to assess how they function as a biomarker in RA.

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Section: Introductionmentioning

confidence: 99%

Galectin-1, -4, and -7 Were Associated with High Activity of Disease in Patients with Rheumatoid Arthritis

Vilar

Pereira

Dantas

et al. 2019

Autoimmune Diseases

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“…Multiple cellular functions have been attributed to galectin-7, most of which are related to epithelial integrity maintenance. Galectin-7 has been previously implicated in cell migration during re-epithelialization events after corneal or epidermal injury [44] and in promoting invasiveness during cancer progression [45]. Moreover, galectin-7 has been shown to interfere with transforming growth factor-β (TGF-β) signaling in response to hepatocyte growth factor (HGF) by promoting smad3 export from the nucleus and thus preventing liver fibrosis [46].…”

Section: Discussionmentioning

confidence: 99%

Quantitative proteomic characterization of lung tissue in idiopathic pulmonary fibrosis

Tian

Gao

et al. 2019

Clin Proteom

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BackgroundIdiopathic pulmonary fibrosis (IPF) is a progressive, eventually fatal disease. IPF is characterized by excessive accumulation of the extracellular matrix (ECM) in the alveolar parenchyma and progressive lung scarring. The pathogenesis of IPF and whether the ECM involved in the process remain unknown.MethodsTo identify potential treatment target and ECM associated proteins that may be involved in the development of IPF, we employed isobaric tag for relative and absolute quantitation (iTRAQ) combined liquid chromatography–tandem mass spectrometry (LC–MS/MS) approach to examine protein expression in lung tissues from IPF patients.ResultsA total of 662 proteins with altered expression (455 upregulated proteins and 207 downregulated proteins) were identified in lung tissue of IPF patients compared with control. KEGG pathway enrichment analysis showed that the altered proteins in lung tissue mainly belonged to the PI3K-Akt signaling, focal adhesion, ECM-receptor interaction, and carbon metabolism pathways. According to the bioinformatic definition of the matrisome, 229 matrisome proteins were identified in lung tissue. These proteins comprised the ECM of lung, of which 104 were core matrisome proteins, and 125 were matrisome-associated proteins. Of the 229 ECM quantified proteins, 56 significantly differentially expressed proteins (19 upregulated proteins and 37 downregulated proteins) were detected in IPF lung tissue samples. In addition to proteins with well-known functions such as COL1A1, SCGB1A1, TAGLN, PSEN2, TSPAN1, CTSB, AGR2, CSPG2, and SERPINB3, we identified several novel ECM proteins with unknown function deposited in IPF lung tissue including LGALS7, ASPN, HSP90AA1 and HSP90AB1. Some of these differentially expressed proteins were further verified using Western blot analysis and immunohistochemical staining.ConclusionsThis study provides a list of proteomes that were detected in IPF lung tissue by iTRAQ technology combined with LC–MS/MS. The findings of this study will contribute better understanding to the pathogenesis of IPF and facilitate the development of therapeutic targets.Electronic supplementary materialThe online version of this article (10.1186/s12014-019-9226-4) contains supplementary material, which is available to authorized users.

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“…Galectin-7 is a marker of stratified squamous epithelium in the gut and skin [ 21 , 171 , 172 ]. Galectin-7 mRNA is found at all stages of epidermal differentiation, including the proliferative basal and differentiated suprabasal compartments [ 173 ].…”

Section: Galectin-7mentioning

confidence: 99%

The Emerging Role of Galectins and O-GlcNAc Homeostasis in Processes of Cellular Differentiation

Tazhitdinova

Timoshenko

2020

Cells

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Galectins are a family of soluble β-galactoside-binding proteins with diverse glycan-dependent and glycan-independent functions outside and inside the cell. Human cells express twelve out of sixteen recognized mammalian galectin genes and their expression profiles are very different between cell types and tissues. In this review, we summarize the current knowledge on the changes in the expression of individual galectins at mRNA and protein levels in different types of differentiating cells and the effects of recombinant galectins on cellular differentiation. A new model of galectin regulation is proposed considering the change in O-GlcNAc homeostasis between progenitor/stem cells and mature differentiated cells. The recognition of galectins as regulatory factors controlling cell differentiation and self-renewal is essential for developmental and cancer biology to develop innovative strategies for prevention and targeted treatment of proliferative diseases, tissue regeneration, and stem-cell therapy.

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Galectin-7 in Epithelial Homeostasis and Carcinomas

Cited by 42 publications

References 122 publications

Galectin-1, -4, and -7 Were Associated with High Activity of Disease in Patients with Rheumatoid Arthritis

Galectin-1, -4, and -7 Were Associated with High Activity of Disease in Patients with Rheumatoid Arthritis

Quantitative proteomic characterization of lung tissue in idiopathic pulmonary fibrosis

The Emerging Role of Galectins and O-GlcNAc Homeostasis in Processes of Cellular Differentiation

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