Ultrastructural localization of lectin-binding sites in different basement membranes

Salamat, Mehrdad; Götz, Werner; Werner, Jens; Herken, Rainer

doi:10.1007/bf00157811

Cited by 4 publications

(4 citation statements)

References 10 publications

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“…13,28,31 The thin basement membranes showed a marked presence of N-acetylgalactosamine residues, whereas a low concentration of these sugar residues was found in thick basement membranes. 32 Our observations showed binding of Con A and WGA to the corneal endothelium. This finding is not in accordance with the results of Panjwani and Baum, 10 Tuori et al, 11 who reported that the corneal endothelium tend to be bound only GSA-I-B4.…”

Section: Articlementioning

confidence: 80%

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: Articlementioning

confidence: 80%

Lectin binding in normal donkey eyeball

Aly

2013

Vet Sci Develop

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“…Heterogeneity in the distribution of the glycoproteins within the Descemet's membrane has been demonstrated previously (Gordon, 1990;Ljubimov et al, 1995 andLawrenson et al, 1998). The thin basement membranes showed a marked presence of N-acetylgalactosamine residues, whereas a low concentration of these sugar residues was found in thick basement membranes (Salamat et al, 1993).…”

Section: Discussionmentioning

confidence: 92%

Histochemical Mapping of Glycoconjugates in the Eyeball of the Buffalo (Bos Bubalis)

2013

Assiut Veterinary Medical Journal

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In the present study, the distribution of various sugar residues in the eyeball tissues of sexually mature buffalo was examined employing fluorescein isothiocyanate-(FITC) conjugated lectins. The present observations 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 buffalo 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 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 buffalo eyeball contains a wide range of glycoconjugates (bearing mannosyl, galactosyl and glucosly residues), and they lack fucosyl residues.

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“…It is known that the TE secretes a BM; several molecules have been localized to the TE-generated BM, including FN, LN, ColIV, and heparin sulfate proteoglycans (Wartiovaara et al, 1979;Leivo et al, 1980;Carnegie, 1991;Thorsteinsdottir, 1992;Hierck et al, 1993;Salamat et al, 1993). Importantly, these three proteins were distributed at the blastocoelic surface of the TE just prior to implantation.…”

Section: Discussionmentioning

confidence: 99%

“…Importantly, these three proteins were distributed at the blastocoelic surface of the TE just prior to implantation. It is known that the TE secretes a BM; several molecules have been localized to the TE-generated BM, including FN, LN, ColIV, and heparin sulfate proteoglycans (Wartiovaara et al ., 1979; Leivo et al ., 1980; Carnegie, 1991; Thorsteinsdottir, 1992; Hierck et al ., 1993; Salamat et al ., 1993). In vitro outgrowth assays have demonstrated that the cellular attachment and outward migration were activated on FN (Bartlett & Menino, 1995; Schilperoort-Haun & Menino, 2002a,b) and, to a greater extent, on ColIV (Carnegie & Cabaca, 1991, 1993) in several species.…”

Section: Discussionmentioning

confidence: 99%

Distribution of tubulointerstitial nephritis antigen-like 1 and structural matrix proteins in mouse embryos during preimplantation developmentin vivoandin vitro

Sakurai

Sato

Mukai

et al. 2012

Zygote

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Summary Tubulointerstitial nephritis antigen-like 1 (TINAGL1) is a novel matricellular protein that interacts with structural matrix proteins and promotes cell adhesion and spreading. We have previously reported unique localization of TINAGL1 to the trophectoderm (TE) of mouse blastocysts. TINAGL1 was found to be upregulated in implantation-competent blastocysts after estrogen treatment using progesterone-treated delayed-implantation models. Moreover, colocalization of TINAGL1 and extracellular matrix (ECM) protein laminin 1 was detected in the Reichert membrane on embryonic days 6.5 and 7.5. Although these data suggested a role for TINAGL1 in the embryo development at postimplantation, its relevance to other ECM proteins during preimplantation development is not clear. In this study, we examined the expression of TINAGL1 and its relevance to other ECM proteins fibronectin (FN) and collagen type IV (ColIV) during in vivo development of preimplantation embryos, particularly at blastocyst stage in detail. Localizations of TINAGL1, FN, and ColIV were similar. In 1-cell to 8-cell embryos, they were expressed in cytoplasm of blastomeres, and in morulae they were localized in the outer cells. FN and ColIV were expressed primarily on outer surface of the cells. In blastocysts, FN and ColIV were distributed in the cytoplasm of TE, but, just prior to implantation, they became localized uniquely to the blastocoelic surface of TE. In in vitro fertilized (IVF) blastocysts, expression levels of TINAGL1 and FN were lower than in in vivo blastocysts. These results suggest that, during preimplantation development, TINAGL1 may be involved in roles of structural matrix proteins, whose expression in blastocysts may be affected by in vitro culture.

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Ultrastructural localization of lectin-binding sites in different basement membranes

Cited by 4 publications

References 10 publications

Lectin binding in normal donkey eyeball

Lectin binding in normal donkey eyeball

Histochemical Mapping of Glycoconjugates in the Eyeball of the Buffalo (Bos Bubalis)

Distribution of tubulointerstitial nephritis antigen-like 1 and structural matrix proteins in mouse embryos during preimplantation developmentin vivoandin vitro

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