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Review Article

Treatment of Anderson-Fabry Disease

Author(s): Irene Simonetta*, Antonino Tuttolomondo, Mario Daidone, Salvatore Miceli and Antonio Pinto

Volume 26, Issue 40, 2020

Page: [5089 - 5099] Pages: 11

DOI: 10.2174/1381612826666200317142412

Abstract

Fabry disease is an X-linked disorder of glycosphingolipid metabolism that results in progressive accumulation of neutral glycosphingolipids, predominantly globotriaosylsphingosine (Gb3) in lysosomes, as well as other cellular compartments of several tissues, causing multi-organ manifestations (acroparesthesias, hypohidrosis, angiokeratomas, signs and symptoms of cardiac, renal, cerebrovascular involvement). Pathogenic mutations lead to a deficiency of the lysosomal enzyme alpha-galactosidase A (GLA). In the presence of high clinical suspicion, a careful physical examination and specific laboratory tests are required. Finally, the diagnosis of Fabry’s disease is confirmed by the demonstration of the absence of or reduced alpha-galactosidase A enzyme activity in hemizygous men and gene typing in heterozygous females. Measurement of the biomarkers Gb3 and Lyso Gb3 in biological specimens may facilitate diagnosis. The current treatment of Anderson-Fabry disease is represented by enzyme replacement therapy (ERT) and oral pharmacological chaperone. Future treatments are based on new strategic approaches such as stem cell-based therapy, pharmacological approaches chaperones, mRNA therapy, and viral gene therapy.

This review outlines the current therapeutic approaches and emerging treatment strategies for Anderson-Fabry disease.

Keywords: Fabry disease, enzyme replacement therapy, gene therapy, viral vectors, chaperone therapy, pharmacological.

« Previous Next »
[1]
Biegstraaten M, Arngrímsson R, Barbey F, et al. Recommendations for initiation and cessation of enzyme replacement therapy in patients with Fabry disease: the European Fabry Working Group consensus document. Orphanet J Rare Dis 2015; 10: 36.
[http://dx.doi.org/10.1186/s13023-015-0253-6] [PMID: 25885911]
[2]
Rombach SM, Smid BE, Bouwman MG, Linthorst GE, Dijkgraaf MGW, Hollak CEM. Long term enzyme replacement therapy for Fabry disease: effectiveness on kidney, heart and brain. Orphanet J Rare Dis 2013; 8: 47.
[http://dx.doi.org/10.1186/1750-1172-8-47] [PMID: 23531228]
[3]
Guidelines - KDIGO Available from https://kdigo.org/guidelines/
[4]
ESC Clinical Practice Guidelines https://www.escardio.org/Guidelines/Clinical
[5]
Viechtbauer W. Conducting meta-analyses in R with the metafor package. J Stat Softw 2010; 36: 1-48.
[http://dx.doi.org/10.18637/jss.v036.i03]
[6]
Weidemann F, Niemann M, Störk S, et al. Long-term outcome of enzyme-replacement therapy in advanced Fabry disease: evidence for disease progression towards serious complications. J Intern Med 2013; 274(4): 331-41.
[http://dx.doi.org/10.1111/joim.12077] [PMID: 23586858]
[7]
Wilcox WR, Banikazemi M, Guffon N, et al. International Fabry Disease Study Group Long-term safety and efficacy of enzyme replacement therapy for Fabry disease. Am J Hum Genet 2004; 75(1): 65-74.
[http://dx.doi.org/10.1086/422366] [PMID: 15154115]
[8]
Germain DP, Charrow J, Desnick RJ, et al. Ten-year outcome of enzyme replacement therapy with agalsidase beta in patients with Fabry disease. J Med Genet 2015; 52(5): 353-8.
[http://dx.doi.org/10.1136/jmedgenet-2014-102797] [PMID: 25795794]
[9]
Tøndel C, Bostad L, Larsen KK, et al. Agalsidase benefits renal histology in young patients with Fabry disease. J Am Soc Nephrol 2013; 24(1): 137-48.
