Schuchman, E.H., Desnick, R.J., Types A and B Niemann-Pick disease. Mol. Genet. Metab. 120 (2017), 27–33.
Schuchman, E.H., The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease. J. Inherit. Metab. Dis. 30 (2007), 654–663.
Otterbach, B., Stoffel, W., Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease). Cell 81 (1995), 1053–1061.
McGovern, M.M., Avetisyan, R., Sanson, B.-J., et al. Disease manifestations and burden of illness in patients with acid sphingomyelinase deficiency (ASMD). Orphanet J. Rare Dis., 12, 2017, 41.
Jessop, E., Upadhyaya, S., Ultra orphan drugs: the NHS model for managing extremely rare diseases. Expert Opin. Orphan Drugs 2 (2014), 1301–1308.
Wasserstein, M.P., Diaz, G.A., Lachmann, R.H., et al. Olipudase alfa for treatment of acid sphingomyelinase deficiency (ASMD): safety and efficacy in adults treated for 30 months. J. Inherit. Metab. Dis., 2018, 1–10.
A Long-term study of olipudase alfa in patients with acid sphingomyelinase deficiency. ClinicalTrials.gov, < https://clinicaltrials.gov/ct2/show/NCT02004704> (accessed 20 July 2018).
Efficacy, safety, pharmacodynamic, and pharmacokinetics study of olipudase alfa in patients with acid sphingomyelinase deficiency. ClinicalTrials.gov, < https://clinicaltrials.gov/ct2/show/NCT02004691> (accessed 20 July 2018).
Safety, tolerability, PK, and efficacy evaluation of repeat ascending doses of olipudase Alfa in pediatric patients <18 Years of age with acid sphingomyelinase deficiency. ClinicalTrials.gov, < https://clinicaltrials.gov/ct2/show/NCT02292654> (accessed 20 July 2018).
Murray, J.M., Thompson, A.M., Vitsky, A., et al. Nonclinical safety assessment of recombinant human acid sphingomyelinase (rhASM) for the treatment of acid sphingomyelinase deficiency: the utility of animal models of disease in the toxicological evaluation of potential therapeutics. Mol. Genet. Metab. 114 (2015), 217–225.
Kolesnick, R., The therapeutic potential of modulating the ceramide/sphingomyelin pathway. J. Clin. Invest. 110 (2002), 3–8.
Spiegel, S., Merrill, A.H., Sphingolipid metabolism and cell growth regulation. FASEB J. 10 (1996), 1388–1397.
E. Gulbins, S.Walter, K.A. Becker, et al., A central role for the acid sphingomyelinase/ceramide system in neurogenesis and major depression. J. Neurochem. 134, 183–192.
Levade, T., Augé N., Veldman, R.J., et al. Sphingolipid mediators in cardiovascular cell biology and pathology. Circ. Res. 89 (2001), 957–968.
Ferlinz, K., Hurwitz, R., Vielhaber, G., et al. Occurrence of two molecular forms of human acid sphingomyelinase. Biochem. J. 301 (1994), 855–862.
Dhami, R., Schuchman, E.H., Mannose 6-phosphate receptor-mediated uptake is defective in acid sphingomyelinase-deficient macrophages: implications for Niemann-Pick disease enzyme replacement therapy. J. Biol. Chem. 279 (2004), 1526–1532.
Rappaport, J., Garnacho, C., Muro, S., Clathrin-mediated endocytosis is impaired in type A-B Niemann-Pick disease model cells and can be restored by ICAM-1-mediated enzyme replacement. Mol. Pharm. 11 (2014), 2887–2895.
Rappaport, J., Manthe, R.L., Garnacho, C., et al. Altered clathrin-independent endocytosis in type A Niemann-Pick disease cells and rescue by ICAM-1-targeted enzyme delivery. Mol. Pharm. 12 (2015), 1366–1376.
Fu, K., Pack, D.W., Klibanov, A.M., et al. Visual evidence of acidic environment within degrading poly(lactic-co-glycolic acid) (PLGA) microspheres. Pharm. Res. 17 (2000), 100–106.
van de Weert, M., Hennink, W.E., Jiskoot, W., Protein instability in poly(lactic-co-glycolic acid) microparticles. Pharm. Res. 17 (2000), 1159–1167.
Sercombe, L., Veerati, T., Moheimani, F., et al. Advances and challenges of liposome assisted drug delivery. Front. Pharmacol., 6, 2015, 286.
Ahsan, F., Rivas, I.P., Khan, M.A., et al. Targeting to macrophages: role of physicochemical properties of particulate carriers–liposomes and microspheres–on the phagocytosis by macrophages. J. Control. Release 79 (2002), 29–40.
Dhami, R., He, X., Gordon, R.E., et al. Analysis of the lung pathology and alveolar macrophage function in the acid sphingomyelinase deficient mouse model of Niemann-Pick disease. Lab. Invest. 81 (2001), 987–999.
