Болезнь Гоше: достижения и перспективы - Журнал Терапевтический архив №7 Вопросы гематологии 2021
Болезнь Гоше: достижения и перспективы
Пономарев Р.В., Лукина Е.А. Болезнь Гоше: достижения и перспективы. Терапевтический архив. 2021; 93 (7): 830–836. DOI: 10.26442/00403660.2021.07.200912
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Аннотация
Болезнь Гоше (БГ) – наиболее распространенное и хорошо изученное заболевание из группы лизосомных болезней накопления, возникающее вследствие наследственного дефицита активности лизосомного фермента кислой β-глюкозидазы (глюкоцереброзидазы), участвующего в катаболизме сфинголипидов. Без преувеличения феноменальные успехи в изучении патогенеза и разработке специфической терапии данного заболевания во 2-й половине XX – начале XXI в. кардинально изменили клинический фенотип БГ, превратив тяжелое прогрессирующее заболевание в бессимптомный метаболический дефект. Эволюция представлений о БГ, тесно связанная с фундаментальными открытиями в области клеточной биологии, биохимии и генетики, может представлять интерес не только для узкой группы специалистов, занимающихся диагностикой и лечением БГ, но и для более широкой аудитории – как модель эффективной работы научного сообщества в лечении редкой метаболической патологии.
Ключевые слова: болезнь Гоше, лизосомные болезни накопления, глюкоцереброзидаза, заместительная ферментная терапия
Keywords: Gaucher disease, lysosomal storage diseases, glucocerebrosidase, enzyme replacement therapy
Ключевые слова: болезнь Гоше, лизосомные болезни накопления, глюкоцереброзидаза, заместительная ферментная терапия
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Keywords: Gaucher disease, lysosomal storage diseases, glucocerebrosidase, enzyme replacement therapy
Список литературы
1. Gaucher PC. De L’epithelioma primitif de la rate, hypertrophie idiopathique de la rate sans leucemie. Academic Thesis, Paris.1882; Available at: https://archive.org/details/b30577792. Accessed: 03.04.21
2. Brill NE. Primary splenomegaly with a report of three cases occuring in one family. Am J Med Sci. 1901;121:377. DOI:10.1097/00000441-190104000-00001
3. Oberling CWP. La maladie de Gaucher chez le nourrisson. Rev franç de pédiat. 1927;3:475.
4. Hillborg PO. Gaucher’s disease in Norrbotten. Nord Med. 1959;61:303-6.
5. Marchand FM. Über Sogennante idiopathische Splenomegalie (Typus Gaucher). Munchen med Wchnschr. 1907;54:1102-3.
6. Leib H. Cerebrosidespeicherung bei Splenomegalie Typos Gaucher. Ztschr Physsiol Chem. 1924;140:305.
7. Aghion H. La Maladie de Gaucher Dans l'enfance (forme cardio-rénale). Dr. Thesis. Paris, 1934.
8. De Duve C, Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435-92. DOI:10.1146/annurev.ph.28.030166.002251
9. Novikoff AB, Beaufay H, De Duve C. Electron microscopy of lysosome-rich fractions from rat liver. J Cell Biol. 1956;2:179-84. DOI:10.1083/jcb.2.4.179
10. Essner E, Novikoff AB. Localization of acid phosphatase activity in hepatic lysosomes by means of electron microscopy. J Biophys Biochem Cytol. 1961;9(4):773-84. DOI:10.1083/jcb.9.4.773
11. De Duve C. Exploring cells with a centrifuge. Science. 1975;189(4198):186-94. DOI:10.1126/science.1138375
12. Ballabio A. The awesome lysosome. EMBO Mol Med. 2016;8(2):73‑6. DOI:10.15252/emmm.201505966
13. Settembre C, Fraldi A, Medina DL, et al. Signals from the lysosome. Nat Rev Mol Cell Biol. 2013;14:283-96. DOI:10.1038/nrm3565.Signals
14. Xu H, Ren D. Lysosomal physiology. Annu Rev Physiol. 2015;77:57‑80. DOI:10.1146/annurev-physiol-021014-071649
15. Andrews NW, Almeida PE, Corrotte M. Damage control: Cellular mechanisms of plasma membrane repair. Trends Cell Biol. 2014;24(12):734-42. DOI:10.1016/j.tcb.2014.07.008
16. Mostov K, Werb Z. Journey across the osteoclast. Science. 1997;276(5310):219-20. DOI:10.1126/science.276.5310.219
17. Aderem A, Underhill DM. Mechanisms of phagocytosos in macrophages. Annu Rev Immunol. 1999;17:593-623. DOI:10.1146/annurev.immunol.17.1.593
18. Do J, McKinney C, Sharma P, et al. Glucocerebrosidase and its relevance to Parkinson disease. Mol Neurodegener. 2019;14:1-16.
DOI:10.1186/s13024-019-0336-2
19. Petkau TL, Leavitt BR. Progranulin in neurodegenerative disease. Trends Neurosci. 2014;37(7):388-98. DOI:10.1016/j.tins.2014.04.003
20. Stirnemann JÔ, Belmatoug N, Camou F, et al. A review of gaucher disease pathophysiology, clinical presentation and treatments. Int J Mol Sci. 2017;18:1-30. DOI:10.3390/ijms18020441
21. Liu L, Zhang N, Dou Y, et al. Lysosomal dysfunction and autophagy blockade contribute to IMB-6G-induced apoptosis in pancreatic cancer cells. Sci Rep. 2017. DOI:10.1038/srep41862
22. Rawnsley DR, Diwan A. Lysosome impairment as a trigger for inflammation in obesity: The proof is in the fat. EBioMedicine. 2020;56:102824. DOI:10.1016/j.ebiom.2020.102824
23. Brady RO, Kanfer J, Shapiro D. The Metabolism of Glucocerebrosides. I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J Biol Chem. 1965;240:39-43.
