Lysosomal storage diseases. Glycoproteinoses — oligosaccharidoses
EDITORIAL
Abstract
The epidemiology, clinical, biochemical and molecular genetic characteristics of oligosaccharidoses are presented —
a group of rare autosomal recessive lysosomal diseases, includes sialidosis, mannosidosis, fucosidosis, aspartylglucosaminuria and α-N-acetylgalactosaminidase deficiency. All these diseases are caused by impaired catabolism of glycoproteins and excessive accumulation of various types of oligosaccharides in lysosomes. Clinically, they are characterized by progressive neuropsychiatric disorders combined with a mild gurler-like phenotype. Two genetically heterogeneous variants of alpha- and beta-mannosidosis are caused by mutations in the MAN2B1 and MANBA genes, respectively, and hereditary deficiency of two related α- and β-mannosidases. The cause of the development of fucosidosis is inactivating mutations in the FUCA1 gene, leading to deficiency of lysosomal α-L-fucosidase and accumulation of fucoglycoproteins and fucoglycolipids. The pathogenesis of aspartylglucosaminuria is associated with impaired catabolism of aspartylglucosamine and its accumulation in the lysosomes of liver, spleen, thyroid, kidney and brain cells. The cause
of α-N-acetylgalactosaminidase deficiency is mutations in the NAGA gene and the accumulation of uncleaved glycoconjugants in lysosomes. A description of existing experimental models is presented and their role in studying the pathogenesis of these severe lysosomal diseases and the development of various therapeutic approaches is discussed.
The most successful treatment for alpha-mannosidosis has been enzyme replacement therapy using a recombinant enzyme — velmanase alfa, which has already passed phase III clinical trials and is used in clinical practice. Pathogenetic treatments for the other oligosaccharidoses discussed here have not been described, although preclinical trials have shown promise for hematopoietic stem cell transplantation and gene therapy for the treatment of β-mannosidosis and aspartyl glucosaminuria, respectively.
References
Аванесян Р.И., Авдеева Т.Г., Алексеева Е.И., и др. Педиатрия: Национальное руководство. Т. 1. Москва: ГЭОТАР-Медиа, 2009.
Горбунова В.Н. Наследственные болезни обмена. Лизосомные болезни накопления // Педиатр. 2021. Т. 12, № 2. С. 73–83. doi: 10.17816/PED12273-83 EDN: LTJHVN
Горбунова В.Н., Бучинская Н.В., Вечкасова А.О. Лизосомные болезни накопления. Муколипидозы // Педиатр. 2024. Т. 15, № 5. С. 81–98. doi: 10.17816/PED15581-98
Семячкина А.Н., Николаева Е.А. Оценка эффективности лечения препаратом велманаза-альфа больных с альфа-маннозидозом // Поликлиника. Орфанные болезни. 2023. № 1. С. 52–56.
Семячкина А.Н., Николаева Е.А., Воскобоева Е.Ю., и др. Альфа-маннозидоз у детей: анализ собственных наблюдений, возможности лечения // Российский вестник перинатологии и педиатрии. 2020. Т. 65, № 4. С. 142–149. doi: 10.21508/1027-4065-2020-65-4-142-149 EDN: JCTRSK
Alkhayat A.H., Kraemer S.A., Leipprandt J.R., et al. Human beta-mannosidase c DNA characterization and first identification of a mutation associated with human beta-mannosidosis // Hum Mol Genet. 1998. Vol. 7, N 1. P. 75–83. doi: 10.1093/hmg/7.1.75
Arvio M., Mononen I. Aspartylglycosaminuria: a review // Orphanet J Rare Dis. 2016. Vol. 11, N 1. ID 162. doi: 10.1186/s13023-016-0544-6
Arvio M., Sauna-Aho O., Peippo M. Bone marrow transplantation for aspartylglucosaminuria: follow-up study of transplanted and non-transplanted patients // J Pediatr. 2001. Vol. 138, N 2. P. 288–290. doi: 10.1067/mpd.2001.110119
Arvio P., Arvio M., Kero M., et al. Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuria // J Med Genet. 1999. Vol. 36, N 5. P. 398–404.
