Galectin-7, a marker of all types of stratified epithelia

2 ABSTRACT.We have investigated the expression and role of galectin-1 and other galectins in psoriasis and in the Th1/Th17 effector and dendritic cell responses associated with this chronic inflammatory skin condition. To determine differences between psoriasis patients and healthy donors, galectins expression was analyzed by RT-PCR assays in skin samples and specifically on epidermal and peripheral blood dendritic cells by immunofluorescence and flow cytometry.In skin of healthy donors galectins 1, 3 and 9 were expressed in a high proportion of Langerhans cells. Also, galectins were differentially expressed in peripheral blood dendritic cell subsets; galectin-1 and galectin-9 were highly expressed in peripheral myeloid dendritic cells compared with plasmacytoid dendritic cells. We found that non-lesional as well as lesional skin samples from psoriasis patients had low levels of galectin-1 at mRNA and protein level in parallel with low levels of IL-10 mRNA compared with skin from healthy patients. However, only lesional skin samples expressed high levels of

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“…2A). Gal-3 and gal-7, a galectin characteristic of keratinocytes [21], were highly expressed on epidermal keratinocytes (Fig. 2A).…”

Section: Gal-1 Gal-3 and Gal-9 Are Expressed In Langerhans Cellsmentioning

confidence: 97%

Psoriasis in humans is associated with down‐regulation of galectins in dendritic cells

Fuente

Pérez‐Gala

Bonay

et al. 2012

The Journal of Pathology

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“…To find out whether this inhibitory effect is intrinsic to galectin-3, heat-inactivated galectin-3 preparations and galectin-7, a prototype galectin bearing only CRD, 35 were also assessed in vitro culture system. Neither heat-inactivated galectin-3 nor galectin-7 inhibited osteoclastogenesis (Figure 3b and c), strongly suggesting that the observed inhibitory effects on osteoclastogenesis are an intrinsic property of galectin-3.…”

Section: Inhibition Of Osteoclast Formation By Galectin-3mentioning

confidence: 99%

A possible suppressive role of galectin-3 in upregulated osteoclastogenesis accompanying adjuvant-induced arthritis in rats

Kukita

Teramachi

et al. 2009

Laboratory Investigation

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Galectin-3 is a b-galactoside-binding animal lectin having pleiotropic effects on cell growth, differentiation, and apoptosis. This lectin has been shown to be involved in phagocytosis by macrophages and in inflammation. Here we investigated an involvement of galectin-3 in the regulatory process of inflammatory bone resorption in rats with adjuvant-induced arthritis (AA rats) accompanying severe bone destruction in the ankle joints. The protein level of galectin-3 in the ankle-joint extracts was markedly augmented at week 3 after adjuvant injection, at the time when severe bone destruction was observed. Immunohistochemical analysis revealed an extremely high expression of galectin-3 in macrophages and granulocytes infiltrated in the area of severe bone destruction. To estimate the role of galectin-3 in osteoclastogenesis and osteoclastic bone resorption, recombinant galectin-3 was added to in vitro culture systems. Galectin-3 markedly inhibited the formation of osteoclasts in cultures of murine osteoclast precursor cell line as well as in rat bone marrow culture systems. This inhibition was not observed by heat-inactivated galectin-3 or by galectin-7. Although recombinant galectin-3 did not affect signaling through mitogen-activated protein kinase (MAPK) or nuclear factor-kB (NF-kB), it specifically suppressed the induction of nuclear factor of activated T-cells c1 (NFATc1). Galectin-3 significantly inhibited dentine resorption by mature osteoclasts in vitro. Furthermore, in vivo studies clearly showed a significant suppression of bone destruction and osteoclast recruitment accompanying arthritis, when galectin-3 was injected into the cavity of ankle joint of AA rats. Thus, abundant galectin-3 observed in the area of severe bone destruction may act as a negative regulator for the upregulated osteoclastogenesis accompanying inflammation to prevent excess bone destruction.

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“…This galectin is a betagalactoside binding protein specifically expressed in stratified epithelia and notably in epidermis, but barely detectable in epidermal tumors and absent from squamous carcinoma cell lines. Further studies over this lectin of 14 kD molecular weight, show that it is a marker of all types of stratified epithelia (75). Another galectin, Galectin-1 an endogenous lectin, possesses galactose specific surface binding sites (69).…”

Section: The Galectin Family Of Proteins and Metagenesismentioning

confidence: 99%

Characterization of lectins and their specificity in carcinomas—An appraisal

Sherwani

Mohmood

Khan

et al. 2003

Indian J Clin Biochem

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Lectins, a group of specific glycoproteins present in animal as well as plant cells, are used as differentiating markers to study cancers and metastatic cell lines. This property of lectins depends on the process of cellular glycosylation. Glycosylation of some of the extracellular membrane proteins and lipids maintains the cell/cell and cell/matrix interactions. Chemical alterations in glycosylation play an important role in the metastatic behavior of tumor cells. Carbohydrate residues of the membrane glycoproteins can be detected using lectins due to their binding specificity to carbohydrates. Lectins, therefore have gained an importance in the field of cancer research. Galectins, a specialized group of lectin like proteins that are Ca+ independent and galactoside binding, are also considered as differentiation markers in some specific cancers like the carcinomas of thyroid.Thus the use of lectins and galectins to identify specific carbohydrates present on cell surface help in invasion and metastasis processes.

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Galectin-7, a marker of all types of stratified epithelia

Cited by 136 publications

References 45 publications

Psoriasis in humans is associated with down‐regulation of galectins in dendritic cells

Psoriasis in humans is associated with down‐regulation of galectins in dendritic cells

A possible suppressive role of galectin-3 in upregulated osteoclastogenesis accompanying adjuvant-induced arthritis in rats

Characterization of lectins and their specificity in carcinomas—An appraisal

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