title: Sphingomyelinases in human tissues. III. Expression of Niemann-Pick disease in cultured skin fibroblasts.
abstract: Sphingomyelinase was effectively extracted cultured fibroblasts homogenized in 1% glycine. The average specific activity was 24.6 nmol substrate hydrolyzed per hr per mg protein. Cultured cells from two cases of Niemann-Pick disease type A and one case of type B had markedly reduced enzyme activity, whereas, in type E cells, total activity was twice normal. Sphingomyelinase was resolved by isoelectric focusing into three peaks of activity (I-II), where I and II were the major forms. Species I had a pI of 4.6, II a pI of 4.8, and III a pI of 5.0. All three peaks, although markedly reduced, were present in cell extracts from both types A and B. All species of enzyme in B cells were found at higher levels than in A cells. Cultured cells from a case of type E contained sphingomyelinase I at a level several fold higher than normal, species II was absent, whereas III was found at near normal levels.
mesh_terms: D002478:Cells, Cultured; D005347:Fibroblasts / Q000201:enzymology; D005696:Galactosidases / Q000302:isolation & purification; D006596:Hexosaminidases / Q000302:isolation & purification; D006801:Humans; D007525:Isoelectric Focusing; D009542:Niemann-Pick Diseases / Q000201:enzymology*; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification*; D012867:Skin / Q000201:enzymology; D013108:Sphingomyelin Phosphodiesterase / Q000302:isolation & purification*
chemical_list: D010727:Phosphoric Diester Hydrolases; D013108:Sphingomyelin Phosphodiesterase; D005696:Galactosidases; D006596:Hexosaminidases