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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 67 (1985), S. 265-271 
    ISSN: 1432-0533
    Keywords: α-l-Fucosidase deficiency ; Human and canine disease ; Lectin histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Selected formalin-fixed, paraffin-embedded tissues of human and canine fucosidosis were stained with nine different lectins. Neurons, splenic sinusoidal cells, hepatic Kupffer cells, tissue macrophages, and capillary endothelium from human patients with fucosidosis stained intensely withUlex europaeus agglutinin-I (UEA-I), but the same cells were unstained in tissues from canine fucosidosis. Since UEA-I specifically binds to terminal fucose residues, and fucose-rich undegraded metabolites are stored in affected cells of both human and canine fucosidosis, the variable lectin staining pattern demonstrates an unexpected species-specific histochemical variability. This finding highlights the fact that although both species have decreased fucosidase activity, the precursor substrates, undegraded stored metabolites, and particular cells affected by this enzyme deficiency are different.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 76 (1988), S. 359-365 
    ISSN: 1432-0533
    Keywords: Hexosaminidase A and B deficiency ; Lectin histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Lectin histochemical studies were performed on selected formalin-fixed, paraffin-embedded tissues of patients affected with the O variant of GM2-gangliosidosis (i.e., Sandhoff's disease). The purpose was to identify specific sugar residues of undegraded “stored” substances in cytoplasm of affected cells. We studied neural tissues from 13 patients, visceral tissues from four patients, and placentae from three affected fetuses. Neurons in all 13 cases studied stained withConcanavalia ensiformis agglutinin (Con A) and withUlex europaeus agglutinin-I (UEA-I). Succinylated wheat germ agglutinin (S-WGA) stained affected visceral cells and astrocytes and macrophages in the central nervous system. These results demonstrate that α-d-mannosyl and α-l-fucosyl residues, which bind Con A and UEA-I, respectively, are present in affected neurons. Furthermore, they revealed the affected nonneuronal cells and astrocytes contain complex carbohydrates with nonreducing terminal β-N-acetylglucosamine, which binds S-WGA.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Canine galactosialidosis ; Morphology ; Biochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An adult-onset lysosomal storage disorder was diagnosed in a 5-year-old Schipperke dog with progressive cerebellar and central vestibular signs. It was characterized by cerebellar atrophy with extensive loss of Purkinje and granular cells, and hydrocephalus. Enlarged and vacuolated neurons were observed in spinal cord and brain; pancreatic centrolobular and islet cells were also vacuolated. Ultrastructurally, enlarged secondary lysosomes laden with lamellated membrane structures were present in neurons and empty enlarged vacuoles were found in pancreatic centroacinar, ductal, and islet cells. On frozen sections neurons stained with Ricinus communis agglutinin-I and wheat germ agglutinin. On paraffin sections neurons stained with luxol fast blue, periodic acid-Schiff, Concanavalia ensiformis agglutinin, and were autofluorescent. These findings indicate an accumulation of glycolipids containing terminal β-galactosyl and α-sialyl residues, and N-linked oligosaccharides. Tissue activity of lysosomal β-galactosidase was 50% of normal and the activity of β-hexosaminidase was elevated. Brain lipid-bound sialic acid was twice normal, with a small increase of GM1-ganglioside, but there was a significant elevation of GM2 (GD2) and GM3 (GD3). In addition, significant elevations of sialylated and non-sialylated oligosaccharides were noted. These clinical, biochemical and pathological findings are similar to those observed in human patients with adult-onset galactosialidosis.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0533
    Keywords: Lectin-histochemistry ; Krabbe's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Lectin-histochemical studies were performed on paraffin-embedded brain tissue sections to identify the specific sugar residues of undegraded “stored” substances in the cytoplasm of globoid cells from patients with globoid cell leukodystrophy. We studied brain tissues from six human patients with galactosylceramide lipidosis (i. e., Krabbe's disease) and compared them to brain tissues from animals with a similar enzyme deficiency including seven Twitcher mice, three dogs and two cats. The globoid cells in all 18 cases studied stained with succinylated-wheat germ agglutinin (S-WGA), but did not stain withDilichos biflorus agglutinin, soybean agglutinin orUlex europaeus agglutinin-I.Bandeirea simplicifolia agglutinin-I stained the globoid cells in Twitcher mice, dogs and cats but not those in humans.Concanavalia ensiformis agglutinin, wheat germ agglutinin andRicinus communis agglutinin-I all stained each of the globoid cells in the mouse, dog and cat tissues, but only in some of the human cases. Peanut agglutinin, however, variably stained globoid cells in the mouse and dog cases but not at all in the human and cat cases. These results demonstrate a common terminal carbohydrate residueN-acetyl glucosamine, which binds S-WGA in the undergraded material stored within the globoid cells in galactoceramide lipidosis. These cells also contained various other stored molecules with sugar residues whose nature is determined by species or individually.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 76 (1988), S. 109-114 