Aula P., Rapola J., von Koskull H., Ammala P. Prenatal diagnosis and fetal pathology of aspartylglucosaminuria // Am J Med Genet. 1984. Vol. 19, N 2. P. 359–367. doi: 10.1002/ajmg.1320190218
Autio S. Aspartylglucosaminuria (AGU). В кн.: Population structure and genetic disorders / A.W. Eriksson, H.R. Forsius, H.R. Nevanlinna, et al editors. New York: Academic Press, 1980. P. 577–582.
Bach G., Kohn G., Lasch E.E., et al. A new variant of mannosidosis with increased residual enzymatic activity and mild clinical manifestation // Pediatr Res. 1978. Vol. 12. P. 1010–1015. doi: 10.1203/00006450-197810000-00012
Bakker H.D., de Sonnaville M.-L.C.S., Vreken P., et al. Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: no association with neuroaxonal dystrophy? // Eur J Hum Genet. 2001. Vol. 9. P. 91–96. doi: 10.1038/sj.ejhg.5200598
Bedilu R., Nummy K.A., Cooper A., et al. Variable clinical presentation of lysosomal beta-mannosidosis in patients with null mutations // Mol Genet Metab. 2002. Vol. 77, N 4. P. 282–290. doi: 10.1016/s1096-7192(02)00172-5
Berg T., Riise H.M.F., Hansen G.M., et al. Spectrum of mutations in alpha-mannosidosis // Am J Hum Genet. 1999. Vol. 64, N 1. P. 77–88. doi: 10.1086/302183
Berg T., Tollersrud O.K., Walkley S.U., et al. Purification of feline lysosomal alpha-mannosidase, determination of its c DNA sequence and identification of a mutation causing alpha-mannosidosis in Persian cats // Biochem J. 1997. Vol. 328, N 3. P. 863–870. doi: 10.1042/bj3280863
Blanz J., Stroobants S., Lullmann-Rauch R., et al. Reversal of peripheral and central neural storage and ataxia after recombinant enzyme replacement therapy in alpha-mannosidosis mice // Hum Mol Genet. 2008. Vol. 17, N 22. P. 3437–3445. doi: 10.1093/hmg/ddn237
Bolfa P., Wang P., Nair R., et al. Hereditary β-mannosidosis in a dog: Clinicopathological and molecular genetic characterization // Mol Genet Metab. 2019. Vol. 128, N 1–2. P. 137–143. doi: 10.1016/j.ymgme.2019.08.002
Borgwardt L., Guffon N., Amraoui Y., et al. Efficacy and safety of Velmanase alfa in the treatment of patients with alpha-mannosidosis: results from the core and extension phase analysis of a phase III multicentre, double-blind, randomised, placebo-controlled trial // J Inherit Metab Dis. 2018. Vol. 41, N 6. P. 1215–1223. doi: 10.1007/s10545-018-0185-0
Carlsen R.B., Pierce J.G. Purification and properties of an alpha-L-fucosidase from rat epididymis // J Biol Chem. 1972. Vol. 247, N 1. P. 23–32. doi: 10.1016/S0021-9258(19)45753-0
Carritt B., King J., Welsh H.M. Gene order and localization of enzyme loci on the short arm of chromosome 1 // Ann Hum Genet. 1982. Vol. 46, N 4. P. 329–335. doi: 10.1111/j.1469-1809.1982.tb01583.x
Ceccarini M.R., Codini M., Conte C., et al. Alpha-mannosidosis: therapeutic strategies// Int J Mol Sci. 2018. Vol. 19, N 5. ID 1500. doi: 10.3390/ijms19051500
Chen X., Snanoudj-Verber S., Pollard L., et al. Pre-clinical gene therapy with AAV9/AGA in aspartylglucosaminuria mice provides evidence for clinical translation // Mol Ther. 2021. Vol. 29, N 3. P. 989–1000. doi: 10.1016/j.ymthe.2020.11.012
Chitayat D., Nakagawa S., Marion R.W., et al. Aspartylglucosaminuria in a Puerto Rican family: additional features of a panethnic disorder // Am J Med Genet. 1988. Vol. 31, N 3. P. 527–532. doi: 10.1002/ajmg.1320310307
Corney G., Fisher R.A.F., Cook P.J.L., et al. Linkage between alpha-fucosidase and the Rhesus blood group // Ann Hum Genet. 1977. Vol. 40, N 4. P. 403–405.
