concanavalin-a and Gangliosidoses

Topics: Adolescent; Binding Sites; Brain; Child; Concanavalin A; Fucose; Galactose; Gangliosidoses; Gaucher Disease; Glycoproteins; Hexosamines; Humans; Infant, Newborn; Leukodystrophy, Globoid Cell; Leukodystrophy, Metachromatic; Lipidoses; Lysosomes; Mannose; Middle Aged; Protein Binding; Sialic Acids; Sphingolipidoses

Concanavalin A (ConA) binding to lipopigments (LPs) of the lipofuscin type was proved to be due to the high content of mannose. The nature of the mannose bearing compound was twofold. One part was soluble in modified chloroform-methanol-water mixture (10:10:3) corresponding possibly to the oligosaccharyl diphosphodolichol (oligo-PP-Dol) described to be increased in LPs especially of inherited types. The second part, most probably a glycoprotein (GP), was entirely resistant to various extraction procedures. 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) and in the myocardium 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 extremely low or entirely 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 dog model of NCL lipid bound mannose clearly predominated, the GP component being concentrated in the cytoplasm and on the periphery od some storage granules. The nature of the GP component, a new finding of LP analysis, is discussed. The metabolic relationship between the two components is uncertain. Neither could be identified as the component resposible for autofluorescence.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Adolescent; Adult; Animals; Ceroid; Child; Child, Preschool; Concanavalin A; Gangliosidoses; Humans; Lipofuscin; Mannose; Mucopolysaccharidoses; Neuronal Ceroid-Lipofuscinoses; Neurons; Olivary Nucleus; Pigments, Biological; Staining and Labeling

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.

Topics: Animals; Ceroid; Child, Preschool; Concanavalin A; Dog Diseases; Dogs; Gangliosidoses; Histocytochemistry; Humans; Infant; Lipofuscin; Mucopolysaccharidoses; Neuronal Ceroid-Lipofuscinoses; Sheep; Sheep Diseases

Lectin histochemical studies were performed on paraffin-embedded brain, spinal cord and eye sections of 16 animals from four different species affected with GM1- and GM2-gangliosidosis to identify specific carbohydrate residues in the perikaryon of neurons. We examined tissues from cats, cattle and dogs with GM1-gangliosidosis and from cats, dogs, and swine with GM2-gangliosidosis and compared them to corresponding normal animals. In all but two cases, the neurons stained intensely with Concanavalia ensiformis agglutinin (Con A); in 12 cases they stained with Dolichos biflorus agglutinin; in 10 cases with Ulex europaeus agglutinin-I; in 9 cases with Griffonia simplicifolia-I; and 8 with soybean agglutinin. Neurons from control tissues stained weakly with Con A, but not with any of the other lectins used. Similar staining patterns of neurons were noted in animals affected with the same disorder originating from the same mutant line. These findings highlight the fact that in gangliosidosis, the lectin staining patterns of neurons may be influenced by the deficiency in enzyme activity and by additional unknown but inherited factors.

Topics: Animals; Brain; Cats; Cattle; Concanavalin A; Dogs; Endothelium; G(M1) Ganglioside; G(M2) Ganglioside; Gangliosides; Gangliosidoses; Lectins; Plant Lectins; Species Specificity; Swine; Wheat Germ Agglutinins

Topics: Adult; Ammonium Chloride; beta-Galactosidase; Cells, Cultured; Child, Preschool; Concanavalin A; Female; Fibroblasts; Galactosidases; Gangliosidoses; Humans; Infant; Kinetics; Lactose Intolerance; Liver; Male; Neuraminidase; Placenta; Pregnancy; Skin; Tissue Extracts

Topics: beta-Galactosidase; Biological Transport; Cell Line; Concanavalin A; Endocytosis; Fibroblasts; Galactosidases; Gangliosidoses; Hexosaminidases; Humans; Kinetics; Sandhoff Disease; Temperature

Topics: Animals; Aspergillus niger; Binding Sites; Biological Transport; Cattle; Chromatography, Affinity; Concanavalin A; Fibroblasts; Galactosidases; Gangliosidoses; Glucosamine; Glucuronidase; Humans; Liver; Male; Mannose; Mannosidases; Mannosides; Plant Lectins; Plants; Protein Binding; Skin; Testis