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

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.