[http://dx.doi.org/10.1681/ASN.2012030316] [PMID: 23274955]
[10]
Skrunes R, Tøndel C, Leh S, et al. Long-term dose-dependent agalsidase effects on kidney histology in Fabry disease. Clin J Am Soc Nephrol 2017; 12(9): 1470-9.
[http://dx.doi.org/10.2215/CJN.01820217] [PMID: 28625968]
[11]
Spada M, Baron R, Elliott PM, et al. The effect of enzyme replacement therapy on clinical outcomes in paediatric patients with Fabry disease - A systematic literature review by a European panel of experts. Mol Genet Metab 2019; 126(3): 212-23.
[http://dx.doi.org/10.1016/j.ymgme.2018.04.007] [PMID: 29785937]
[12]
Tsujiuchi M, Ebato M, Maezawa H, et al. Long-term effects of enzyme replacement therapy for Anderson-Fabry Disease. Int Heart J 2019; 60(1): 208-14.
[http://dx.doi.org/10.1536/ihj.17-688] [PMID: 30464119]
[13]
Ortiz A, Abiose A, Bichet DG, et al. Time to treatment benefit for adult patients with Fabry disease receiving agalsidase β: data from the Fabry Registry. J Med Genet 2016; 53(7): 495-502.
[http://dx.doi.org/10.1136/jmedgenet-2015-103486] [PMID: 26993266]
[14]
Sheppard MN, Cane P, Florio R, et al. A detailed pathologic examination of heart tissue from three older patients with Anderson-Fabry disease on enzyme replacement therapy. Cardiovasc Pathol 2010; 19(5): 293-301.
[http://dx.doi.org/10.1016/j.carpath.2009.05.003] [PMID: 19631563]
[15]
Wanner C, Germain DP, Hilz MJ, Spada M, Falissard B, Elliott PM. Therapeutic goals in Fabry disease: Recommendations of a European expert panel, based on current clinical evidence with enzyme replacement therapy. Mol Genet Metab 2019; 126(3): 210-1.
[http://dx.doi.org/10.1016/j.ymgme.2018.04.004] [PMID: 29724657]
[16]
Tuttolomondo A, Simonetta I, Duro G, et al. Inter-familial and intra-familial phenotypic variability in three Sicilian families with Anderson-Fabry disease. Oncotarget 2017; 8(37): 61415-24.
[http://dx.doi.org/10.18632/oncotarget.18250] [PMID: 28977874]
[17]
Sheng S, Wu L, Nalleballe K, et al. Fabry’s disease and stroke: Effectiveness of enzyme replacement therapy (ERT) in stroke prevention, a review with meta-analysis. J Clin Neurosci 2019; 65: 83-6.
[http://dx.doi.org/10.1016/j.jocn.2019.03.064] [PMID: 30955952]
[18]
Lenders M, Brand E. Effects of enzyme replacement therapy and antidrug antibodies in patients with Fabry disease. J Am Soc Nephrol 2018; 29(9): 2265-78.
[http://dx.doi.org/10.1681/ASN.2018030329] [PMID: 30093456]
[19]
Schiffmann R, Kopp JB, Austin HA III, et al. Enzyme replacement therapy in Fabry disease: a randomized controlled trial. JAMA 2001; 285(21): 2743-9.
[http://dx.doi.org/10.1001/jama.285.21.2743] [PMID: 11386930]
[20]
Beck M, Hughes D, Kampmann C, et al. Fabry Outcome Survey Study Group Long-term effectiveness of agalsidase alfa enzyme replacement in Fabry disease: A Fabry Outcome Survey analysis. Mol Genet Metab Rep 2015; 3: 21-7.
[http://dx.doi.org/10.1016/j.ymgmr.2015.02.002] [PMID: 26937390]
[21]
Schiffmann R, Ries M, Timmons M, Flaherty JT, Brady RO. Long-term therapy with agalsidase alfa for Fabry disease: safety and effects on renal function in a home infusion setting. Nephrol Dial Transplant 2006; 21(2): 345-54.
[http://dx.doi.org/10.1093/ndt/gfi152] [PMID: 16204287]
[22]
Feriozzi S, Torras J, Cybulla M, Nicholls K, Sunder-Plassmann G, West M. FOS Investigators. The effectiveness of long-term agalsidase alfa therapy in the treatment of Fabry nephropathy. Clin J Am Soc Nephrol 2012; 7(1): 60-9.