24. Kampine JP, Brady RO, Kanfer JN, et al. Diagnosis of Gaucher’s disease and Niemann-Pick disease with small samples of venous blood. Science. 1967;155(3758):86-8. DOI:10.1126/science.155.3758.86
25. Schneider RO, Ellis WG, Brady RO, et al. Infantile (type II) Gaucher’s disease: In utero diagnosis and fetal pathology. J Pediatr. 1972;81(6):1134-9. DOI:10.1016/s0022-3476(72)80245-2
26. De Duve C. From cytases to lysosomes. Fed Proc. 1964;23:1045-9
27. Ginns EI, Choudary PV., Tsuji S, et al. Gene mapping and leader polypeptide sequence of human glucocerebrosidase: Implications for Gaucher disease. Proc Natl Acad Sci USA. 1985;82(20):7101-5. DOI:10.1073/pnas.82.20.7101
28. Tsuji S, Choudary PV., Martin BM, et al. A Mutation in the Human Glucocerebrosidase Gene in Neuronopathic Gaucher’s Disease. N Engl J Med. 1987;316(10):570-5.
DOI:10.1056/nejm198703053161002
29. Tsuji S, Martin BM, Barranger JA, et al. Genetic heterogeneity in type 1 Gaucher disease: Multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci USA. 1988;85(7):2349-52. DOI:10.1073/pnas.85.7.2349
30. Grabowski GA. Phenotype, diagnosis, and treatment of Gaucher’s disease. Lancet. 2008;372:1263-1271. DOI:10.1016/S0140-6736(08)61522-6
31. Pentchev PG, Brady RO, Hibbert SR, et al. Isolation and characterization of glucocerebrosidase from human placental tissue. J Biol Chem. 1973;248:5256-5261.DOI:10.1016/s0021-9258(19)43595-3
32. Brady RO, Pentchev PG, Gal AE, et al. Replacement Therapy for Inherited Enzyme Deficiency: Use of Purified Glucocerebrosidase in Gaucher’s Disease. N Engl J Med. 1974;291:989-93. DOI:10.1056/NEJM197411072911901
33. Furbish FS, Blair HE, Shiloach J, et al. Enzyme replacement therapy in Gaucher’s disease: large-scale purification of glucocerebrosidase suitable for human administration. Proc Natl Acad Sci USA. 1977;74(8):3560‑3563. DOI:10.1073/pnas.74.8.3560
34. Doebber TW, Wu MS, Bugianesi RL, et al. Enhanced macrophage uptake of synthetically glycosylated human placental β-glucocerebrosidase. J Biol Chem. 1982;257(5):2193-9.
35. Barton NW, Brady RO, Murray GJ, et al. Replacement therapy for inherited enzyme deficiency – macrophage-targeted glucocerebrosidase for gaucher’s disease. N Engl J Med. 1991;324(21):1464-70. DOI:10.1056/NEJM199105233242104
36. Eds. AH Futerman, A Zimran. Gaucher disease. Taylor & Francis Group, LLC, 2007.
37. Starzyk K, Richards S, Yee J, et al. The long-term international safety experience of imiglucerase therapy for Gaucher disease. Mol Genet Metab. 2007;90:157-63. DOI:10.1016/j.ymgme.2006.09.003
38. Mistry PK, Batista JL, Andersson HC, et al. Transformation in pretreatment manifestations of Gaucher disease type 1 during two decades of alglucerase/imiglucerase enzyme replacement therapy in the International Collaborative Gaucher Group (ICGG) Gaucher Registry. Am J Hematol. 2017;92(9):929-39. DOI:10.1002/ajh.24801
39. Davidson BA, Hassan S, Garcia EJ, et al. Exploring genetic modifiers of Gaucher disease: The next horizon. Hum Mutat. 2018;39:1739-51. DOI:10.1002/humu.23611
40. Ivanova M, Limgala RP, Changsila E, et al. Gaucheromas: When macrophages promote tumor formation and dissemination. Blood Cells, Mol Dis. 2018;68:100-5. DOI:10.1016/j.bcmd.2016.10.018
41. Mistry PK, Sirrs S, Chan A, et al. Pulmonary hypertension in type 1 Gaucher’s disease: Genetic and epigenetic determinants of phenotype and response to therapy. Mol Genet Metab. 2002;77(1-2):91-8. DOI:10.1016/S1096-7192(02)00122-1
42. Boot RG, Verhoek M, de Fost M, et al. Marked elevation of the chemokine CCL18/PARC in Gaucher disease: A novel surrogate marker for assessing therapeutic intervention. Blood. 2004;103(1):33-9. DOI:10.1182/blood-2003-05-1612
43. Kanneganti M, Kamba A, Mizoguchi E. Role of chitotriosidase (Chitinase 1) under normal and disease conditions. J Epithel Biol Pharmacol. 2012;5:1-9. DOI:10.2174/1875044301205010001
44. Raskovalova T, Deegan PB, Yang R, et al. Plasma chitotriosidase activity versus CCL18 level for assessing type I Gaucher disease severity: Protocol for a systematic review with meta-analysis of individual participant data. Syst Rev. 2017;6:1-10.
