Lectin-binding sites in the anterior segment of the human eye

Rittig, Michael; Brigel, Claudia; Lütjen–Drecoll, Elke

doi:10.1007/bf00918485

Cited by 23 publications

(13 citation statements)

References 17 publications

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“…26 The pattern of lectin binding in the corneal epithelium suggests the presence of glycoconjugates containing terminal α-mannose, N-acetylglucosamine and sialic acid residues and sparse terminal α-galactose and β-N-acetylgalactosamine residues. 9,17,27,28 This generally agrees to my results.…”

Section: Discussionsupporting

confidence: 82%

“…This agrees to our results. The different staining pattern between apical and basal cells of the corneal epithelium has been described previously by several authors in different species, 6,9,24,27 and it is related to the differentiation of epithelial cell, as they move to the apical layers of the epithelium. 29 Furthermore, Con A and WGA were bound to the corneal stroma in my experiment, but no binding of this lectins was seen in the study of Panjwani and Baum, 16 who reported that PNA is the only lectin that is bound to the corneal stroma.…”

Section: Discussionmentioning

confidence: 99%

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Lectin binding in normal donkey eyeball

Aly

2013

Vet Sci Develop

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In the present study, the distribution of various sugar residues in the eyeball tissues of sexually mature donkey was examined by employing fluorescein isothiocyanate-conjugated lectins. Our results revealed the presence of mannose (labeled by lectins ConA), galactose (labeled by PNA, GSAI, ECA), GalNAc (labeled by SBA, VVA), and GlcNAc (labeled by WGA) residues in the donkey ocular tissues. The epithelium and stroma of the ocular tissues were labeled with mannose (ConA) and GlcNAc (WGA) binding lectins. Binding sites for WGA and PNA to the rod and cone cells of the retina were evident. The lectins Con A, WGA and GSAI are bound strongly to the endothelium of blood vessels and to smooth muscle cells of the iris. In conclusion, the findings of the present study clearly indicate that the donkey eyeball contains a wide range of glycoconjugates (bearing mannosyl, galactosyl and glucosly residues), and it lacks fucosyl residues.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Lectin binding in normal donkey eyeball

Aly

2013

Vet Sci Develop

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“…Further, a number of histochemical studies have demonstrated WGA binding to the ocular surface glycocalyx, in which membrane-associated type mucin is located. 19,20 In the characterization of the ocular surface material in dogs, Hick et al reported that the extracted materials in void volume by gel filtration showed a positive peak for anti-mucin antibody. 21 Therefore, the high molecular weight glycoconjugate measured by this method has a property as a mucin-like glycoprotein.…”

Section: Discussionmentioning

confidence: 98%

Rebamipide Increases the Mucin-Like Glycoprotein Production in Corneal Epithelial Cells

Takeji

Urashima

Aoki

et al. 2012

Journal of Ocular Pharmacology and Therapeutics

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Purpose: Dry eye is a multifactorial disease of tears and the ocular surface due to tear deficiency or excessive tear evaporation. Tear film instability is due to a disturbance in ocular surface mucin leading to a dysfunction of mucin, resulting in dry eye. In this study, we examined the effect of rebamipide, an anti-ulcer agent, on glycoconjugate production, as an indicator of mucin-like glycoprotein in cultured corneal epithelial cells. Further, we investigated the effect of rebamipide on the gene expression of membrane-associated mucins. Methods: Confluent cultured human corneal epithelial cells were incubated with rebamipide for 24 h. The glycoconjugate content in the supernatant and the cell extracts was measured by wheat germ agglutininenzyme-linked lectin assay combined gel-filtration method. In the experiment on mucin gene expression, cultured human corneal epithelial cells were collected at 0, 3, 6, and 12 h after administration of rebamipide. Real-time quantitative polymerase chain reaction was used to analyze the quantity of MUC1, MUC 4, and MUC16 gene expression. Results: Rebamipide significantly increased the glycoconjugate contents in the supernatant and cell extract. In the mucin gene expression in the cells, rebamipide increased MUC1 and MUC4 gene expression, but did not increase MUC16 gene expression. Conclusions: Rebamipide promoted glycoconjugate, which has a property as a mucin-like glycoprotein, in human corneal epithelial cells. The increased production was mediated by MUC1 and MUC4 gene expression.

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“…Recently, lectins' have been used in eye research, mainly for human material (Wells et al, 1988;Brandon et aL, 1988;Tripathi et al, 1989Tripathi et al, , 1990Rittig et al, 1990;Bishop et al, 199i; for review see Prause, 1991). In the present study, the binding of several different lectins to anterior parts of the bovine eye was analysed.…”

Section: Introductionmentioning

confidence: 99%

Lectin binding in the anterior segment of the bovine eye

1994

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Eleven different fluorescent lectin-conjugates were used to reveal the location of carbohydrate residues in frozen sections of the anterior segment of bovine eyes. The lectins were specific for the following five major carbohydrate groups: (1) glucose/mannose group (Concanavalin A (Con A)); (2) N-acetylglucosamine group (wheat germ agglutinin (WGA)); (3) galactose/N-acetylgalactosamine group (Dolichos biflorus agglutinin (DBA), Helix pomatia agglutinin (HPA), Helix aspersa agglutinin (HAA), Psophocarpus tetragonolobus agglutinin (PTA), Griffonia simplicifolia agglutinin-I-B4 (GSA-I-B4), Artocarpus integrifolia agglutinin (JAC), peanut agglutinin (PNA) and Ricinus communis agglutinin (RCA-I)); (4) L-fucose group (Ulex europaeus agglutinin (UEA-I)); (5) sialic acid group (wheat germ agglutinin (WGA)). All the studied lectins except UEA-I reacted widely with different structures and the results suggest that there are distinct patterns of expression of carbohydrate residues in the anterior segment of the bovine eye. UEA-I bound only to epithelial structures. Some of the lectins reacted very intensely with apical cell surfaces of conjunctival and corneal epithelia suggesting a different glycosylation at the glycocalyx of the epithelia. Also, the binding patterns of conjunctival and corneal epithelia differed with some of the lectins: PNA and RCA-I did not bind at all, and GSA-I-B4 bound only very weakly to the epithelium of the cornea, whereas they bound to the epithelium of the conjunctiva. In addition, HPA, HAA, PNA and WGA did not bind to the corneal basement membrane, but bound to the conjunctiva and vascular basement membranes. This suggests that corneal basement membrane is somehow different from other basement membranes. Lectins with the same carbohydrate specificity (DBA, HPA, HAA and PTA) reacted with the sections almost identically, but some differences were noticed: DBA did not bind to the basement membrane of the conjunctiva and the sclera and did bind to the basement membrane of the cornea, whereas other lectins with same carbohydrate specificities reacted vice versa. Also, the binding of PTA to the trabecular meshwork was negligible, whereas other lectins with the same carbohydrate specificities reacted with the trabecular meshwork. GSA-I-B4 reacted avidly with the endothelium of blood vessels and did not bind to the stroma, so that it made blood vessels very prominent and it might be used as an endothelial marker. This lectin also reacted avidly with the corneal endothelium. Therefore, GSA-I-B4 appears to be a specific marker in bovine tissues for both blood vessel and corneal endothelium cells.

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Lectin-binding sites in the anterior segment of the human eye

Cited by 23 publications

References 17 publications

Lectin binding in normal donkey eyeball

Lectin binding in normal donkey eyeball

Rebamipide Increases the Mucin-Like Glycoprotein Production in Corneal Epithelial Cells

Lectin binding in the anterior segment of the bovine eye

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