Coucke P., Mangelschots K., Speleman F., et al. Assignment of the fucosidase pseudogene FUCA1P to chromosome region 2q31-q32 // Cytogenet Cell Genet. 1991. Vol. 57, N 2–3. P. 120–122. doi: 10.1159/000133129
Darby J.K., Willems P.G., Nakashima P., et al. Restriction analysis of the structural alpha-L-fucosidase gene and its linkage to fucosidosis // Am J Hum Genet. 1988. Vol. 43, N 5. P. 749–755.
de Groot P.G., Westerveld A., Meera Khan P., Tager J.M. Localization of a gene for human alpha-galactosidase B (= N-acetyl-alpha-D-galactosaminidase) on chromosome 22 // Hum Genet. 1978. Vol. 44. P. 305–312. doi: 10.1007/BF00394295
de Jong J., van den Berg C., Wijburg H., et al. Alpha-N-acetylgalactosaminidase deficiency with mild clinical manifestations and difficult biochemical diagnosis // J Pediatr. 1994. Vol. 125, N 3. P. 385–391. doi: 10.1016/S0022-3476(05)83281-0
Desnick R.J., Schindler D. Alpha-N-acetylgalactosaminidase deficiency: Schindler disease. В кн.: The metabolic and molecular bases of inherited disease. Vol. III. 8th ed. / C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, editors. New York: Mc Graw-Hill, 2001.
Dunder U., Valtonen P., Kelo E., Mononen I. Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice // J Inherit Metab Dis. 2010. Vol. 33, N 5. P. 611–617. doi: 10.1007/s10545-010-9158-7
Fisher K.J., Aronson N.N. Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients: amino acid substitution cys163-to-ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits // J Biol Chem. 1991. Vol. 266, N 18. P. 12105–12113. doi: 10.1016/S0021-9258(18)99071-X
Fisher K.J., Tollersrud O.K., Aronson N.N. Cloning and sequence analysis of a c DNA for human glycosylasparaginase: a single gene encodes the subunits of this lysosomal amidase // FEBS Lett. 1990. Vol. 269, N 2. P. 440–444. doi: 10.1016/0014-5793(90)81211-6
Fowler M.L., Nakai H., Byers M.G., et al. Chromosome 1 localization of the human alpha-L-fucosidase strructural gene with a homologous site on chromosome 2 // Cytogenet Cell Genet. 1986. Vol. 43, N 1–2. P. 103–108. doi: 10.1159/000132304
Geurts van Kessel A.H.M., Westerveld A., de Groot P.G., et al. Regional localization of the genes coding for human ACO2, ARSA, and NAGA on chromosome 22 // Cytogenet Cell Genet. 1980. Vol. 28, N 3. P. 169–172. doi: 10.1159/000131527
Goodspeed K., Chen X., Tchan M. Aspartylglucosaminuria. В кн.: Gene Reviews / M.P. Adam, J. Feldman, G.M. Mirzaa, et al editors. Seattle (WA): University of Washington, Seattle. P. 1993–2024.
Goodspeed K., Feng C., Laine M., Lund T.C. Aspartylglucosaminuria: Clinical presentation and potential therapies // J Child Neurol. 2021. Vol. 36, N 5. P. 403–414. doi: 10.1177/0883073820980904
Gordon B.A., Rupar C.A., Rip J.W., et al. Aspartylglucosaminuria in a Canadian family // Clin Invest Med. 1998. Vol. 21, N 3. P. 114–123.