DOI:10.1186/s13643-017-0483-x
45. Elmonem MA, van den Heuvel LP, Levtchenko EN. Immunomodulatory Effects of Chitotriosidase Enzyme. Enzyme Res. 2016;2016:2682680. DOI:10.1155/2016/2682680
46. Hurvitz N, Dinur T, Cohen MB, et al. Glucosylsphingosine (Lyso-gb1) as a biomarker for monitoring treated and untreated children with gaucher disease. Int J Mol Sci. 2019;20:1-9. DOI:10.3390/ijms20123033
47. Murugesan V, Chuang WL, Liu J, et al. Glucosylsphingosine is a key biomarker of Gaucher disease. Am J Hematol. 2016;91:1082-9. DOI:10.1002/ajh.24491
48. Пономарев Р.В., Лукина Е.А., Сысоева Е.П. Поддерживающий режим заместительной ферментной терапии у взрослых больных болезнью Гоше I типа: предварительные результаты. Гематология и трансфузиология. 2019;64(3):331-41 [Ponomarev RV, Lukina KA, Sysoeva EP, et al. Reduced dosing regimen of enzyme replacement therapy in adults patients with type I Gaucher disease: preliminary results. Russ J Hematol Transfusiology. 2019;64(3):331‑41 (in Russian)].
DOI:10.35754/0234-5730-2019-64-3-331-341
49. Fink JK, Correll PH, Perry LK, et al. Correction of glucocerebrosidase deficiency after retroviral-mediated gene transfer into hematopoietic progenitor cells from patients with Gaucher disease. Proc Natl Acad Sci USA. 1990;87(6):2334-8.
DOI:10.1073/pnas.87.6.2334
50. Enquist IB, Nilsson E, Ooka A, et al. Effective cell and gene therapy in a murine model of Gaucher disease. Proc Natl Acad USA. 2006;103(37):13819-24. DOI:10.1073/pnas.0606016103
51. Du S, Ou H, Cui R, et al. Delivery of Glucosylceramidase Beta Gene Using AAV9 Vector Therapy as a Treatment Strategy in Mouse Models of Gaucher Disease. Hum Gene Ther. 2019;30:155-67. DOI:10.1089/hum.2018.072
2. Brill NE. Primary splenomegaly with a report of three cases occuring in one family. Am J Med Sci. 1901;121:377. DOI:10.1097/00000441-190104000-00001
3. Oberling CWP. La maladie de Gaucher chez le nourrisson. Rev franç de pédiat. 1927;3:475.
4. Hillborg PO. Gaucher’s disease in Norrbotten. Nord Med. 1959;61:303-6.
5. Marchand FM. Über Sogennante idiopathische Splenomegalie (Typus Gaucher). Munchen med Wchnschr. 1907;54:1102-3.
6. Leib H. Cerebrosidespeicherung bei Splenomegalie Typos Gaucher. Ztschr Physsiol Chem. 1924;140:305.
7. Aghion H. La Maladie de Gaucher Dans l'enfance (forme cardio-rénale). Dr. Thesis. Paris, 1934.
8. De Duve C, Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435-92. DOI:10.1146/annurev.ph.28.030166.002251
9. Novikoff AB, Beaufay H, De Duve C. Electron microscopy of lysosome-rich fractions from rat liver. J Cell Biol. 1956;2:179-84. DOI:10.1083/jcb.2.4.179
10. Essner E, Novikoff AB. Localization of acid phosphatase activity in hepatic lysosomes by means of electron microscopy. J Biophys Biochem Cytol. 1961;9(4):773-84. DOI:10.1083/jcb.9.4.773
11. De Duve C. Exploring cells with a centrifuge. Science. 1975;189(4198):186-94. DOI:10.1126/science.1138375
12. Ballabio A. The awesome lysosome. EMBO Mol Med. 2016;8(2):73‑6. DOI:10.15252/emmm.201505966
13. Settembre C, Fraldi A, Medina DL, et al. Signals from the lysosome. Nat Rev Mol Cell Biol. 2013;14:283-96. DOI:10.1038/nrm3565.Signals
14. Xu H, Ren D. Lysosomal physiology. Annu Rev Physiol. 2015;77:57‑80. DOI:10.1146/annurev-physiol-021014-071649
15. Andrews NW, Almeida PE, Corrotte M. Damage control: Cellular mechanisms of plasma membrane repair. Trends Cell Biol. 2014;24(12):734-42. DOI:10.1016/j.tcb.2014.07.008
16. Mostov K, Werb Z. Journey across the osteoclast. Science. 1997;276(5310):219-20. DOI:10.1126/science.276.5310.219
17. Aderem A, Underhill DM. Mechanisms of phagocytosos in macrophages. Annu Rev Immunol. 1999;17:593-623. DOI:10.1146/annurev.immunol.17.1.593
18. Do J, McKinney C, Sharma P, et al. Glucocerebrosidase and its relevance to Parkinson disease. Mol Neurodegener. 2019;14:1-16.
