What is ASM—Acid sphingomyelinase?

Acid sphingomyelinase(ASM, EC 3.1.4.12) is a lysosomal glycoprotein that catalyses the hydrolysis of sphingomyelin into ceramide and phosphorylcholine. Fusion of secretory lysosomes with the corpuscle apparent and about-face of lysosomal ASM assimilate the alien advertisement of the corpuscle film plays an important role during accent acknowledgment. CD95 ligands and cytokines such as bump afterlife factor-α, interleukin-1 and interferon-γ but aswell added stimuli including oxidative stress, acknowledging oxygen and nitrogen species, ionizing radiation, UV-C radiation, calefaction shock and added agents of stress, abrasion or infections by HIV or bacilli accept been apparent to activate ceramide assembly, affected to be in allotment due to added ASM activity. Ceramide, in turn, leads to film about-face and after signalling that after-effects in corpuscle activation, actual generally corpuscle accent or apoptosis. In accession to ASM, at atomic three added sphingomyelinases accept been declared in beastly beef that alter in their pH optimum and cofactor dependency. Although these enzymes and an absolute de novo amalgam alleyway are another mechanisms for ceramide generation, activation of ASM itself has been accurate to be analytical for some cellular responses, such as apoptosis induced by acknowledging oxygen and nitrogen breed, chemotherapy drugs such as cisplatin, bacilli, radiation and CD95. Furthermore, in adverse to added sphingomyelinases, ASM action is deeply adapted
Acid sphingomyelinase is best known for its involvement in the lysosomal storage disorder Niemann-Pick disease (NPD). Through studies that began by investigating this rare disease, recent findings have uncovered the important role of this enzyme in the initiation of ceramide-mediated signal transduction. This unique function involves translocation of the enzyme from intracellular compartments to the outer leaflet of the cell membrane, where hydrolysis of sphingomyelin into ceramide initiates membrane reorganization and facilitates the formation and coalescence of lipid microdomains.
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