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Immunological Studies on Acidic Sphingomyelinase
1986Intrinsic properties of acidic sphingomyelinase cause major difficulties in attempts to produce a satisfactory antibody. The only two published papers do not carry conviction: the monoclonal antibody described by Freeman et al. (1983) was not demonstrated to precipitate sphingomyelinase activity while monospecificity of the polyclonal antibody prepared
Robert Rousson +2 more
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Acid Sphingomyelinase of Human Brain: Purification to Homogeneity
Journal of Neurochemistry, 1982Abstract: Acid sphingomyelinase (sphingomyelin phosphodiesterase, EC 3.1.4.12) was purified from human brain by extraction with 0.1% Triton X‐100, followed by sequential chromatography on Concanavalin A‐Sepharose, octyl‐Sepharose, hydroxylapatite, DEAE‐cellulose, red A‐agarose, Sephadex G‐200, and DEAE‐cellulose with ampholyte elution ...
T, Yamanaka, K, Suzuki
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Development of carbohydrate-derived inhibitors of acid sphingomyelinase
Bioorganic & Medicinal Chemistry, 2010The acid sphingomyelinase is an emerging drug target, especially for inflammatory lung diseases. Presently, there are no directly-acting potent inhibitors available for cell-based studies. The potent inhibitor phosphatidylinositol-3,5-bisphosphate (PtdIns3,5P2) is not only unsuited for cell culture studies, but also does not provide hints for further ...
Anke G, Roth +2 more
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Potent Inhibition of Acid Sphingomyelinase by Phosphoinositide Analogues
ChemBioChem, 2009AbstractThe different mammalian sphingomyelinases are involved in cell regulation, apoptosis and inflammatory events. Recent reports suggest pharmacological potential especially for inhibitors of the acid sphingomyelinase. Phosphatidyl inositol‐3,5bisphosphate (PtdIns3,5P2) is the most potent selective acid sphingomyelinase inhibitor known to date.
Anke Gundula, Roth +2 more
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Acid and neutral sphingomyelinases: roles and mechanisms of regulation
Biochemistry and Cell Biology, 2004Ceramide, an emerging bioactive lipid and second messenger, is mainly generated by hydrolysis of sphingomyelin through the action of sphingomyelinases. At least two sphingomyelinases, neutral and acid sphingo myelinases, are activated in response to many extracellular stimuli.
Norma, Marchesini, Yusuf A, Hannun
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Current and Emerging Treatments for Acid Sphingomyelinase Deficiency
DrugsAcid sphingomyelinase deficiency is an ultra-rare disease characterised by generalised storage of sphingomyelin, caused by deficiency of the lysosomal enzyme acid sphingomyelinase, owing to the presence of biallelic pathogenic variants in the SMPD1 gene. The main disease manifestations are in the liver, spleen, lung and bone - with some patients having
Tamires Silva Alves +2 more
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The lysosomal targeting of acid sphingomyelinase /
2005Acid sphingomyelinase (ASM), a member of the saposin like protein (SAPLIP) family, is a lysosomal hydrolase that converts sphingomyelin to ceramide. The deficient activity of ASM causes a variant form (i.e., type A/B) of the inherited disorder Niemann-Pick disease. The lysosomal targeting mechanism of ASM has not been conclusively identified.
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Acid sphingomyelinase in steatohepatitis
2016Steatohepatitis (SH) is an intermediate stage of fatty liver disease and one of the most common causes of chronic liver disease worldwide that may progress to cirrhosis and liver cancer. SH encompasses alcoholic (ASH) and nonalcoholic steatohepatitis (NASH), the latter being of particular concern due to its association with obesity and insulin ...
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Update on Functional Inhibitors of Acid Sphingomyelinase (FIASMAs) in SARS-CoV-2 Infection
Pharmaceuticals, 2021Gwenolé Loas, Pascal Le Corre
exaly
[Acid sphingomyelinase deficiency: A review].
La Revue de medecine interneAcid sphingomyelinase deficiency, formerly known as Niemann-Pick disease types B, A/B, and B, is a rare genetic disorder. It is an inherited autosomal recessive disease, linked to mutations in the SMPD1 gene. It is a lysosomal storage disease that leads to the accumulation of sphingomyelin mainly in macrophages, resulting in a multisystemic phenotype ...
Martin, Michaud +3 more
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