DOI:10.1186/s13024-019-0336-2
19. Petkau TL, Leavitt BR. Progranulin in neurodegenerative disease. Trends Neurosci. 2014;37(7):388-98. DOI:10.1016/j.tins.2014.04.003
20. Stirnemann JÔ, Belmatoug N, Camou F, et al. A review of gaucher disease pathophysiology, clinical presentation and treatments. Int J Mol Sci. 2017;18:1-30. DOI:10.3390/ijms18020441
21. Liu L, Zhang N, Dou Y, et al. Lysosomal dysfunction and autophagy blockade contribute to IMB-6G-induced apoptosis in pancreatic cancer cells. Sci Rep. 2017. DOI:10.1038/srep41862
22. Rawnsley DR, Diwan A. Lysosome impairment as a trigger for inflammation in obesity: The proof is in the fat. EBioMedicine. 2020;56:102824. DOI:10.1016/j.ebiom.2020.102824
23. Brady RO, Kanfer J, Shapiro D. The Metabolism of Glucocerebrosides. I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J Biol Chem. 1965;240:39-43.
24. Kampine JP, Brady RO, Kanfer JN, et al. Diagnosis of Gaucher’s disease and Niemann-Pick disease with small samples of venous blood. Science. 1967;155(3758):86-8. DOI:10.1126/science.155.3758.86
25. Schneider RO, Ellis WG, Brady RO, et al. Infantile (type II) Gaucher’s disease: In utero diagnosis and fetal pathology. J Pediatr. 1972;81(6):1134-9. DOI:10.1016/s0022-3476(72)80245-2
26. De Duve C. From cytases to lysosomes. Fed Proc. 1964;23:1045-9
27. Ginns EI, Choudary PV., Tsuji S, et al. Gene mapping and leader polypeptide sequence of human glucocerebrosidase: Implications for Gaucher disease. Proc Natl Acad Sci USA. 1985;82(20):7101-5. DOI:10.1073/pnas.82.20.7101
28. Tsuji S, Choudary PV., Martin BM, et al. A Mutation in the Human Glucocerebrosidase Gene in Neuronopathic Gaucher’s Disease. N Engl J Med. 1987;316(10):570-5.
DOI:10.1056/nejm198703053161002
29. Tsuji S, Martin BM, Barranger JA, et al. Genetic heterogeneity in type 1 Gaucher disease: Multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci USA. 1988;85(7):2349-52. DOI:10.1073/pnas.85.7.2349
30. Grabowski GA. Phenotype, diagnosis, and treatment of Gaucher’s disease. Lancet. 2008;372:1263-1271. DOI:10.1016/S0140-6736(08)61522-6
31. Pentchev PG, Brady RO, Hibbert SR, et al. Isolation and characterization of glucocerebrosidase from human placental tissue. J Biol Chem. 1973;248:5256-5261.DOI:10.1016/s0021-9258(19)43595-3
32. Brady RO, Pentchev PG, Gal AE, et al. Replacement Therapy for Inherited Enzyme Deficiency: Use of Purified Glucocerebrosidase in Gaucher’s Disease. N Engl J Med. 1974;291:989-93. DOI:10.1056/NEJM197411072911901
33. Furbish FS, Blair HE, Shiloach J, et al. Enzyme replacement therapy in Gaucher’s disease: large-scale purification of glucocerebrosidase suitable for human administration. Proc Natl Acad Sci USA. 1977;74(8):3560‑3563. DOI:10.1073/pnas.74.8.3560
34. Doebber TW, Wu MS, Bugianesi RL, et al. Enhanced macrophage uptake of synthetically glycosylated human placental β-glucocerebrosidase. J Biol Chem. 1982;257(5):2193-9.
35. Barton NW, Brady RO, Murray GJ, et al. Replacement therapy for inherited enzyme deficiency – macrophage-targeted glucocerebrosidase for gaucher’s disease. N Engl J Med. 1991;324(21):1464-70. DOI:10.1056/NEJM199105233242104
36. Eds. AH Futerman, A Zimran. Gaucher disease. Taylor & Francis Group, LLC, 2007.
37. Starzyk K, Richards S, Yee J, et al. The long-term international safety experience of imiglucerase therapy for Gaucher disease. Mol Genet Metab. 2007;90:157-63. DOI:10.1016/j.ymgme.2006.09.003
38. Mistry PK, Batista JL, Andersson HC, et al. Transformation in pretreatment manifestations of Gaucher disease type 1 during two decades of alglucerase/imiglucerase enzyme replacement therapy in the International Collaborative Gaucher Group (ICGG) Gaucher Registry. Am J Hematol. 2017;92(9):929-39. DOI:10.1002/ajh.24801
39. Davidson BA, Hassan S, Garcia EJ, et al. Exploring genetic modifiers of Gaucher disease: The next horizon. Hum Mutat. 2018;39:1739-51. DOI:10.1002/humu.23611
40. Ivanova M, Limgala RP, Changsila E, et al. Gaucheromas: When macrophages promote tumor formation and dissemination. Blood Cells, Mol Dis. 2018;68:100-5. DOI:10.1016/j.bcmd.2016.10.018
41. Mistry PK, Sirrs S, Chan A, et al. Pulmonary hypertension in type 1 Gaucher’s disease: Genetic and epigenetic determinants of phenotype and response to therapy. Mol Genet Metab. 2002;77(1-2):91-8. DOI:10.1016/S1096-7192(02)00122-1
42. Boot RG, Verhoek M, de Fost M, et al. Marked elevation of the chemokine CCL18/PARC in Gaucher disease: A novel surrogate marker for assessing therapeutic intervention. Blood. 2004;103(1):33-9. DOI:10.1182/blood-2003-05-1612
43. Kanneganti M, Kamba A, Mizoguchi E. Role of chitotriosidase (Chitinase 1) under normal and disease conditions. J Epithel Biol Pharmacol. 2012;5:1-9. DOI:10.2174/1875044301205010001
44. Raskovalova T, Deegan PB, Yang R, et al. Plasma chitotriosidase activity versus CCL18 level for assessing type I Gaucher disease severity: Protocol for a systematic review with meta-analysis of individual participant data. Syst Rev. 2017;6:1-10.
