Localization of fluorescence-labeled lectin binding sites on photoreceptor cells of the monkey retina

Uehara, F; Sameshima, M; Muramatsu, Takashi; Ohba, Norio

doi:10.1016/0014-4835(83)90094-5

Cited by 59 publications

(30 citation statements)

References 23 publications

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“…Neuraminidase from Clostridium perfringens (type V; Sigma) was diluted (1 Ul/ml) in 0.05 M acetate buffer, pH 5.3, and applied to the sections for 4 hr at 37°C. This procedure exposes the penultimate carbohydrate residues blocked by sialic acid (Uehara et al, 1985). The sections were then washed in acetate buffer and stained.…”

Section: Lectin-binding Studiesmentioning

confidence: 99%

Renal corpuscle of the sturgeon kidney: An ultrastructural, chemical dissection, and lectin‐binding study

2003

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The sturgeon is an ancient species of fish that thrives in a wide range of ecological environments, from freshwater to seawater. Basic in this process of adaptation is the ability of the kidney to control fluid filtration and urine formation. However, the morphological basis of this process is mostly unknown. The aim of the present study was to use microdissection techniques (scanning electron microscopy (SEM), transmission electron microscopy (TEM), and lectin-binding histochemistry) to examine the structure of the renal corpuscle of the sturgeon Acipenser nacarii in order to reveal morphologic features that could be related to function, phylogeny, and habitat. The renal corpuscles are aligned along the intrarrenal arteries. The urinary pole shows a siphon-like neck segment (NS) in 92% of the nephrons, whose structural characteristics are different from those of other fish. The podocytes have cuboidal cellular bodies, intercellular contacts, and poorly developed cell processes. The podocyte glycocalyx contains N-acetylglucosamine and lacks sialic acid. The structural and lectin-binding patterns are similar to those found in the immature mammalian kidney. The glomerular basement membrane (GBM) is very thick and consists of three layers: a lamina rara externa, a lamina densa, and a thick subendothelial lamina. The latter contains tubular microfibrils, collagen fibers, and long mesangial cell processes. Frequently, the podocyte bodies attach directly to the GBM, and the area occupied by the filtration slits is very small. Furthermore, the GBM shows a glycosylation pattern different from that observed in most vertebrates. Contrary to what would be expected in sturgeons living in freshwater, the A. nacarii renal corpuscle morphology suggests a low glomerular filtration rate. Anat Rec Part A 272A: 563-573, 2003.

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Section: Lectin-binding Studiesmentioning

confidence: 99%

Renal corpuscle of the sturgeon kidney: An ultrastructural, chemical dissection, and lectin‐binding study

2003

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“…37, 48, and 49), most of which remain uncharacterized. Information regarding IPM composition has originated from several histochemical and lectin cytochemical studies (35,(50)(51)(52). The CMS, identified initially on the basis of its PNA-binding properties (34,50), was later shown to contain chondroitin 6-sulfate (36).…”

Section: Discussionmentioning

confidence: 99%

Sequestration of basic fibroblast growth factor in the primate retinal interphotoreceptor matrix.

Hageman¹,

Kirchoff-Rempe²,

Lewis³

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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The interphotoreceptor matrix (IPM) occupies the extracellular space between the photoreceptors of the retina and the apical surface of the retinal pigmented epithelium. A large proportion of the IPM is composed of aqueousinsoluble glycoconjugates, including chondroitin sulfatecontaining proteoglycans, the distribution of which exhibits both apical-basal and photoreceptor cell type-specific heterogeneities. The precise function of most insoluble IPM constituents is unknown, although the available evidence suggests some may contribute to retinal adhesion or photoreceptor survival. We have now identified basic fibroblast growth factor (bFGF), or an immunologically related protein from the FGF family, within the IPM. The IPM is labeled on sections of primate retinas by a battery of polyclonal antibodies (Abs) directed against various peptide sequences of bFGF and by an Ab to bovine brain bFGF. bFGF Abs also bind to purified preparations of aqueous-insoluble IPM. AU bFGF Abs utilized cross-react with equivalent low molecular mass components of 16.5-17.5 kDa on Western blots of insoluble IPM proteins, purified bFGF, and recombinant bFGF. The Abs do not bind any aqueous-soluble IPM components, suggesting that the bFGF is normally bound to an insoluble 1PM constituent(s) in situ. The fact that bFGF is sequestered in the IPM and is located in such close proximity to the photoreceptors, the retinal pigmented epithelium, and Mueller's glia raises the strong possibility that it is synthesized by and regulates the activities of one or more of these three cell types in vivo.The fibroblast growth factors (FGFs) are a family of peptides that have been isolated from a broad range of cell types. FGFs share a number of structural, biochemical, and biological properties, the most characteristic being that they bind to heparin (1-4). The FGF family consists of acidic FGF (aFGF), basic FGF (bFGF), and a number of other related molecules that exhibit significant sequence homology to these two proteins. FGFs, like some other growth factors, are regarded as multifunctional in that they have a range of effects and activities in vitro that depend upon the target cell type (5). To date, FGFs have been shown: to influence neuronal differentiation, survival, and regeneration (6-9); to act as mitogens (10-13) and as inducing factors (14-17); to modulate protein synthesis (12,18); and to induce cell motility and migration (19). Much more is known about the effects of FGFs in vitro than under in vivo conditions.Although biochemical assays have shown that FGFs are present in a wide variety of cell types and tissues (for review, see refs. 3 and 4), only a few studies have sought to determine their specific cellular and/or extracellular distributions. Antibodies (Abs) have been used to localize bFGF to the cytoplasm of rat brain neurons (20-22) and chicken striated muscle myoblasts (23) and to the extracellular matrix of mouse hind-limb muscle (24). A recent comprehensive study of bFGF distribution in the 18-day rat fetus revealed intrace...

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“…61 Their was also found in human, 40 in pig and cat and in rabbit retina. 22 These observations are different to our results.…”

Section: Articlementioning

confidence: 92%

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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Localization of fluorescence-labeled lectin binding sites on photoreceptor cells of the monkey retina

Cited by 59 publications

References 23 publications

Renal corpuscle of the sturgeon kidney: An ultrastructural, chemical dissection, and lectin‐binding study

Renal corpuscle of the sturgeon kidney: An ultrastructural, chemical dissection, and lectin‐binding study

Sequestration of basic fibroblast growth factor in the primate retinal interphotoreceptor matrix.

Lectin binding in normal donkey eyeball

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