Mannose-specific binding sites in synoviocytes of rat synovial membrane: An ultrastructural-cytochemical study

Graabæk, Pernille Møller

doi:10.1016/0889-1605(86)90064-9

Cited by 4 publications

(1 citation statement)

References 24 publications

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“…Enzymes which are inherently glycosylated (e.g. dog intestinal alkaline phosphatase and horseradish peroxidase) do not require chemical derivatization, since their glycan chains are already suitable as ligand for galactose-or mannose-speci®c binding sites (Hardonk and Scholtens, 1980;Straus, 1981Straus, , 1983Graabek, 1986). This situation warrants comment due to the widespread application of colour-generating kit systems containing peroxidase and also other glycoproteins such as avidin as integral components.…”

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confidence: 99%

Glycohistochemistry: The Why and How of Detection and Localization of Endogenous Lectins

Gabius¹

2001

Anat Histol Embryol

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The central dogma of molecular biology limits the downstream flow of genetic information to proteins. Progress from the last two decades of research on cellular glycoconjugates justifies adding the enzymatic production of glycan antennae with information-bearing determinants to this famous and basic pathway. An impressive variety of regulatory processes including cell growth and apoptosis, folding and routing of glycoproteins and cell adhesion/migration have been unravelled and found to be mediated or modulated by specific protein (lectin)-carbohydrate interactions. The conclusion has emerged that it would have meant missing manifold opportunities not to recruit the sugar code to cellular information transfer. Currently, the potential for medical applications in anti-adhesion therapy or drug targeting is one of the major driving forces fuelling progress in glycosciences. In histochemistry, this concept has prompted the introduction of carrier-immobilized carbohydrate ligands (neoglycoconjugates) to visualize the cells' capacity to be engaged in oligosaccharide recognition. After their isolation these tissue lectins will be tested for ligand analysis. Since fine specificities of different lectins can differ despite identical monosaccharide binding, the tissue lectins will eventually replace plant agglutinins to move from glycan profiling and localization to functional considerations. Namely, these two marker types, i.e. neoglycoconjugates and tissue lectins, track down accessible binding sites with relevance for involvement in interactions in situ. The documented interplay of synthetic organic chemistry and biochemistry with cyto- and histochemistry nourishes the optimism that the application of this set of innovative custom-prepared tools will provide important insights into the ways in which glycans can act as hardware in transmitting information during normal tissue development and pathological situations.

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Glycohistochemistry: The Why and How of Detection and Localization of Endogenous Lectins

Gabius¹

2001

Anat Histol Embryol

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Competition between ligands of glycosyltransferases and horseradish peroxidase for binding sites on intracellular and plasma membranes of HeLa cells

Straus

Keller

1990

Histochemistry

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A micro-method for the semi-quantitation of surface-bound horseradish peroxidase (HRP) was developed and was applied to study the competition between ligands of glycosyltransferases and HRP for binding sites on the surface of HeLa cells. Dried coverslip cultures of HeLa cells, fixed in methanol, were placed on 0.3 ml of the incubation medium on parafilm and were incubated for 45 min at 37 degrees C. The incubation medium contained HRP, lysozyme and Ca2+ in HEPES buffer, pH 7.2. After washing, the cells were incubated for 60 min at 37 degrees C in HEPES buffer containing 20 mM Ca2+. After this treatment, the plasma membranes showed a strong cytochemical reaction for HRP. Most of the HRP was released into buffer solution during a 5 h incubation at 37 degrees C in the absence of Ca2+, and was measured by spectrophotometry. The addition of 20 mM Ca2+ to the buffer solution prevented the release of most of the HRP from the plasma membranes thus showing that the binding of HRP required Ca2+. Ligands of glycosyltransferases were added to the incubation medium with HRP. The amount of HRP released from the cells decreased in relation to the competing potency and concentration of these ligands. The method was applied to estimate the concentration of some ligands of galactosyltransferase and sialyltransferase that caused a 50% decrease in the release of previously-bound HRP. CMP-neuraminic acid and gangliosides showed a higher competing potency to the surface binding of HRP than UDP-galactose and chitotriose. The spectrophotometric analysis was correlated (on duplicate samples) with cytochemical observations.(ABSTRACT TRUNCATED AT 250 WORDS)

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Aging of the human synovium: An in vivo and ex vivo morphological study

Pasquali‐Ronchetti

Frizziero²,

Guerra³

et al. 1992

Seminars in Arthritis and Rheumatism

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Mannose-specific binding sites in synoviocytes of rat synovial membrane: An ultrastructural-cytochemical study

Cited by 4 publications

References 24 publications

Glycohistochemistry: The Why and How of Detection and Localization of Endogenous Lectins

Glycohistochemistry: The Why and How of Detection and Localization of Endogenous Lectins

Competition between ligands of glycosyltransferases and horseradish peroxidase for binding sites on intracellular and plasma membranes of HeLa cells

Aging of the human synovium: An in vivo and ex vivo morphological study

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