DOI:10.1186/s13643-017-0483-x
45. Elmonem MA, van den Heuvel LP, Levtchenko EN. Immunomodulatory Effects of Chitotriosidase Enzyme. Enzyme Res. 2016;2016:2682680. DOI:10.1155/2016/2682680
46. Hurvitz N, Dinur T, Cohen MB, et al. Glucosylsphingosine (Lyso-gb1) as a biomarker for monitoring treated and untreated children with gaucher disease. Int J Mol Sci. 2019;20:1-9. DOI:10.3390/ijms20123033
47. Murugesan V, Chuang WL, Liu J, et al. Glucosylsphingosine is a key biomarker of Gaucher disease. Am J Hematol. 2016;91:1082-9. DOI:10.1002/ajh.24491
48. Ponomarev RV, Lukina KA, Sysoeva EP, et al. Reduced dosing regimen of enzyme replacement therapy in adults patients with type I Gaucher disease: preliminary results. Russ J Hematol Transfusiology. 2019;64(3):331‑41 (in Russian)
DOI:10.35754/0234-5730-2019-64-3-331-341
49. Fink JK, Correll PH, Perry LK, et al. Correction of glucocerebrosidase deficiency after retroviral-mediated gene transfer into hematopoietic progenitor cells from patients with Gaucher disease. Proc Natl Acad Sci USA. 1990;87(6):2334-8.
DOI:10.1073/pnas.87.6.2334
50. Enquist IB, Nilsson E, Ooka A, et al. Effective cell and gene therapy in a murine model of Gaucher disease. Proc Natl Acad USA. 2006;103(37):13819-24. DOI:10.1073/pnas.0606016103
51. Du S, Ou H, Cui R, et al. Delivery of Glucosylceramidase Beta Gene Using AAV9 Vector Therapy as a Treatment Strategy in Mouse Models of Gaucher Disease. Hum Gene Ther. 2019;30:155-67. DOI:10.1089/hum.2018.072
2. Brill NE. Primary splenomegaly with a report of three cases occuring in one family. Am J Med Sci. 1901;121:377. DOI:10.1097/00000441-190104000-00001
3. Oberling CWP. La maladie de Gaucher chez le nourrisson. Rev franç de pédiat. 1927;3:475.
4. Hillborg PO. Gaucher’s disease in Norrbotten. Nord Med. 1959;61:303-6.
5. Marchand FM. Über Sogennante idiopathische Splenomegalie (Typus Gaucher). Munchen med Wchnschr. 1907;54:1102-3.
6. Leib H. Cerebrosidespeicherung bei Splenomegalie Typos Gaucher. Ztschr Physsiol Chem. 1924;140:305.
7. Aghion H. La Maladie de Gaucher Dans l'enfance (forme cardio-rénale). Dr. Thesis. Paris, 1934.
8. De Duve C, Wattiaux R. Functions of lysosomes. Annu Rev Physiol. 1966;28:435-92. DOI:10.1146/annurev.ph.28.030166.002251
9. Novikoff AB, Beaufay H, De Duve C. Electron microscopy of lysosome-rich fractions from rat liver. J Cell Biol. 1956;2:179-84. DOI:10.1083/jcb.2.4.179
10. Essner E, Novikoff AB. Localization of acid phosphatase activity in hepatic lysosomes by means of electron microscopy. J Biophys Biochem Cytol. 1961;9(4):773-84. DOI:10.1083/jcb.9.4.773
11. De Duve C. Exploring cells with a centrifuge. Science. 1975;189(4198):186-94. DOI:10.1126/science.1138375
12. Ballabio A. The awesome lysosome. EMBO Mol Med. 2016;8(2):73‑6. DOI:10.15252/emmm.201505966
13. Settembre C, Fraldi A, Medina DL, et al. Signals from the lysosome. Nat Rev Mol Cell Biol. 2013;14:283-96. DOI:10.1038/nrm3565.Signals
14. Xu H, Ren D. Lysosomal physiology. Annu Rev Physiol. 2015;77:57‑80. DOI:10.1146/annurev-physiol-021014-071649
15. Andrews NW, Almeida PE, Corrotte M. Damage control: Cellular mechanisms of plasma membrane repair. Trends Cell Biol. 2014;24(12):734-42. DOI:10.1016/j.tcb.2014.07.008
16. Mostov K, Werb Z. Journey across the osteoclast. Science. 1997;276(5310):219-20. DOI:10.1126/science.276.5310.219
17. Aderem A, Underhill DM. Mechanisms of phagocytosos in macrophages. Annu Rev Immunol. 1999;17:593-623. DOI:10.1146/annurev.immunol.17.1.593
18. Do J, McKinney C, Sharma P, et al. Glucocerebrosidase and its relevance to Parkinson disease. Mol Neurodegener. 2019;14:1-16.