[http://dx.doi.org/10.2215/CJN.03130411] [PMID: 22246281]
[23]
Weidemann F, Krämer J, Duning T, et al. Patients with Fabry disease after enzyme replacement therapy dose reduction versus treatment switch. J Am Soc Nephrol 2014; 25(4): 837-49.
[http://dx.doi.org/10.1681/ASN.2013060585] [PMID: 24556354]
[24]
Breunig F, Weidemann F, Strotmann J, Knoll A, Wanner C. Clinical benefit of enzyme replacement therapy in Fabry disease. Kidney Int 2006; 69(7): 1216-21.
[http://dx.doi.org/10.1038/sj.ki.5000208] [PMID: 16609685]
[25]
Warnock DG, Ortiz A, Mauer M, et al. Fabry Registry. Renal outcomes of agalsidase beta treatment for Fabry disease: role of proteinuria and timing of treatment initiation. Nephrol Dial Transplant 2012; 27(3): 1042-9.
[http://dx.doi.org/10.1093/ndt/gfr420] [PMID: 21804088]
[26]
Warnock DG, Thomas CP, Vujkovac B, et al. Antiproteinuric therapy and Fabry nephropathy: factors associated with preserved kidney function during agalsidase-beta therapy. J Med Genet 2015; 52(12): 860-6.
[http://dx.doi.org/10.1136/jmedgenet-2015-103471] [PMID: 26490103]
[27]
Whybra C, Miebach E, Mengel E, et al. A 4-year study of the efficacy and tolerability of enzyme replacement therapy with agalsidase alfa in 36 women with Fabry disease. Genet Med 2009; 11(6): 441-9.
[http://dx.doi.org/10.1097/GIM.0b013e3181a23bec] [PMID: 19346951]
[28]
Kampmann C, Perrin A, Beck M. Effectiveness of agalsidase alfa enzyme replacement in Fabry disease: cardiac outcomes after 10 years’ treatment. Orphanet J Rare Dis 2015; 10: 125.
[http://dx.doi.org/10.1186/s13023-015-0338-2] [PMID: 26416388]
[29]
Schiffmann R, Pastores GM, Lien Y-HH, et al. Agalsidase alfa in pediatric patients with Fabry disease: a 6.5-year open-label follow-up study. Orphanet J Rare Dis 2014; 9: 169.
[http://dx.doi.org/10.1186/s13023-014-0169-6] [PMID: 25425121]
[30]
Weidemann F, Breunig F, Beer M, et al. Improvement of cardiac function during enzyme replacement therapy in patients with Fabry disease: a prospective strain rate imaging study. Circulation 2003; 108(11): 1299-301.
[http://dx.doi.org/10.1161/01.CIR.0000091253.71282.04] [PMID: 12952834]
[31]
Spinelli L, Pisani A, Sabbatini M, et al. Enzyme replacement therapy with agalsidase beta improves cardiac involvement in Fabry’s disease. Clin Genet 2004; 66(2): 158-65.
[http://dx.doi.org/10.1111/j.1399-0004.2004.00284.x] [PMID: 15253767]
[32]
Weidemann F, Niemann M, Breunig F, et al. Long-term effects of enzyme replacement therapy on fabry cardiomyopathy: evidence for a better outcome with early treatment. Circulation 2009; 119(4): 524-9.
[http://dx.doi.org/10.1161/CIRCULATIONAHA.108.794529] [PMID: 19153271]
[33]
Machann W, Breunig F, Weidemann F, et al. Cardiac energy metabolism is disturbed in Fabry disease and improves with enzyme replacement therapy using recombinant human galactosidase A. Eur J Heart Fail 2011; 13(3): 278-83.
[http://dx.doi.org/10.1093/eurjhf/hfq211] [PMID: 21149315]
[34]
Moore DF, Scott LT, Gladwin MT, et al. Regional cerebral hyperperfusion and nitric oxide pathway dysregulation in Fabry disease: reversal by enzyme replacement therapy. Circulation 2001; 104(13): 1506-12.