Gowda V.K., Nagarajan B., Suryanarayana S.G., Srinivasan V.M. Familial global developmental delay secondary to β-mannosidosis // J Pediatr Neurosci. 2021. Vol. 16, N 2. P. 149–152. doi: 10.4103/jpn.JPN_65_20
Gron K., Aula P., Peltonen L. Linkage of aspartylglucosaminuria (AGU) to marker loci on the long arm of chromosome 4 // Hum Genet. 1990. Vol. 85. P. 233–236. doi: 10.1007/BF00193202
Guffon N., Tylki-Szymanska A., Borgwardt L., et al. Recognition of alpha-mannosidosis in paediatric and adult patients: presentation of a diagnostic algorithm from an international working group // Mol Genet Metab. 2019. Vol. 126, N 4. P. 470–474. doi: 10.1016/j.ymgme.2019.01.024
Hocking J.D., Jolly R.D., Batt R.D. Deficiency of alpha-mannosidase in Angus cattle: an inherited lysosomal storage disease // Biochem J. 1972. Vol. 128, N 1. P. 69–78. doi: 10.1042/bj1280069
Ikonen E., Baumann M., Gron K., et al. Aspartylglucosaminuria: c DNA encoding human aspartylglucosaminidase and the missense mutation causing the disease // EMBO J. 1991. Vol. 10. P. 51–58. doi: 10.1002/j.1460-2075.1991.tb07920.x
Ikonen E., Peltonen L. Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease // Hum Mutat. 1992. Vol. 1, N 5. P. 361–365. doi: 10.1002/humu.1380010503
Intra J., Perotti M.-E., Pavesi G., Horner D. Comparative and phylogenetic analysis of alpha-L-fucosidase genes // Gene. 2007. Vol. 392, N 1–2. P. 34–46. doi: 10.1016/j.gene.2006.11.002
Isoniemi A., Hietala M., Aula P., et al. Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene // Hum Mutat. 1995. Vol. 5, N 4. P. 318–326. doi: 10.1002/humu.1380050408
Johnson K., Dawson G. Molecular defect in processing alpha-fucosidase in fucosidosis // Biochem Biophys Res Commun. 1985. Vol. 133, N 1. P. 90–97. doi: 10.1016/0006-291X(85)91845-5
Jolly R.D., Dittmer K.E., Garrick D.J., et al. β -mannosidosis in German shepherd dogs // Vet Pathol. 2019. Vol. 56, N 5. P. 743–748. doi: 10.1177/0300985819839239
Jones M.Z., Dawson G. Caprine beta-mannosidosis: inherited deficiency of beta-D-mannosidase // J Biol Chem. 1981. Vol. 256, N 10. P. 5185–5188. doi: 10.1016/S0021-9258(19)69384-1
Kaartinen V., Mononen I., Voncken J.W., et al. A mouse model for the human lysosomal disease aspartylglycosaminuria // Nat Med. 1996. Vol. 2. P. 1375–1378. doi: 10.1038/nm1296-1375
Kaneda Y., Hayes H., Uchida T., et al. Regional assignment of five genes on human chromosome 19 // Chromosoma. 1987. Vol. 95. P. 8–12. doi: 10.1007/BF00293835
Kanzaki T., Yokota M., Mizuno N., et al. Novel lysosomal glycoaminoacid storage disease with angiokeratoma corporis diffusum // Lancet. 1989. Vol. 333, N 8643. P. 875–876. doi: 10.1016/S0140-6736(89)92867-5
Keulemans J.L.M., Reuser A.J.J., Kroos M.A., et al. Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype // J Med Genet. 1996. Vol. 33, N 6. P. 458–464. doi: 10.1136/jmg.33.6.458
Kleijer W.J., Hu P., Thoomes R., et al. Beta-mannosidase deficiency: heterogeneous manifestation in the first female patient and her brother // J Inherit Metab Dis. 1990. Vol. 13, N 6. P. 867–872. doi: 10.1007/BF01800211
Kretz K.A., Cripe D., Carson J.S., et al. Structure and sequence of the human alpha-L-fucosidase gene and pseudogene // Genomics. 1992. Vol. 12, N 2. P. 276–280. doi: 10.1016/0888-7543(92)90374-2