DOI:10.1186/s13024-019-0336-2
19. Petkau TL, Leavitt BR. Progranulin in neurodegenerative disease. Trends Neurosci. 2014;37(7):388-98. DOI:10.1016/j.tins.2014.04.003
20. Stirnemann JÔ, Belmatoug N, Camou F, et al. A review of gaucher disease pathophysiology, clinical presentation and treatments. Int J Mol Sci. 2017;18:1-30. DOI:10.3390/ijms18020441
21. Liu L, Zhang N, Dou Y, et al. Lysosomal dysfunction and autophagy blockade contribute to IMB-6G-induced apoptosis in pancreatic cancer cells. Sci Rep. 2017. DOI:10.1038/srep41862
22. Rawnsley DR, Diwan A. Lysosome impairment as a trigger for inflammation in obesity: The proof is in the fat. EBioMedicine. 2020;56:102824. DOI:10.1016/j.ebiom.2020.102824
23. Brady RO, Kanfer J, Shapiro D. The Metabolism of Glucocerebrosides. I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J Biol Chem. 1965;240:39-43.
24. Kampine JP, Brady RO, Kanfer JN, et al. Diagnosis of Gaucher’s disease and Niemann-Pick disease with small samples of venous blood. Science. 1967;155(3758):86-8. DOI:10.1126/science.155.3758.86
25. Schneider RO, Ellis WG, Brady RO, et al. Infantile (type II) Gaucher’s disease: In utero diagnosis and fetal pathology. J Pediatr. 1972;81(6):1134-9. DOI:10.1016/s0022-3476(72)80245-2
26. De Duve C. From cytases to lysosomes. Fed Proc. 1964;23:1045-9
27. Ginns EI, Choudary PV., Tsuji S, et al. Gene mapping and leader polypeptide sequence of human glucocerebrosidase: Implications for Gaucher disease. Proc Natl Acad Sci USA. 1985;82(20):7101-5. DOI:10.1073/pnas.82.20.7101
28. Tsuji S, Choudary PV., Martin BM, et al. A Mutation in the Human Glucocerebrosidase Gene in Neuronopathic Gaucher’s Disease. N Engl J Med. 1987;316(10):570-5.
DOI:10.1056/nejm198703053161002
29. Tsuji S, Martin BM, Barranger JA, et al. Genetic heterogeneity in type 1 Gaucher disease: Multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci USA. 1988;85(7):2349-52. DOI:10.1073/pnas.85.7.2349
30. Grabowski GA. Phenotype, diagnosis, and treatment of Gaucher’s disease. Lancet. 2008;372:1263-1271. DOI:10.1016/S0140-6736(08)61522-6
31. Pentchev PG, Brady RO, Hibbert SR, et al. Isolation and characterization of glucocerebrosidase from human placental tissue. J Biol Chem. 1973;248:5256-5261.DOI:10.1016/s0021-9258(19)43595-3
32. Brady RO, Pentchev PG, Gal AE, et al. Replacement Therapy for Inherited Enzyme Deficiency: Use of Purified Glucocerebrosidase in Gaucher’s Disease. N Engl J Med. 1974;291:989-93. DOI:10.1056/NEJM197411072911901
33. Furbish FS, Blair HE, Shiloach J, et al. Enzyme replacement therapy in Gaucher’s disease: large-scale purification of glucocerebrosidase suitable for human administration. Proc Natl Acad Sci USA. 1977;74(8):3560‑3563. DOI:10.1073/pnas.74.8.3560
34. Doebber TW, Wu MS, Bugianesi RL, et al. Enhanced macrophage uptake of synthetically glycosylated human placental β-glucocerebrosidase. J Biol Chem. 1982;257(5):2193-9.
35. Barton NW, Brady RO, Murray GJ, et al. Replacement therapy for inherited enzyme deficiency – macrophage-targeted glucocerebrosidase for gaucher’s disease. N Engl J Med. 1991;324(21):1464-70. DOI:10.1056/NEJM199105233242104
36. Eds. AH Futerman, A Zimran. Gaucher disease. Taylor & Francis Group, LLC, 2007.
37. Starzyk K, Richards S, Yee J, et al. The long-term international safety experience of imiglucerase therapy for Gaucher disease. Mol Genet Metab. 2007;90:157-63. DOI:10.1016/j.ymgme.2006.09.003
38. Mistry PK, Batista JL, Andersson HC, et al. Transformation in pretreatment manifestations of Gaucher disease type 1 during two decades of alglucerase/imiglucerase enzyme replacement therapy in the International Collaborative Gaucher Group (ICGG) Gaucher Registry. Am J Hematol. 2017;92(9):929-39. DOI:10.1002/ajh.24801
39. Davidson BA, Hassan S, Garcia EJ, et al. Exploring genetic modifiers of Gaucher disease: The next horizon. Hum Mutat. 2018;39:1739-51. DOI:10.1002/humu.23611
40. Ivanova M, Limgala RP, Changsila E, et al. Gaucheromas: When macrophages promote tumor formation and dissemination. Blood Cells, Mol Dis. 2018;68:100-5. DOI:10.1016/j.bcmd.2016.10.018
41. Mistry PK, Sirrs S, Chan A, et al. Pulmonary hypertension in type 1 Gaucher’s disease: Genetic and epigenetic determinants of phenotype and response to therapy. Mol Genet Metab. 2002;77(1-2):91-8. DOI:10.1016/S1096-7192(02)00122-1
42. Boot RG, Verhoek M, de Fost M, et al. Marked elevation of the chemokine CCL18/PARC in Gaucher disease: A novel surrogate marker for assessing therapeutic intervention. Blood. 2004;103(1):33-9. DOI:10.1182/blood-2003-05-1612
43. Kanneganti M, Kamba A, Mizoguchi E. Role of chitotriosidase (Chitinase 1) under normal and disease conditions. J Epithel Biol Pharmacol. 2012;5:1-9. DOI:10.2174/1875044301205010001
44. Raskovalova T, Deegan PB, Yang R, et al. Plasma chitotriosidase activity versus CCL18 level for assessing type I Gaucher disease severity: Protocol for a systematic review with meta-analysis of individual participant data. Syst Rev. 2017;6:1-10.
