Ultrastructural analysis of the central terminals of primary sensory neurones labelled by transganglionic transport of bandeiraea simplicifolia I-isolectin B4.

In this study the ultrastructural appearance of primary sensory neurones labelled by the injection of the plant lectin Bandeiraea simplicifolia I-isolectin B(4) (BSI-B(4)) into a peripheral nerve has been examined in the rat. Electron microscopy of the somata of retrogradely labelled neurones showed the lectin to be associated with the inner surface of cytoplasmic vesicles, supporting the premise that the uptake of BSI-B(4) into sensory neurones is by the process of receptor-mediated endocytosis. Light and electron microscopic analysis of the spinal cord revealed transganglionically transported lectin in unmyelinated axons in the dorsolateral funiculus and axon terminals concentrated mainly within lamina II of the dorsal horn. Detailed analysis of 1377 of these axon terminals revealed that the majority were glomerular in shape and surrounded by up to 14 other unlabelled profiles. These findings suggest that primary sensory neurones which transganglionically transport BSI-B(4) have a synaptic ultrastructure similar to that which has been previously reported for unmyelinated primary sensory neurones. Moreover, it appears that the axon terminals of these neurones are subjected to extensive modulation. Examination of the vesicle content of lectin labelled axon terminals revealed that the majority contained small agranular vesicles while large granular vesicles were observed only occasionally. These findings support the suggestion that the populations of neurones expressing binding sites for BSI-B(4) are fairly distinct from those containing neuroactive peptides. In conclusion, the results of the current study suggest that the lectin BSI-B(4) can be used as a histological marker for a subpopulation of small diameter primary sensory neurones and provide further evidence for the potential of this lectin as a useful tool in the study of pain.