[http://dx.doi.org/10.1161/hc3801.096352] [PMID: 11571244]
[35]
Fellgiebel A, Gartenschläger M, Wildberger K, Scheurich A, Desnick RJ, Sims K. Enzyme replacement therapy stabilized white matter lesion progression in Fabry disease. Cerebrovasc Dis 2014; 38(6): 448-56.
[http://dx.doi.org/10.1159/000369293] [PMID: 25502511]
[36]
Beck M, Ricci R, Widmer U, et al. Fabry disease: overall effects of agalsidase alfa treatment. Eur J Clin Invest 2004; 34(12): 838-44.
[http://dx.doi.org/10.1111/j.1365-2362.2004.01424.x] [PMID: 15606727]
[37]
Hoffmann B, Beck M, Sunder-Plassmann G, Borsini W, Ricci R, Mehta A. FOS European Investigators. Nature and prevalence of pain in Fabry disease and its response to enzyme replacement therapy--a retrospective analysis from the Fabry Outcome Survey. Clin J Pain 2007; 23(6): 535-42.
[http://dx.doi.org/10.1097/AJP.0b013e318074c986] [PMID: 17575495]
[38]
Hilz MJ, Brys M, Marthol H, Stemper B, Dütsch M. Enzyme replacement therapy improves function of C-, Adelta-, and Abeta-nerve fibers in Fabry neuropathy. Neurology 2004; 62(7): 1066-72.
[http://dx.doi.org/10.1212/01.WNL.0000118207.84514.40] [PMID: 15079003]
[39]
Dehout F, Roland D, Treille de Granseigne S, Guillaume B, Van Maldergem L. Relief of gastrointestinal symptoms under enzyme replacement therapy in patients with Fabry disease. J Inherit Metab Dis 2004; 27(4): 499-505.
[http://dx.doi.org/10.1023/B:BOLI.0000037342.59612.69] [PMID: 15303007]
[40]
Hoffmann B, Schwarz M, Mehta A, Keshav S. Fabry Outcome Survey European Investigators Gastrointestinal symptoms in 342 patients with Fabry disease: prevalence and response to enzyme replacement therapy. Clin Gastroenterol Hepatol 2007; 5(12): 1447-53.
[http://dx.doi.org/10.1016/j.cgh.2007.08.012] [PMID: 17919989]
[41]
Banikazemi M, Ullman T, Desnick RJ. Gastrointestinal manifestations of Fabry disease: clinical response to enzyme replacement therapy. Mol Genet Metab 2005; 85(4): 255-9.
[http://dx.doi.org/10.1016/j.ymgme.2005.04.009] [PMID: 15939645]
[42]
Wilcox WR, Feldt-Rasmussen U, Martins AM, et al. Improvement of Fabry disease-related gastrointestinal symptoms in a significant proportion of female patients treated with agalsidase beta: data from the fabry registry. JIMD Rep 2018; 38: 45-51.
[http://dx.doi.org/10.1007/8904_2017_28] [PMID: 28510034]
[43]
Linthorst GE, Hollak CEM, Donker-Koopman WE, Strijland A, Aerts JMFG. Enzyme therapy for Fabry disease: neutralizing antibodies toward agalsidase alpha and beta. Kidney Int 2004; 66(4): 1589-95.
[http://dx.doi.org/10.1111/j.1523-1755.2004.00924.x] [PMID: 15458455]
[44]
Smid BE, Hoogendijk SL, Wijburg FA, Hollak CEM, Linthorst GE. A revised home treatment algorithm for Fabry disease: influence of antibody formation. Mol Genet Metab 2013; 108(2): 132-7.
[http://dx.doi.org/10.1016/j.ymgme.2012.12.005] [PMID: 23332169]
[45]
Rombach SM, Aerts JMFG, Poorthuis BJHM, et al. Long-term effect of antibodies against infused alpha-galactosidase A in Fabry disease on plasma and urinary (lyso)Gb3 reduction and treatment outcome. PLoS One 2012; 7(10)e47805
[http://dx.doi.org/10.1371/journal.pone.0047805] [PMID: 23094092]
[46]
Lidove O, West ML, Pintos-Morell G, et al. Effects of enzyme replacement therapy in Fabry disease--a comprehensive review of the medical literature. Genet Med 2010; 12(11): 668-79.