DOI:10.1186/s13643-017-0483-x
45. Elmonem MA, van den Heuvel LP, Levtchenko EN. Immunomodulatory Effects of Chitotriosidase Enzyme. Enzyme Res. 2016;2016:2682680. DOI:10.1155/2016/2682680
46. Hurvitz N, Dinur T, Cohen MB, et al. Glucosylsphingosine (Lyso-gb1) as a biomarker for monitoring treated and untreated children with gaucher disease. Int J Mol Sci. 2019;20:1-9. DOI:10.3390/ijms20123033
47. Murugesan V, Chuang WL, Liu J, et al. Glucosylsphingosine is a key biomarker of Gaucher disease. Am J Hematol. 2016;91:1082-9. DOI:10.1002/ajh.24491
48. Пономарев Р.В., Лукина Е.А., Сысоева Е.П. Поддерживающий режим заместительной ферментной терапии у взрослых больных болезнью Гоше I типа: предварительные результаты. Гематология и трансфузиология. 2019;64(3):331-41 [Ponomarev RV, Lukina KA, Sysoeva EP, et al. Reduced dosing regimen of enzyme replacement therapy in adults patients with type I Gaucher disease: preliminary results. Russ J Hematol Transfusiology. 2019;64(3):331‑41 (in Russian)].
DOI:10.35754/0234-5730-2019-64-3-331-341
49. Fink JK, Correll PH, Perry LK, et al. Correction of glucocerebrosidase deficiency after retroviral-mediated gene transfer into hematopoietic progenitor cells from patients with Gaucher disease. Proc Natl Acad Sci USA. 1990;87(6):2334-8.
DOI:10.1073/pnas.87.6.2334
50. Enquist IB, Nilsson E, Ooka A, et al. Effective cell and gene therapy in a murine model of Gaucher disease. Proc Natl Acad USA. 2006;103(37):13819-24. DOI:10.1073/pnas.0606016103
51. Du S, Ou H, Cui R, et al. Delivery of Glucosylceramidase Beta Gene Using AAV9 Vector Therapy as a Treatment Strategy in Mouse Models of Gaucher Disease. Hum Gene Ther. 2019;30:155-67. DOI:10.1089/hum.2018.072
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19. Petkau TL, Leavitt BR. Progranulin in neurodegenerative disease. Trends Neurosci. 2014;37(7):388-98. DOI:10.1016/j.tins.2014.04.003
20. Stirnemann JÔ, Belmatoug N, Camou F, et al. A review of gaucher disease pathophysiology, clinical presentation and treatments. Int J Mol Sci. 2017;18:1-30. DOI:10.3390/ijms18020441
21. Liu L, Zhang N, Dou Y, et al. Lysosomal dysfunction and autophagy blockade contribute to IMB-6G-induced apoptosis in pancreatic cancer cells. Sci Rep. 2017. DOI:10.1038/srep41862
22. Rawnsley DR, Diwan A. Lysosome impairment as a trigger for inflammation in obesity: The proof is in the fat. EBioMedicine. 2020;56:102824. DOI:10.1016/j.ebiom.2020.102824
23. Brady RO, Kanfer J, Shapiro D. The Metabolism of Glucocerebrosides. I. Purification and properties of a glucocerebroside-cleaving enzyme from spleen tissue. J Biol Chem. 1965;240:39-43.
24. Kampine JP, Brady RO, Kanfer JN, et al. Diagnosis of Gaucher’s disease and Niemann-Pick disease with small samples of venous blood. Science. 1967;155(3758):86-8. DOI:10.1126/science.155.3758.86
25. Schneider RO, Ellis WG, Brady RO, et al. Infantile (type II) Gaucher’s disease: In utero diagnosis and fetal pathology. J Pediatr. 1972;81(6):1134-9. DOI:10.1016/s0022-3476(72)80245-2
26. De Duve C. From cytases to lysosomes. Fed Proc. 1964;23:1045-9
27. Ginns EI, Choudary PV., Tsuji S, et al. Gene mapping and leader polypeptide sequence of human glucocerebrosidase: Implications for Gaucher disease. Proc Natl Acad Sci USA. 1985;82(20):7101-5. DOI:10.1073/pnas.82.20.7101
28. Tsuji S, Choudary PV., Martin BM, et al. A Mutation in the Human Glucocerebrosidase Gene in Neuronopathic Gaucher’s Disease. N Engl J Med. 1987;316(10):570-5.