Leipprandt J.R., Kraemer S.A., Haithcock B.E., et al. Caprine beta-mannosidase: sequencing and characterization of the c DNA and identification of the molecular defect of caprine beta-mannosidosis // Genomics. 1996. Vol. 37, N 1. P. 51–56. doi: 10.1006/geno.1996.0519
Liao Y.-F., Lal A., Moremen K.W. Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid alpha-mannosidase // J Biol Chem. 1996. Vol. 271, N 45. P. 28348–28358. doi: 10.1074/jbc.271.45.28348
Lund A.M., Borgwardt L., Cattaneo F., et al. Comprehensive long-term efficacy and safety of recombinant human alpha-mannosidase (velmanase alfa) treatment in patients with alpha-mannosidosis // J Inherit Metab Dis. 2018. Vol. 41, N 6. P. 1225–1233. doi: 10.1007/s10545-018-0175-2
Lund T.C., Miller W.P., Eisengart J.B., et al. Biochemical and clinical response after umbilical cord blood transplant in a boy with early childhood-onset beta-mannosidosis // Mol Genet Genomic Med. 2019. Vol. 7, N 7. ID e00712. doi: 10.1002/mgg3.712
Malachowski J.A., Jones M.Z. Beta-mannosidosis: lesions of the distal peripheral nervous system // Acta Neuropath. 1983. Vol. 61. P. 95–100. doi: 10.1007/BF00697387
Mononen I., Fisher K.J., Kaartinen V., Aronson N.N. Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation // FASEB J. 1993. Vol. 7, N 13. P. 1247–1256. doi: 10.1096/fasebj.7.13.8405810
Mononen I., Heisterkamp N., Kaartinen V., et al. Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase // PNAS. 1991. Vol. 88, N 7. P. 2941–2945. doi: 10.1073/pnas.88.7.2941
Mononen I., Ylikangas P., Mononen T., Savolainen K. Neonatal detection of aspartylglycosaminuria // Lancet. 1994. Vol. 343, N 8908. P. 1297–1298. doi: 10.1016/S0140-6736(94)92187-3
Mynarek M., Tolar J., Albert M.H., et al. Allogeneic hematopoietic SCT for alpha-mannosidosis: an analysis of 17 patients // Bone Marrow Transplant. 2012. Vol. 47, N 3. P. 352–359. doi: 10.1038/bmt.2011.99
Naumchik B.M., Gupta A., Flanagan-Steet H., et al. The role of hematopoietic cell transplant in the glycoprotein diseases // Cells. 2020. Vol. 9, N 6. ID 1411. doi: 10.3390/cells9061411
Nebes V.L., Schmidt M.C. Human lysosomal alpha-mannosidase: isolation and nucleotide sequence of the full-length c DNA // Biochem Biophys Res Commun. 1994. Vol. 200, N 1. P. 239–245. doi: 10.1006/bbrc.1994.1440
Nilssen O., Berg T., Riise H.M.F., et al. Alpha-mannosidosis: functional cloning of the lysosomal alpha-mannosidase c DNA and identification of a mutation in two affected siblings // Hum Mol Genet. 1997. Vol. 6, N 5. P. 717–726. doi: 10.1093/hmg/6.5.717
Occhiodoro T., Beckmann K.R., Morris C.P., Hopwood J.J. Human alpha-L-fucosidase: complete coding sequence from c DNA clones // Biochem Biophys Res Commun. 1989. Vol. 164, N 1. P. 439–445. doi: 10.1016/0006-291X(89)91739-7
Ockerman P.A., Autio S., Norder N.E. Diagnosis of mannosidosis // Lancet. 1973. Vol. 301, N 7796. P. 207–208. doi: 10.1016/S0140-6736(73)90045-7
Oinonen C., Tikkanen R., Rouvinen J., Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase // Nat Struct Biol. 1995. Vol. 2. P. 1102–1108. doi: 10.1038/nsb1295-1102
