The Microanalysis of Saccharide Structures of Normal and Neoplastic Tissues

Stoddart, R. W.; Collins, Robert D.; Jacobson, Wendy S.

doi:10.1042/bst0020481

Cited by 13 publications

(4 citation statements)

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“…PHA and PNA. A similar negative response to R C A has been reported by Stoddart et al (1974). During glycosylation of proteins these sugars are assembled in a more distal position to the polypeptide backbone.…”

Section: Discussionsupporting

confidence: 80%

The lectin binding affinity of Reed‐Sternberg cells

Morris

Stuart

1983

The Journal of Pathology

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Reed-Sternberg cells from ten cases of Hodgkin's disease were examined by the direct immunofluorescence technique, for their affinity for nine lectins. The surrounding lymphocytes and monocytes of HD tissue were also assessed for their ability to bind lectins. RS cells showed considerable heterogeneity of reaction. Overall, there was a marked decrease in the binding of most of the lectins studied in HD cases as compared to normal peripheral blood mononuclear cells. This was particularly evident for RCA, PHA and PNA binding. It is suggested that there is a defect in carbohydrate metabolism, with fewer lectin-binding sites on both RS cells and on the mononuclear cell populations in Hodgkin's disease. Further quantitative work is required to verify this.

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Section: Discussionsupporting

confidence: 80%

The lectin binding affinity of Reed‐Sternberg cells

Morris

Stuart

1983

The Journal of Pathology

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“…This may result in conformational changes in the membrane components. Stoddart et al (1974) and Thomson et al (1978) have shown that aprotinin binds to sialyl residues present on the surface of cells. One could envisage, therefore, the possibility of a rearrangement of the surface components as a result of aprotinin binding.…”

Section: Discussionmentioning

confidence: 99%

Aprotinin Induces Surface Changes in Malignant Cells in Culture: a Possible Mode of Antitumour Action

Latner¹,

Gv²

1979

Pathobiology

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Treatment of TRES cells with aprotinin (Trasylol®) produced marked changes in their surface properties. There was a concentration-dependent increase in the surface charge density of the cells. The agglutinability of the cells was inhibited by the antiproteinase. The cells became less adhesive to concanavalin A-linked plates. The adhesion of treated TRES cells appeared to be mediated by lectin receptors with lower specificity for concanavalin A. These observations and an analysis of the kinetics of adhesion have suggested the possibility that a new class of concanavalin A receptors appears on the surface of aprotinin-treated TRES cells, which might increase immunogenicity of the cells.

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“…Sections were de-waxed in xylol, hydrated through graded alcohols to water and treated for 1 min with 0.5 % osmic acid to quench auto-fluorescence (Kiernan and Stoddart, 1973;Stoddart and Kiernan, 1973a;Stoddart et al, 1974;McCance et al, 1975). The excess of osmium was removed by washing for 4 h in running water, and the sections were then stained by exposure to standing drops o f the appropriate solutions of the lectins (table I) for 1 min.…”

Section: Methodsmentioning

confidence: 99%

Changes in the Organs of Pigs in Response to Feeding for the First 24 h after Birth

Em²

1976

Neonatology

122

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The duodenum, jejunum, ileum and large intestine of newborn, and 24-hour-old fed and unfed piglets, and of 10-day-old piglets have been studied by new histochemical methods. At birth Meissner’s plexus was most developed in the duodenum. There was little change during the first 24 h, but by 10 days it had become elaborated. Goblet cells were present at birth in all parts of the intestine. After 24 h a large proportion of those in the duodenum had discharged and were being replaced with a new generation. Similar changes took place more slowly in the jejunum and ileum and very much more slowly in the large intestine. Feeding increased the rate of turnover.

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The Microanalysis of Saccharide Structures of Normal and Neoplastic Tissues

Cited by 13 publications

References 0 publications

The lectin binding affinity of Reed‐Sternberg cells

The lectin binding affinity of Reed‐Sternberg cells

Aprotinin Induces Surface Changes in Malignant Cells in Culture: a Possible Mode of Antitumour Action

Changes in the Organs of Pigs in Response to Feeding for the First 24 h after Birth

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