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- W1570332911 abstract "Abstract N-(n-Hexyl)-O-glucosylsphingosine completely inhibited β-glucosidase in cultured rat astrocytoma (RGC-6) and mouse neuroblastoma cell strains (NB41A and NB2a), creating a model for the infantile Gaucher nervous system. The inhibitor, at a concentration of 5 µg per ml, caused a 5-fold elevation of glucosylceramide in RGC-6 and a 6-fold elevation in NB41A cells. Under these conditions the growth rates of cells were unaffected. Other lysosomal enzymes were only depressed to approximately 80% of normal with the exception of β-glucuronidase (37% of normal); such reductions would not be anticipated to cause abnormal pathology and none was observed. Studies with glucosyl[14C]ceramide (labeled in the stearoyl moiety) showed that the glycolipid was rapidly taken up from the medium. In the presence of the β-glucosidase inhibitor the uptake of glucosylceramide was reduced in NB2a, NB41A, and RGC-6 cells, and in the latter two cell strains no subsequent catabolism could be detected. Studies with more complex glycolipids, such as gangliosides, showed that they were readily taken up and metabolized and that catabolism was not affected by the inhibitor. This was interpreted as evidence for two β-glucosidases, one which utilizes free glucosylceramide and is deficient in Gaucher's disease and the other which acts as an integral part of a multienzyme complex for the degradation of complex glycolipids and has normal activity in Gaucher's disease. Results indicated that specific catabolic reactions may be inhibited by substrate analogs to simulate the pathology of certain genetic diseases in neurons and glia in tissue culture." @default.
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- W1570332911 date "1974-07-01" @default.
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- W1570332911 title "Inhibition of β-Glucosidase by N-(n-Hexyl)-O-glucosylsphingosine in Cell Strains of Neurological Origin" @default.
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- W1570332911 doi "https://doi.org/10.1016/s0021-9258(19)42466-6" @default.
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