[http://dx.doi.org/10.1097/GIM.0b013e3181f13b75] [PMID: 20962662]
[47]
Keating GM, Simpson D. Agalsidase Beta: a review of its use in the management of Fabry disease. Drugs 2007; 67(3): 435-55.
[http://dx.doi.org/10.2165/00003495-200767030-00007] [PMID: 17335299]
[48]
Vedder AC, Breunig F, Donker-Koopman WE, et al. Treatment of Fabry disease with different dosing regimens of agalsidase: effects on antibody formation and GL-3. Mol Genet Metab 2008; 94(3): 319-25.
[http://dx.doi.org/10.1016/j.ymgme.2008.03.003] [PMID: 18424138]
[49]
Banikazemi M, Bultas J, Waldek S, et al. Fabry Disease Clinical Trial Study Group Agalsidase-beta therapy for advanced Fabry disease: a randomized trial. Ann Intern Med 2007; 146(2): 77-86.
[http://dx.doi.org/10.7326/0003-4819-146-2-200701160-00148] [PMID: 17179052]
[50]
Lenders M, Stypmann J, Duning T, Schmitz B, Brand S-M, Brand E. Serum-mediated inhibition of enzyme replacement therapy in fabry disease. J Am Soc Nephrol 2016; 27(1): 256-64.
[http://dx.doi.org/10.1681/ASN.2014121226] [PMID: 25933799]
[51]
Wachholz PA, Durham SR. Induction of ‘blocking’ IgG antibodies during immunotherapy. Clin Exp Allergy 2003; 33(9): 1171-4.
[http://dx.doi.org/10.1046/j.1365-2222.2003.01765.x] [PMID: 12956735]
[52]
Banugaria SG, Prater SN, McGann JK, et al. Bortezomib in the rapid reduction of high sustained antibody titers in disorders treated with therapeutic protein: lessons learned from Pompe disease. Genet Med 2013; 15(2): 123-31.
[http://dx.doi.org/10.1038/gim.2012.110] [PMID: 23060045]
[53]
Lenders M, Schmitz B, Brand S-M, Foell D, Brand E. Characterization of drug-neutralizing antibodies in patients with Fabry disease during infusion. J Allergy Clin Immunol 2018; 141(6): 2289-92.e7.
[http://dx.doi.org/10.1016/j.jaci.2017.12.1001] [PMID: 29421273]
[54]
Warnock DG, Bichet DG, Holida M, et al. Oral migalastat HCl leads to greater systemic exposure and tissue levels of active α-galactosidase A in Fabry patients when co-administered with infused agalsidase. PLoS One 2015; 10(8)e0134341
[http://dx.doi.org/10.1371/journal.pone.0134341] [PMID: 26252393]
[55]
Sunder-Plassmann G, Schiffmann R, Nicholls K. Migalastat for the treatment of Fabry disease. Expert Opin Orphan Drugs 2018; 6: 301-9.
[http://dx.doi.org/10.1080/21678707.2018.1469978]
[56]
Approves Galafold FDA. FDA Approves Galafold (migalastat) for the treatment of Fabry disease. Available from: https://www.drugs.com/newdrugs/fda-approves-galafold-migalastat-fabry-4797.html
[57]
Hughes DA, Nicholls K, Sunder-Plassmann G, et al. Safety of switching to Migalastat from enzyme replacement therapy in Fabry disease: Experience from the Phase 3 ATTRACT study. Am J Med Genet A 2019; 179(6): 1069-73.
[http://dx.doi.org/10.1002/ajmg.a.61105] [PMID: 30920142]
[58]
Hughes DA, Nicholls K, Shankar SP, et al. Oral pharmacological chaperone migalastat compared with enzyme replacement therapy in Fabry disease: 18-month results from the randomised phase III ATTRACT study. J Med Genet 2017; 54(4): 288-96.