Daemen, T., Velinova, M., Regts, J., et al. Different intrahepatic distribution of phosphatidylglycerol and phosphatidylserine liposomes in the rat. Hepatology 26 (1997), 416–423.
Semple, S.C., Chonn, A., Cullis, P.R., Interactions of liposomes and lipid-based carrier systems with blood proteins: relation to clearance behaviour in vivo. Adv. Drug Deliv. Rev. 32 (1998), 3–17.
Liu, D., Liu, F., Song, Y.K., Recognition and clearance of liposomes containing phosphatidylserine are mediated by serum opsonin. Biochim. Biophys. Acta 1235 (1995), 140–146.
Scherphof, G., Roerdink, F., Waite, M., et al. Disintegration of phosphatidylcholine liposomes in plasma as a result of interaction with high-density lipoproteins. Biochim. Biophys. Acta 542 (1978), 296–307.
Harashima, H., Sakata, K., Funato, K., et al. Enhanced hepatic uptake of liposomes through complement activation depending on the size of liposomes. Pharm. Res. 11 (1994), 402–406.
Aggarwal, P., Hall, J.B., McLeland, C.B., et al. Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv. Drug Deliv. Rev. 61 (2009), 428–437.
Linke, T., Wilkening, G., Lansmann, S., et al. Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins. Biol. Chem. 382 (2001), 283–290.
Xiong, Z.-J., Huang, J., Poda, G., et al. Structure of human acid sphingomyelinase reveals the role of the saposin domain in activating substrate hydrolysis. J. Mol. Biol. 428 (2016), 3026–3042.
Möbius, W., van Donselaar, E., Ohno-Iwashita, Y., et al. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 4 (2003), 222–231.
Oninla, V.O., Breiden, B., Babalola, J.O., et al. Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2. J. Lipid Res. 55 (2014), 2606–2619.
Jenkins, R.W., Canals, D., Hannun, Y.A., Roles and regulation of secretory and lysosomal acid sphingomyelinase. Cell. Signal. 21 (2009), 836–846.
de Vries, R.P., de Vries, E., Bosch, B.J., et al. The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity. Virology 403 (2010), 17–25.
Moll, M., Kaufmann, A., Maisner, A., Influence of N-glycans on processing and biological activity of the nipah virus fusion protein. J. Virol. 78 (2004), 7274–7278.
Freeze, H.H., Kranz, C., Endoglycosidase and glycoamidase release of N-linked glycans. Curr. Protoc. Mol. Biol., 0, 2010, 17, 10.1002/0471142727.mb1713as89 Epub ahead of print January.
Zhang, H., Thin-film hydration followed by extrusion method for liposome preparation. Methods Mol. Biol. 1522 (2017), 17–22.
Fiske, C.H., Subbarow, Y., The colorimetric determination of phosphorus. J. Biol. Chem. 66 (1925), 375–400.
Bligh, E.G., Dyer, W.J., A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37 (1959), 911–917.
Voorink-Moret, M., Goorden, S.M.I., van Kuilenburg, A.B.P., et al. Rapid screening for lipid storage disorders using biochemical markers. Mol. Genet. Metab. 123 (2018), 76–84.
Hasilik, A., The early and late processing of lysosomal enzymes: proteolysis and compartmentation. Experientia 48 (1992), 130–151.
von Figura, K., Hasilik, A., Lysosomal enzymes and their receptors. Annu. Rev. Biochem. 55 (1986), 167–193.
Lansmann, S., Ferlinz, K., Hurwitz, R., et al. Purification of acid sphingomyelinase from human placenta: characterization and N-terminal sequence. FEBS Lett. 399 (1996), 227–231.
Qiu, H., Edmunds, T., Baker-Malcolm, J., et al. Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine. J. Biol. Chem. 278 (2003), 32744–32752.
Dalton, A.C., Barton, W.A., Over-expression of secreted proteins from mammalian cell lines. Protein Sci. 23 (2014), 517–525.
He, X., Miranda, S.R., Xiong, X., et al. Characterization of human acid sphingomyelinase purified from the media of overexpressing Chinese hamster ovary cells. Biochim. Biophys. Acta 1432 (1999), 251–264.
Kang, J.H., Jang, W.Y., Ko, Y.T., The effect of surface charges on the cellular uptake of liposomes investigated by live cell imaging. Pharm. Res. 34 (2017), 704–717.
Kamps, J., Scherphof, G., Receptor versus non-receptor mediated clearance of liposomes. Adv. Drug Deliv. Rev. 32 (1998), 81–97.
Adler, J., Parmryd, I., Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient. Cytometry A 77 (2010), 733–742.
Chuang, W.-L., Pacheco, J., Cooper, S., et al. Lyso-sphingomyelin is elevated in dried blood spots of Niemann-Pick B patients. Mol. Genet. Metab. 111 (2014), 209–211.
Kolter, T., Sandhoff, K., Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol. 21 (2005), 81–103.
World Medical Association, World Medical Association Declaration of Helsinki: ethical principles for medical research involving human subjects. JAMA 310 (2013), 2191–2194.
