Detection of galectin-3 in tear fluid at disease states and immunohistochemical and lectin histochemical analysis in human corneal and conjunctival epithelium

Hrdlickova-Cela, E.

doi:10.1136/bjo.85.11.1336

Cited by 44 publications

(37 citation statements)

References 21 publications

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“…Hensin/gp340 polymerization is regulated by galectin-3, a known protein component of the cornea that participates in the wound-healing response (3, 21). Galectin-3 is found in the cornea and conjunctiva, but not in the lacrimal gland, and is up-regulated in ocular-surface disease (3,9). gp340/hensin, a molecule that both inhibits microbial invasion and promotes epithelial differentiation, could be a key player in ocular mucosal protection.…”

Section: Discussionmentioning

confidence: 99%

Glycoprotein 340 in Normal Human Ocular Surface Tissues and Tear Film

Jumblatt¹,

Imbert²,

Young³

et al. 2006

Infect Immun

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The tear film is a complex mixture of secreted fluid, ions, proteins, glycoproteins, and lipids that lubricates and protects the ocular surface. Recently, several antimicrobial peptides have been described in the tear fluid. In this study, we describe the presence of the large secreted glycoprotein gp340 in the tear film. Western blot analysis showed that gp340 is abundant in secreted tears and in the lacrimal glands. Lesser amounts of gp340 were detected in the cornea and conjunctiva. Consistent with Western blot data, reverse transcription-PCR and real-time quantitative PCR showed that gp340 transcripts were abundant in lacrimal gland tissue and were also present in the cornea and conjunctiva. Immunohistochemistry localized gp340 to the acinar cells of the lacrimal gland and the deeper layers of the conjunctival epithelium. gp340 was not detected in conjunctival goblet cells. In the cornea, gp340 was present only in a peripheral band of basal epithelial cells, suggesting that gp340 may play a role in the cycle of corneal epithelial renewal. To determine if tear film gp340 may function as a bacterial agglutinin as it does in saliva, tears were incubated with streptococcal cells and the formation of bacterial aggregates was monitored. Addition of tears to late-exponential-phase Streptococcus mutans cells resulted in time-and dose-dependent aggregation of the bacteria. Furthermore, Western blot analysis confirmed the presence of cell-associated gp340 in isolated bacterial aggregates. The ocular pathogen Staphylococcus aureus, but not Pseudomonas aeruginosa, also aggregated when incubated with tears. These results suggest that gp340 is a normal component of the tear film and that the glycoprotein may function as a bacterial agglutinin.

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Section: Discussionmentioning

confidence: 99%

Glycoprotein 340 in Normal Human Ocular Surface Tissues and Tear Film

Jumblatt¹,

Imbert²,

Young³

et al. 2006

Infect Immun

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“…Galectin-3 is expressed by epithelia lining the body surfaces that are exposed to Candida colonization, such as oral mucosa, corneal, and conjunctival epithelia, and intestinal epithelia (62)(63)(64)(65), that constitute the first line of host defense against Candida invasion. Although relatively high concentrations of soluble galectin-3 (20 M) were required to trigger Candida death in vitro, abundant galectin-3 has been detected in the local milieu surrounding inflammatory cells in human tissues (58), and galectin binding to extracellular matrix proteins has been shown to concentrate galectin (59).…”

Section: Discussionmentioning

confidence: 99%

Galectin-3 Induces Death of Candida Species Expressing Specific β-1,2-Linked Mannans

Kohatsu

Hsu

Jegalian

et al. 2006

The Journal of Immunology

202

157

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Lectins play a critical role in host protection against infection. The galectin family of lectins recognizes saccharide ligands on a variety of microbial pathogens, including viruses, bacteria, and parasites. Galectin-3, a galectin expressed by macrophages, dendritic cells, and epithelial cells, binds bacterial and parasitic pathogens including Leishmania major, Trypanosoma cruzi, and Neisseria gonorrhoeae. However, there have been no reports of galectins having direct effects on microbial viability. We found that galectin-3 bound only to Candida albicans species that bear β-1,2-linked oligomannans on the cell surface, but did not bind Saccharomyces cerevisiae that lacks β-1,2-linked oligomannans. Surprisingly, binding directly induced death of Candida species containing specific β-1,2-linked oligomannosides. Thus, galectin-3 can act as a pattern recognition receptor that recognizes a unique pathogen-specific oligosaccharide sequence. This is the first description of antimicrobial activity for a member of the galectin family of mammalian lectins; unlike other lectins of the innate immune system that promote opsonization and phagocytosis, galectin-3 has direct fungicidal activity against opportunistic fungal pathogens.

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“…[3][4][5] The expression of galectin-3 is upregulated under inflammatory conditions, such as in tears from patients with ocular diseases and in human atherosclerotic lesions. 6,7 The expression of galectin-3 was also detected in bronchoalveolar lavage fluid obtained from mice with inflamed airways. 8 These findings implicate galectin-3 expression in the pathological responses of inflammation.…”

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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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Detection of galectin-3 in tear fluid at disease states and immunohistochemical and lectin histochemical analysis in human corneal and conjunctival epithelium

Cited by 44 publications

References 21 publications

Glycoprotein 340 in Normal Human Ocular Surface Tissues and Tear Film

Glycoprotein 340 in Normal Human Ocular Surface Tissues and Tear Film

Galectin-3 Induces Death of Candida Species Expressing Specific β-1,2-Linked Mannans

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

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