[http://dx.doi.org/10.1136/jmedgenet-2016-104178] [PMID: 27834756]
[59]
Germain DP, Nicholls K, Giugliani R, et al. Efficacy of the pharmacologic chaperone migalastat in a subset of male patients with the classic phenotype of Fabry disease and migalastat-amenable variants: data from the phase 3 randomized, multicenter, double-blind clinical trial and extension study. Genet Med 2019; 21(9): 1987-97.
[http://dx.doi.org/10.1038/s41436-019-0451-z] [PMID: 30723321]
[60]
Arenz C. Recent advances and novel treatments for sphingolipidoses. Future Med Chem 2017; 9(14): 1687-700.
[http://dx.doi.org/10.4155/fmc-2017-0065] [PMID: 28857617]
[61]
Ashe KM, Budman E, Bangari DS, et al. Efficacy of enzyme and substrate reduction therapy with a novel antagonist of glucosylceramide synthase for fabry disease. Mol Med 2015; 21: 389-99.
[http://dx.doi.org/10.2119/molmed.2015.00088] [PMID: 25938659]
[62]
Kizhner T, Azulay Y, Hainrichson M, et al. Characterization of a chemically modified plant cell culture expressed human α-Galactosidase-A enzyme for treatment of Fabry disease. Mol Genet Metab 2015; 114(2): 259-67.
[http://dx.doi.org/10.1016/j.ymgme.2014.08.002] [PMID: 25155442]
[63]
Shen J-S, Busch A, Day TS, et al. Mannose receptor-mediated delivery of moss-made α-galactosidase A efficiently corrects enzyme deficiency in Fabry mice. J Inherit Metab Dis 2016; 39(2): 293-303.
[http://dx.doi.org/10.1007/s10545-015-9886-9] [PMID: 26310963]
[64]
Schiffmann R, Goker-Alpan O, Holida M, et al. Pegunigalsidase alfa, a novel PEGylated enzyme replacement therapy for Fabry disease, provides sustained plasma concentrations and favorable pharmacodynamics: A 1-year Phase 1/2 clinical trial. J Inherit Metab Dis 2019; 42(3): 534-44.
[http://dx.doi.org/10.1002/jimd.12080] [PMID: 30834538]
[65]
Simonetta I, Tuttolomondo A, Di Chiara T, et al. Genetics and gene therapy of Anderson-Fabry disease. Curr Gene Ther 2018; 18(2): 96-106.
[http://dx.doi.org/10.2174/1566523218666180404161315] [PMID: 29618309]
[66]
Biffi A, Montini E, Lorioli L, et al. Lentiviral hematopoietic stem cell gene therapy benefits metachromatic leukodystrophy. Science 2013; 341(6148)1233158
[http://dx.doi.org/10.1126/science.1233158] [PMID: 23845948]
[67]
Biffi A, Gentner BR, Naldini L. Gene vector 2010. Google patents WO2010125471A21 2010.
[68]
Jung SC, Han IP, Limaye A, et al. Adeno-associated viral vector-mediated gene transfer results in long-term enzymatic and functional correction in multiple organs of Fabry mice. Proc Natl Acad Sci USA 2001; 98(5): 2676-81.
[http://dx.doi.org/10.1073/pnas.051634498] [PMID: 11226298]
[69]
Rozenfeld PA. Fabry disease: treatment and diagnosis. IUBMB Life 2009; 61(11): 1043-50.
[http://dx.doi.org/10.1002/iub.257] [PMID: 19859978]
[70]
Park J, Murray GJ, Limaye A, et al. Long-term correction of globotriaosylceramide storage in Fabry mice by recombinant adeno-associated virus-mediated gene transfer. Proc Natl Acad Sci USA 2003; 100(6): 3450-4.
[http://dx.doi.org/10.1073/pnas.0537900100] [PMID: 12624185]
[71]
Takahashi H, Hirai Y, Migita M, et al. Long-term systemic therapy of Fabry disease in a knockout mouse by adeno-associated virus-mediated muscle-directed gene transfer. Proc Natl Acad Sci USA 2002; 99(21): 13777-82.