    ISSN: 1432-0533
    Keywords: Lectin histochemistry ; Mammalian gangliosidosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 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 withConcanavalia ensiformis agglutinin (Con A); in 12 cases they stained withDolichos biflorus agglutinin; in 10 cases withUlex europaeus agglutinin-I; in 9 cases withGriffonia 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.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: KeyWordsOsteopetrosis ; Carbohydrate and lipid storage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In infantile lysosomal storage disease associated with osteopetrosis the nature of the enzyme deficiency as well as the type of material accumulated are both unknown. We used lectin histochemistry to characterize the storage material of previously reported cases. Using paraffin sections neurons stained positively with Luxol fast blue (LFB), periodic acid-Schiff (PAS), Concanavalia ensiformis agglutinin, Datura stramonium agglutinin, Griffonia simplicifolia-I, Lens culinaris agglutinin, Ricinus communis agglutinin-I, succinylated wheat germ aggluninin and wheat germ agglutinin, indicating an accumulation of fucosylated N-glycosidically linked oligosaccharides containing β- and α-galactosyl residues and compounds containing N-acetyllactos- amine. Reticuloendothelial cells in liver and in spleen did not stain with LFB, but did stain with PAS and the above lectins. These results indicate that there is storage of both carbohydrates and lipids in neurons, and stored carbohydrates with similar residues in reticuloendothelial cells in this disease, where the primary defect is still unknown.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 87 (1994), S. 594-597 
    ISSN: 1432-0533
    Keywords: Osteopetrosis ; Carbohydrate and lipid storage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In infantile lysosomal storage disease associated with osteopetrosis the nature of the enzyme deficiency as well as the type of material accumulated are both unknown. We used lectin histochemistry to characterize the storage material of previously reported cases. Using paraffin sections neurons stained positively with Luxol fast blue (LFB), periodic acid-Schiff (PAS), Concanavalia ensiformis agglutinin, Datura stramonium agglutinin, Griffonia simplicifolia-I, Lens culinaris agglutinin, Ricinus communis agglutinin-I, succinylated wheat germ aggluninin and wheat germ agglutinin, indicating an accumulation of fucosylated N-glycosidically linked oligosaccharides containing β- and α-galactosyl residues and compounds containing N-acetyllactos-amine. Reticuloendothelial cells in liver and in spleen did not stain with LFB, but did stain with PAS and the above lectins. These results indicate that there is storage of both carbohydrates and lipids in neurons, and stored carbohydrates with similar residues in reticuloendothelial cells in this disease, where the primary defect is still unknown.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 276 (1984), S. 216-223 
    ISSN: 1432-069X
    Keywords: Carbohydrate residues ; Normal skin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Sections of biopsies of normal skin obtained from 11 individuals were incubated with 8 lectins using an avidin-biotin complex (ABC). All sections when incubated with the appropriate lectin showed the presence of the following carbohydrate residues: l-fucose, β-(1–4)-d-GlcNAc)2 (N-acetylglucosamine), acetylneuraminic acid, Gal-β-(1–3)-GalNAc (N-acetyl-galactosamine), β-d-galactose, α-d-glucose, and α-d-mannose. In addition, sections of individuals with blood group A showed α-d-GalNAc and sections of individuals with blood group B showed α-d-galactose. In the stratum (str.) basale, carbohydrates were present in small quantities, but as the cells matured and moved upward, the incorporation of carbohydrates into the cell membranes increased considerably. In the str. granulosum, lectin reactivity was absent in many sections, probably due to masking by phospholipids. The dark cells in the eccrine glands showed reactivity with all lectins except in the one nonsecretor with blood group A1, whose dark cells showed no l-fucose and α-d-GalNAc. The endothelial cells of the blood vessels showed lectin reactivity except when incubated with concanavalin A. The sebaceous glands showed both cytoplasmic and membrane staining when incubated with various lectins.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 649 (1981), S. 239-243 
    ISSN: 0005-2736
    Keywords: (Mouse bladder) ; Filipin-cholesterol complex ; Freeze-fracture ; Nuclear membrane
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part B: Biochemistry and 106 (1993), S. 373-382 
    ISSN: 0305-0491
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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