Results 151 to 160 of about 6,648 (196)
New insights on the use of desipramine as an inhibitor for acid ceramidase
FEBS Letters, 2006 Treatment of different cancer cell lines with desipramine induced a time- and dose-dependent downregulation of acid ceramidase. Desipramine’s effect on acid ceramidase appeared specific for amphiphilic agents (desipramine, chlorpromazine, and chloroquine)
James Norris +2 more
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Sphingolipids and acid ceramidase as therapeutic targets in cancer therapy [PDF]
Critical Reviews in Oncology/Hematology, 2019 Background: Sphingolipids have been shown to play a key part in cancer cell growth and death and have increasingly become the subject of novel anti-cancer therapies.
Dale Vimalachandran +2 more
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Purification and characterization of human intestinal neutral ceramidase
Biochimie, 2007 Sphingolipids are degraded by sphingomyelinase and ceramidase in the gut to ceramide and sphingosine, which may inhibit cell proliferation and induce apoptosis, and thus have anti-tumour effects in the gut.
Lena Ohlsson +2 more
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Acid ceramidase and human disease
Biochimica Et Biophysica Acta - Biomembranes, 2006 Acid ceramidase (N-acylsphingosine deacylase, EC 3.5.1.23; AC) is the lipid hydrolase responsible for the degradation of ceramide into sphingosine and free fatty acids within lysosomes. The enzymatic activity was first identified over four decades ago, and is deficient in the inherited lipid storage disorder, Farber Lipogranulomatosis (Farber disease).
Edward H Schuchman, Jae Ho Park
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Chemistry and Physics of Lipids, 2016
The topic of ceramidases has experienced an enormous boost during the last few years. Ceramidases catalyze the degradation of ceramide to sphingosine and fatty acids. Ceramide is not only the central hub of sphingolipid biosynthesis and degradation, it is also a key molecule in sphingolipid signaling, promoting differentiation or apoptosis.
Essa M, Saied, Christoph, Arenz
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The topic of ceramidases has experienced an enormous boost during the last few years. Ceramidases catalyze the degradation of ceramide to sphingosine and fatty acids. Ceramide is not only the central hub of sphingolipid biosynthesis and degradation, it is also a key molecule in sphingolipid signaling, promoting differentiation or apoptosis.
Essa M, Saied, Christoph, Arenz
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The molecular medicine of acid ceramidase
Biological Chemistry, 2015Abstract Acid ceramidase (N-acylsphingosine deacylase, EC 3.5.1.23; AC) is the lipid hydrolase responsible for the degradation of ceramide into sphingosine and free fatty acids within lysosomes. The enzymatic activity was first identified over four decades ago and is deficient in two rare inherited disorders, Farber lipogranulomatosis (Farber disease ...
Michael, Frohbergh +2 more
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Acid and alkaline ceramidases of rat tissues
Biochemistry and Cell Biology, 1986Ceramidase (N-acylsphingosine deacylase) was measured in rat tissue homogenates with N-[1-14C]oleoyl- and N-[9,10-3H]palmitoyl-sphingosine. Two activities were observed with pH optima of approximately 5 and 8. The activity at pH 8 exceeded that at pH 5 in all tissues and tissue areas examined, and both activities decreased in the following order ...
M W, Spence, S, Beed, H W, Cook
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Alkaline sphingomyelinases and ceramidases of the gastrointestinal tract
Chemistry and Physics of Lipids, 1999In addition to the acid and neutral sphingomyelinases (SMase) that occur in most tissues, distinct alkaline sphingomyelinases occur in the mucosa of the gastrointestinal tract and human bile. These enzymes exhibit characteristic properties with regard to bile-salt dependence, protease resistance, and longitudinal distribution in the gut. Alkaline SMase
A, Nilsson, R D, Duan
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Ceramidase Deficiency in Farber's Disease (Lipogranulomatosis)
Science, 1972Ceramidase activity could not be demonstrated in the kidney and cerebellum from a deceased patient with Farber's disease, whereas the activities of six control acid hydrolase enzymes appeared normal. This enzyme defect presumably accounts for the accumulation that has been described in two patients and may represent the biochemical basis of this ...
M, Sugita, J T, Dulaney, H W, Moser
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