Lectin histochemical study of lipopigments: results with concanavalin A.

Concanavalin A (Con A) binding to lipopigments (LPs) of the lipofuscin type was proved to be due to the high content of mannose. Two mannose bearing compounds could be recognized due to their different organic solvent solubility. One was best soluble in modified chloroform-methanol-water mixture (10:10:3) and corresponded most probably to the oligosaccharyl disphosphodolichol (oligo-PP-Dol) described to be significantly increased in LPs of inherited type. The second one, organic solvent insoluble corresponded to a glycoprotein (GP). The ratio of the two components varied. The deposition of the typical lipofuscin (age pigment) was dominated by the GP component. Its amount was greatest in neurolipofuscin (especially in the olivary nucleus) but very little in hepatocytic lipofuscin. In human neuronal ceroid lipofuscinoses (of early juvenile, and juvenile types) both components were found in large quantities in the storage granules of the affected neurons. The "protein type variant" of the storage material (Elleder, 1978) displayed the highest degree of lipid-bound mannose accumulation, the GP component being absent. In the late infantile, infantile and Kufs variants studied in paraffin sections only, the GP component was detectable, too as in the case of the secondary neuronal LP in mucopolysaccharidoses and gangliosidoses. In the canine model of NCL lipid bound mannose clearly predominated, the GP component being in low amount on average. Neither of the Con A reactive glycoconjugates could be identified as the component responsible for autofluorescence. However, both are most probably responsible for PAS positivity of lipofuscins. There were no detectable Con A reactive glycoconjugates in the histiocytic ceroid.