[http://dx.doi.org/10.1073/pnas.222221899] [PMID: 12370426]
[72]
Li C, Ziegler RJ, Cherry M, et al. Adenovirus-transduced lung as a portal for delivering alpha-galactosidase A into systemic circulation for Fabry disease. Mol Ther 2002; 5(6): 745-54.
[http://dx.doi.org/10.1006/mthe.2002.0605] [PMID: 12027559]
[73]
Ogawa K, Hirai Y, Ishizaki M, et al. Long-term inhibition of glycosphingolipid accumulation in Fabry model mice by a single systemic injection of AAV1 vector in the neonatal period. Mol Genet Metab 2009; 96(3): 91-6.
[http://dx.doi.org/10.1016/j.ymgme.2008.10.017] [PMID: 19091614]
[74]
Sabatino DE, Mackenzie TC, Peranteau W, et al. Persistent expression of hF.IX After tolerance induction by in utero or neonatal administration of AAV-1-F.IX in hemophilia B mice. Mol Ther 2007; 15(9): 1677-85.
[http://dx.doi.org/10.1038/sj.mt.6300219] [PMID: 17565352]
[75]
Passineau MJ, Fahrenholz T, Machen L, et al. α-Galactosidase A expressed in the salivary glands partially corrects organ biochemical deficits in the fabry mouse through endocrine trafficking. Hum Gene Ther 2011; 22(3): 293-301.
[http://dx.doi.org/10.1089/hum.2010.069] [PMID: 20858137]
[76]
Novo FJ, Górecki DC, Goldspink G, MacDermot KD. Gene transfer and expression of human alpha-galactosidase from mouse muscle in vitro and in vivo. Gene Ther 1997; 4(5): 488-92.
[http://dx.doi.org/10.1038/sj.gt.3300410] [PMID: 9274727]
[77]
Przybylska M, Wu I-H, Zhao H, et al. Partial correction of the alpha-galactosidase A deficiency and reduction of glycolipid storage in Fabry mice using synthetic vectors. J Gene Med 2004; 6(1): 85-92.
[http://dx.doi.org/10.1002/jgm.468] [PMID: 14716680]
[78]
Nakamura G, Maruyama H, Ishii S, et al. Naked plasmid DNA-based alpha-galactosidase A gene transfer partially reduces systemic accumulation of globotriaosylceramide in Fabry mice. Mol Biotechnol 2008; 38(2): 109-19.
[http://dx.doi.org/10.1007/s12033-007-9008-5] [PMID: 18219591]
[79]
Barisoni L, Jennette JC, Colvin R, et al. Novel quantitative method to evaluate globotriaosylceramide inclusions in renal peritubular capillaries by virtual microscopy in patients with fabry disease. Arch Pathol Lab Med 2012; 136(7): 816-24.
[http://dx.doi.org/10.5858/arpa.2011-0350-OA] [PMID: 22742555]
[80]
An D, Schneller JL, Frassetto A, et al. Systemic messenger RNA therapy as a treatment for methylmalonic acidemia. Cell Rep 2017; 21(12): 3548-58.
[http://dx.doi.org/10.1016/j.celrep.2017.11.081] [PMID: 29262333]
[81]
Jiang L, Berraondo P, Jericó D, et al. Systemic messenger RNA as an etiological treatment for acute intermittent porphyria. Nat Med 2018; 24(12): 1899-909.
[http://dx.doi.org/10.1038/s41591-018-0199-z] [PMID: 30297912]
[82]
Zhu X, Yin L, Theisen M, et al. Systemic mRNA therapy for the treatment of fabry disease: preclinical studies in wild-type mice, fabry mouse model, and wild-type non-human primates. Am J Hum Genet 2019; 104(4): 625-37.
[http://dx.doi.org/10.1016/j.ajhg.2019.02.003] [PMID: 30879639]
[83]
Loomis KH, Kirschman JL, Bhosle S, Bellamkonda RV, Santangelo PJ. Strategies for modulating innate immune activation and protein production of in vitro transcribed mRNAs. J Mater Chem B Mater Biol Med 2016; 4(9): 1619-32.