Palo J., Mattsson K. Eleven new cases of aspartylglycosaminuria // J Ment Defic Res. 1970. Vol. 14, N 2. P. 168–173. doi: 10.1111/j.1365-2788.1970.tb01111.x
Peltola M., Kyttälä A., Heinonen O., et al. Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse // Gene Ther. 1998. Vol. 5, N 10. P. 1314–1321. doi: 10.1038/sj.gt.3300740
Phillips D., Hennermann J.B., Tylki-Szymanska A., et al. Use of the Bruininks-Oseretsky test of motor proficiency (BOT-2) to Assess efficacy of velmanase alfa as enzyme therapy for alpha-mannosidosis // Mol Genet Metab Rep. 2020. Vol. 23. ID 100586. doi: 10.1016/j.ymgmr.2020.100586
Riise H.M.F., Berg T., Nilssen O., et al. Genomic structure of the human lysosomal alpha-mannosidase gene (MANB) // Genomics. 1997. Vol. 42, N 2. P. 200–207. doi: 10.1006/geno.1997.4668
Riise Stensland H.M.F., Persichetti E., Sorriso C., et al. Identification of two novel beta-mannosidosis-associated sequence variants: biochemical analysis of beta-mannosidase (MANBA) missense mutations // Mol Genet Metab. 2008. Vol. 94, N 4. P. 476–480. doi: 10.1016/j.ymgme.2008.04.010
Rísquez-Cuadro R., Matsumoto R., Ortega-Caballero F., et al. Pharmacological chaperones for the treatment of α-mannosidosis // J Med Chem. 2019. Vol. 62, N 12. P. 5832–5843. doi: 10.1021/acs.jmedchem.9b00153
Roces D.P., Lullmann-Rauch R., Peng J., et al. Efficacy of enzyme replacement therapy in alpha-mannosidosis mice: a preclinical animal study // Hum Mol Genet. 2004. Vol. 13, N 18. P. 1979–1988. doi: 10.1093/hmg/ddh220
Saarela J., Laine M., Oinonen C., et al. Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations // Hum Mol Genet. 2001. Vol. 10, N 9. P. 983–995. doi: 10.1093/hmg/10.9.983
Safka B.D., Varga L., Uhrova Meszarosova A., et al. Variant c.2158-2A>G in MANBA is an important and frequent cause of hereditary hearing loss and beta-mannosidosis among the Czech and Slovak Roma population — evidence for a new ethnic-specific variant // Orphanet J Rare Dis. 2020. Vol. 15, N 1. ID 222. doi: 10.1186/s13023-020-01508-3
Sangiorgi S., Mochi M., Beretta M., et al. Genetic and demographic characterization of a population with high incidence of fucosidosis // Hum Hered. 1982. Vol. 32, N 2. P. 100–105. doi: 10.1159/000153267
Santoro L., Zampini L., Padella L., et al. Early biochemical effects of velmanase alfa in a 7-month-old infant with alpha-mannosidosis // JIMD Rep. 2020. Vol. 55, N 1. P. 15–21. doi: 10.1002/jmd2.12144
Sedel F., Friderici K., Nummy K., et al. Atypical Gilles de la Tourette syndrome with beta-mannosidase deficiency // Arch Neurol. 2006. Vol. 63, N 1. P. 129–131. doi: 10.1001/archneur.63.1.129
Seo H.-C., Wilems P.J., O’Brien J.S. Six additional mutations in fucosidosis: three nonsense mutations and three frameshift mutations // Hum Mol Genet. 1993. Vol. 2, N 8. P. 1205–1208. doi: 10.1093/hmg/2.8.1205
Taylor R.M., Farrow B.R.H., Stewart G.J., Healy P.J. Enzyme replacement in nervous tissue after allogeneic bone-marrow transplantation for fucosidosis in dogs // Lancet. 1986. Vol. 328, N 8510. P. 772–774. doi: 10.1016/S0140-6736(86)90299-0
Tollersrud O.K., Aronson N.N. Purification and characterization of rat liver glycosylasparaginase // Biochem J. 1989. Vol. 260, N 1. P. 101–108. doi: 10.1042/bj2600101
