g(m3)-ganglioside and Gangliosidosis--GM1

g(m3)-ganglioside has been researched along with Gangliosidosis--GM1* in 1 studies

Other Studies

1 other study(ies) available for g(m3)-ganglioside and Gangliosidosis--GM1

Article	Year
Metabolism of GM1 ganglioside in cultured skin fibroblasts: anomalies in gangliosidoses, sialidoses, and sphingolipid activator protein (SAP, saposin) 1 and prosaposin deficient disorders. Human genetics, 1992, Volume: 89, Issue:5 Cultured skin fibroblasts from controls and patients with lysosomal storage diseases were loaded with GM1 ganglioside that had been labelled with tritium in its ceramide moiety. After a 65-h or 240-h incubation, a large percentage of this ganglioside remained undegraded in GM1 gangliosidoses, whereas in the other storage diseases studied, one of its metabolites accumulated by 2-4 fold relative to controls. Labelled GM2 ganglioside accumulated in 4 variants of GM2 gangliosidosis, whereas labelled GM3 ganglioside accumulated in sialidosis, galactosialidoses and sphingolipid activator protein 1 (SAP-1, saposin B) and prosaposin (saposin A, B, C and D) deficient lipidoses. The reduced degradation of GM3 ganglioside in the SAP-1 and prosaposin deficiencies was attributed to the deficient function of SAP-1. The prosaposin deficient cells also showed a reduced re-utilization of radioactive metabolites from GM1 ganglioside (i.e. sphingosine and fatty acid) for phospholipid biosynthesis compared with fibroblasts from the SAP-1 deficient patient or normal controls. This anomaly was ascribed to the previously shown defect in ceramide degradation in prosaposin deficiency. Topics: Child, Preschool; Chromatography, Thin Layer; Fibroblasts; G(M1) Ganglioside; G(M2) Ganglioside; G(M3) Ganglioside; Gangliosidosis, GM1; Glycoproteins; Humans; Infant; Lysosomal Storage Diseases; Neuraminidase; Protein Precursors; Saposins; Skin; Sphingolipid Activator Proteins; Sphingolipidoses	1992

Article

Year

Metabolism of GM1 ganglioside in cultured skin fibroblasts: anomalies in gangliosidoses, sialidoses, and sphingolipid activator protein (SAP, saposin) 1 and prosaposin deficient disorders.

Human genetics, 1992, Volume: 89, Issue:5

Cultured skin fibroblasts from controls and patients with lysosomal storage diseases were loaded with GM1 ganglioside that had been labelled with tritium in its ceramide moiety. After a 65-h or 240-h incubation, a large percentage of this ganglioside remained undegraded in GM1 gangliosidoses, whereas in the other storage diseases studied, one of its metabolites accumulated by 2-4 fold relative to controls. Labelled GM2 ganglioside accumulated in 4 variants of GM2 gangliosidosis, whereas labelled GM3 ganglioside accumulated in sialidosis, galactosialidoses and sphingolipid activator protein 1 (SAP-1, saposin B) and prosaposin (saposin A, B, C and D) deficient lipidoses. The reduced degradation of GM3 ganglioside in the SAP-1 and prosaposin deficiencies was attributed to the deficient function of SAP-1. The prosaposin deficient cells also showed a reduced re-utilization of radioactive metabolites from GM1 ganglioside (i.e. sphingosine and fatty acid) for phospholipid biosynthesis compared with fibroblasts from the SAP-1 deficient patient or normal controls. This anomaly was ascribed to the previously shown defect in ceramide degradation in prosaposin deficiency.

Topics: Child, Preschool; Chromatography, Thin Layer; Fibroblasts; G(M1) Ganglioside; G(M2) Ganglioside; G(M3) Ganglioside; Gangliosidosis, GM1; Glycoproteins; Humans; Infant; Lysosomal Storage Diseases; Neuraminidase; Protein Precursors; Saposins; Skin; Sphingolipid Activator Proteins; Sphingolipidoses

1992