[http://dx.doi.org/10.1039/C5TB01753J] [PMID: 32263015]
[84]
Vaidyanathan S, Azizian KT, Haque AKMA, et al. Uridine depletion and chemical modification increase Cas9 mRNA activity and reduce immunogenicity without HPLC purification. Mol Ther Nucleic Acids 2018; 12: 530-42.
[http://dx.doi.org/10.1016/j.omtn.2018.06.010] [PMID: 30195789]
[85]
Ramaswamy S, Tonnu N, Tachikawa K, et al. Systemic delivery of factor IX messenger RNA for protein replacement therapy. Proc Natl Acad Sci USA 2017; 114(10): E1941-50.
[http://dx.doi.org/10.1073/pnas.1619653114] [PMID: 28202722]
[86]
DeRosa F, Guild B, Karve S, et al. Therapeutic efficacy in a hemophilia B model using a biosynthetic mRNA liver depot system. Gene Ther 2016; 23(10): 699-707.
[http://dx.doi.org/10.1038/gt.2016.46] [PMID: 27356951]
[87]
Akinc A, Querbes W, De S, et al. Targeted delivery of RNAi therapeutics with endogenous and exogenous ligand-based mechanisms. Mol Ther 2010; 18(7): 1357-64.
[http://dx.doi.org/10.1038/mt.2010.85] [PMID: 20461061]
[88]
Suzuki Y. Chaperone therapy update: Fabry disease, GM1-gangliosidosis and Gaucher disease. Brain Dev 2013; 35(6): 515-23.
[http://dx.doi.org/10.1016/j.braindev.2012.12.002] [PMID: 23290321]
[89]
Mignani R, Feriozzi S, Pisani A, et al. Agalsidase therapy in patients with Fabry disease on renal replacement therapy: a nationwide study in Italy. Nephrol Dial Transplant 2008; 23(5): 1628-35.
[http://dx.doi.org/10.1093/ndt/gfm813] [PMID: 18057066]
[90]
Petta S, Adinolfi LE, Fracanzani AL, et al. Hepatitis C virus eradication by direct-acting antiviral agents improves carotid atherosclerosis in patients with severe liver fibrosis. J Hepatol 2018; 69(1): 18-24.
[http://dx.doi.org/10.1016/j.jhep.2018.02.015] [PMID: 29505844]
[91]
Petta S, Valenti L, Tuttolomondo A, et al. Interferon lambda 4 rs368234815 TT>δG variant is associated with liver damage in patients with nonalcoholic fatty liver disease. Hepatology 2017; 66(6): 1885-93.
[http://dx.doi.org/10.1002/hep.29395] [PMID: 28741298]
[92]
Tuttolomondo A, Maida C, Pinto A. Diabetic foot syndrome: Immune-inflammatory features as possible cardiovascular markers in diabetes. World J Orthop 2015; 6(1): 62-76.
[http://dx.doi.org/10.5312/wjo.v6.i1.62] [PMID: 25621212]
[93]
Tuttolomondo A, Di Raimondo D, Pecoraro R, et al. KIRIIND (KIR Infectious and Inflammatory Diseases) Collaborative Group. HLA and killer cell immunoglobulin-like receptor (KIRs) genotyping in patients with acute ischemic stroke. J Neuroinflammation 2019; 16(1): 88.
[http://dx.doi.org/10.1186/s12974-019-1469-5] [PMID: 30995924]
[94]
Tuttolomondo A, Pecoraro R, Casuccio A, et al. Peripheral frequency of CD4+ CD28- cells in acute ischemic stroke: relationship with stroke subtype and severity markers. Medicine (Baltimore) 2016; 94(24): 1.
[PMID: 31265549]
[95]
Di Raimondo D, Tuttolomondo A, Buttà C, et al. Metabolic and anti-inflammatory effects of a home-based programme of aerobic physical exercise. Int J Clin Pract 2013; 67(12): 1247-53.
[http://dx.doi.org/10.1111/ijcp.12269] [PMID: 24246205]
[96]
Pinto A, Tuttolomondo A, Di Raimondo D, Fernandez P, Licata G. Risk factors profile and clinical outcome of ischemic stroke patients admitted in a Department of Internal Medicine and classified by TOAST classification. Int Angiol 2006; 25(3): 261-7.
[PMID: 16878074]

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