Tollersrud O.K., Nilssen O., Tranebjaerg L., Borud O. Aspartylglucosaminuria in Northern Norway: a molecular and genealogical study // J Med Genet. 1994. Vol. 31, N 5. P. 360–363. doi: 10.1136/jmg.31.5.360
Van Diggelen O.P., Schindler D., Willemsen R., et al. Alpha-N-acetylgalactosaminidase deficiency, a new lysosomal storage disorder // J Inherit Metab Dis. 1988. Vol. 11, N 4. P. 349–357. doi: 10.1007/BF01800424
Walkley S.U., Thrall M.A., Dobrenis K., et al. Bone marrow transplantation corrects the enzyme defect in neurons of the central nervous system in a lysosomal storage disease // PNAS. 1994. Vol. 91, N 8. P. 2970–2974. doi: 10.1073/pnas.91.8.2970
Wang A.M., Desnick R.J. Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha-galactosidase A gene provides evidence for evolution from a common ancestral gene // Genomics. 1991. Vol. 10, N 1. P. 133–142. doi: 10.1016/0888-7543(91)90493-X
Wang A.M., Kanzaki T., Desnick R.J. The molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes angiokeratoma corporis diffusum with glycopeptiduria // J Clin Invest. 1994. Vol. 94, N 2. P. 839–845. doi: 10.1172/JCI117404
Wang A.M., Schindler D., Desnick R.J. Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy // J Clin Invest. 1990. Vol. 86, N 5. P. 1752–1756. doi: 10.1172/JCI114901
Wang A.M., Stewart C.L., Desnick R.J. Schindler disease: generation of a murine model by targeted disruption of the alpha-N-acetylgalactosaminidase gene // Pediatr Res. 1994. Vol. 35. P. 115A only.
Willems P.G., Darby J.K., Di Cioccio R.A. Identification of a mutation in sructural alpha-L-fucosidase gene in fucosidosis // Am J Hum Genet. 1988. Vol. 43. P. 756–763.
Willems P.G., Gatti R., Darby J.K., et al. Fucosidosis revisited: a review of 77 patients // Am J Med Genet. 1991. Vol. 38, N 1. P. 111–131. doi: 10.1002/ajmg.1320380125.
Willems P.J., Seo H.-C., Coucke P., et al. Spectrum of mutations in fucosidosis // Eur J Hum Genet. 1999. Vol. 7. P. 60–67. doi: 10.1038/sj.ejhg.5200272.
Williamson M., Cragg H., Grant J., et al. A 5-prime splice site mutation in fucosidosis // J Med Genet. 1993. Vol. 30. P. 218–223. doi: 10.1136/jmg.30.3.218.
Yang M., Allen H., Di Cioccio R.A. A mutation generating a stop codon in the alpha-L-fucosidase gene of a fucosidosis patients // Biochem Biophys Res Commun. 1992. Vol. 189, N 2. P. 1063–1068. doi: 10.1016/0006-291X(92)92312-L.
Yoon S.Y., Hunter J.E., Chawla S., et al. Global CNS correction in a large brain model of human alpha-mannosidosis by intravascular gene therapy // Brain. 2020. Vol. 143, N 7. P. 2058–2072. doi: 10.1093/brain/awaa161.
Yoshida K., Ikeda S.-i., Yanagisawa N., et al. Two Japanese cases with aspartylglycosaminuria: clinical and morphological features // Clin Genet. 1991. Vol. 40, N 4. P. 318–325. doi: 10.1111/j.1399-0004.1991.tb03102.x.
Zhu M., Lovell K.L., Patterson J.S., et al. Beta-mannosidosis mice: a model for the human lysosomal storage disease // Hum Mol Genet. 2006. Vol. 15, N 3. P. 493–500. doi: 10.1093/hmg/ddi465.
Zlotogora J., Ben-Neriah Z., Abu-Libdeh B.Y., Zeigler M. Aspartylglucosaminuria among Palestinian Arabs // J Inherit Metab Dis. 1997. Vol. 20, N 6. P. 799–802. doi: 10.1023/A:1005371802085.
