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Beschreibung

Sphingomyelin phosphodiesterase 3 (UniProt: Q9NY59, also known as EC: 3.1.4.12, Neutral sphingomyelinase 2, nSMase-2, nSMase2, Neutral sphingomyelinase II) is encoded by the SMPD3 gene (Gene ID: 55512) in human. SMases are classified based on their pH optimum into acid, neutral, and alkaline subtypes. Four different neutral SMases have been described in mammals and nSMase-2 is shown to be the most predominant in cellular systems. nSMase-2 is a phosphoprotein whose activity is regulated by calcineurin (PP2B) and it is shown to be exclusively phosphorylated on serine residues. It is predominantly expressed in the brain and its levels are shown to be up-regulated during G0/G1 phases. Two isoforms of nSMase-2 are reported that are produced by alternative splicing. nSMase-2 catalyzes the generation of bioactive lipid ceramide through the hydrolysis of the membrane lipid sphingomyelin and specifically hydrolyzes the phosphocholine-headgroup from sphingomyelin. It does not exhibit phospholipase C-type activity against phosphatidylcholine, lysophosphatidylcholine, platelet activating factor or lyso-platelet activating factor. For its activity a neutral pH and divalent cations (Mg2+ or Mn2+) are required and its activity is stimulated by the presence of phosphatidylserine (PS) and unsaturated fatty acids. NSMase-2 undergoes palmitoylation and palmitoylation-deficient protein is target for lysosomal degradation. (Ref.: Filosto, S., et al (2010). J. Biol. Chem. 285 (14), 10213-10222, Shamseddine, A.A., et al (2013). Adv. Enz. Regul. 57: 24-41).