Secretory Granule Proteoglycans of Mast Cells and Natural Killer Cells

Stevens, Richard L

doi:10.1002/9780470513385.ch15

Novartis Foundation Symposia

2007

DOI: 10.1002/9780470513385.ch15

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Secretory Granule Proteoglycans of Mast Cells and Natural Killer Cells

Richard L Stevens

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2011

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Cited by 9 publications

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An ultrastructural study of the morphology and lectin-binding properties of human mast cell granules

1988

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The morphological characteristics and lectin-binding properties of mast cell granules from four human neurofibromata are described. Ultrastructural examination of the granules revealed that some contained dense cores, others had membranous configurations and some forms were intermediate between the two. A round electron-lucent area was present in some granules. After treatment with biotinylated lectins (10 micrograms ml-1) followed by an avidin-peroxidase revealing system (5 micrograms ml-1 in 0.125 M Tris-buffered saline with 0.347 M NaCl, pH 7.6), mast cell granules strongly bound Concanavalin A, garden pea, lentil, wheatgerm, erythro- and leuco-kidney bean lectins. This indicated the presence of abundant N-linked complex-type saccharide sequences. Soybean and peanut lectins showed only weak binding, while the presence of sparse alpha-L-fucosyl terminals was indicated by the weak binding of winged pea lectin. The staining intensity of wheatgerm lectin was considerably reduced when incubated in the presence of its specific competing sugar tri-N-acetylchitotriose. Despite a wide variety of morphological differences between granules, all showed similar staining patterns and all granules within a single cell shared the same binding characteristics.

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An ultrastructural study of the morphology and lectin-binding properties of human mast cell granules

1988

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Lectin histochemistry of the mast cell: A light microscopical study

Kirkpatrick

Jones²,

Stoddart³

1988

Histochem J

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SummaryThe purpose of this study was to determine if human mast cell granules contain non-repeating oligosaccharide sequences. The binding of lectins to human mast cell granules was studied using a panel of 11 lectins variously selective for both N-and O-linked oligosaccharide sequences. The tissues were principally derived from cutaneous neurofibromata and benign and malignant breast diseases, that is, readily available human material with a known high content of mast cells. Lectin-binding sites in the formalin-fixed paraffin-embedded or resin-embedded material were visualized by means of biotinylated lectins and an avidin-peroxidase technique for light microscopy. The results indicate that human mast cell granules contain abundant N-linked sequences, but few or no O-linked residues. These sequences appear to be mostly in the form of non-bisected highly branched or smaller biantennate sequences, although variable positive binding with erythrophytohaemagglutinin was observed, indicating some degree of bisection.

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Distribution, density and histochemical profiles of the lung mast cells during the post-hatching period of Japanese quails (Coturnix coturnix japonica)

Harem

Lïman

Alan

2011

Research in Veterinary Science

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Secretory Granule Proteoglycans of Mast Cells and Natural Killer Cells

Cited by 9 publications

References 31 publications

An ultrastructural study of the morphology and lectin-binding properties of human mast cell granules

An ultrastructural study of the morphology and lectin-binding properties of human mast cell granules

Lectin histochemistry of the mast cell: A light microscopical study

Distribution, density and histochemical profiles of the lung mast cells during the post-hatching period of Japanese quails (Coturnix coturnix japonica)

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