DOI:10.1056/nejm198703053161002
29. Tsuji S, Martin BM, Barranger JA, et al. Genetic heterogeneity in type 1 Gaucher disease: Multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci USA. 1988;85(7):2349-52. DOI:10.1073/pnas.85.7.2349
30. Grabowski GA. Phenotype, diagnosis, and treatment of Gaucher’s disease. Lancet. 2008;372:1263-1271. DOI:10.1016/S0140-6736(08)61522-6
31. Pentchev PG, Brady RO, Hibbert SR, et al. Isolation and characterization of glucocerebrosidase from human placental tissue. J Biol Chem. 1973;248:5256-5261.DOI:10.1016/s0021-9258(19)43595-3
32. Brady RO, Pentchev PG, Gal AE, et al. Replacement Therapy for Inherited Enzyme Deficiency: Use of Purified Glucocerebrosidase in Gaucher’s Disease. N Engl J Med. 1974;291:989-93. DOI:10.1056/NEJM197411072911901
33. Furbish FS, Blair HE, Shiloach J, et al. Enzyme replacement therapy in Gaucher’s disease: large-scale purification of glucocerebrosidase suitable for human administration. Proc Natl Acad Sci USA. 1977;74(8):3560‑3563. DOI:10.1073/pnas.74.8.3560
34. Doebber TW, Wu MS, Bugianesi RL, et al. Enhanced macrophage uptake of synthetically glycosylated human placental β-glucocerebrosidase. J Biol Chem. 1982;257(5):2193-9.
35. Barton NW, Brady RO, Murray GJ, et al. Replacement therapy for inherited enzyme deficiency – macrophage-targeted glucocerebrosidase for gaucher’s disease. N Engl J Med. 1991;324(21):1464-70. DOI:10.1056/NEJM199105233242104
36. Eds. AH Futerman, A Zimran. Gaucher disease. Taylor & Francis Group, LLC, 2007.
37. Starzyk K, Richards S, Yee J, et al. The long-term international safety experience of imiglucerase therapy for Gaucher disease. Mol Genet Metab. 2007;90:157-63. DOI:10.1016/j.ymgme.2006.09.003
38. Mistry PK, Batista JL, Andersson HC, et al. Transformation in pretreatment manifestations of Gaucher disease type 1 during two decades of alglucerase/imiglucerase enzyme replacement therapy in the International Collaborative Gaucher Group (ICGG) Gaucher Registry. Am J Hematol. 2017;92(9):929-39. DOI:10.1002/ajh.24801
39. Davidson BA, Hassan S, Garcia EJ, et al. Exploring genetic modifiers of Gaucher disease: The next horizon. Hum Mutat. 2018;39:1739-51. DOI:10.1002/humu.23611
40. Ivanova M, Limgala RP, Changsila E, et al. Gaucheromas: When macrophages promote tumor formation and dissemination. Blood Cells, Mol Dis. 2018;68:100-5. DOI:10.1016/j.bcmd.2016.10.018
41. Mistry PK, Sirrs S, Chan A, et al. Pulmonary hypertension in type 1 Gaucher’s disease: Genetic and epigenetic determinants of phenotype and response to therapy. Mol Genet Metab. 2002;77(1-2):91-8. DOI:10.1016/S1096-7192(02)00122-1
42. Boot RG, Verhoek M, de Fost M, et al. Marked elevation of the chemokine CCL18/PARC in Gaucher disease: A novel surrogate marker for assessing therapeutic intervention. Blood. 2004;103(1):33-9. DOI:10.1182/blood-2003-05-1612
43. Kanneganti M, Kamba A, Mizoguchi E. Role of chitotriosidase (Chitinase 1) under normal and disease conditions. J Epithel Biol Pharmacol. 2012;5:1-9. DOI:10.2174/1875044301205010001
44. Raskovalova T, Deegan PB, Yang R, et al. Plasma chitotriosidase activity versus CCL18 level for assessing type I Gaucher disease severity: Protocol for a systematic review with meta-analysis of individual participant data. Syst Rev. 2017;6:1-10.
DOI:10.1186/s13643-017-0483-x
45. Elmonem MA, van den Heuvel LP, Levtchenko EN. Immunomodulatory Effects of Chitotriosidase Enzyme. Enzyme Res. 2016;2016:2682680. DOI:10.1155/2016/2682680
46. Hurvitz N, Dinur T, Cohen MB, et al. Glucosylsphingosine (Lyso-gb1) as a biomarker for monitoring treated and untreated children with gaucher disease. Int J Mol Sci. 2019;20:1-9. DOI:10.3390/ijms20123033
47. Murugesan V, Chuang WL, Liu J, et al. Glucosylsphingosine is a key biomarker of Gaucher disease. Am J Hematol. 2016;91:1082-9. DOI:10.1002/ajh.24491
48. Ponomarev RV, Lukina KA, Sysoeva EP, et al. Reduced dosing regimen of enzyme replacement therapy in adults patients with type I Gaucher disease: preliminary results. Russ J Hematol Transfusiology. 2019;64(3):331‑41 (in Russian)
DOI:10.35754/0234-5730-2019-64-3-331-341
49. Fink JK, Correll PH, Perry LK, et al. Correction of glucocerebrosidase deficiency after retroviral-mediated gene transfer into hematopoietic progenitor cells from patients with Gaucher disease. Proc Natl Acad Sci USA. 1990;87(6):2334-8.
DOI:10.1073/pnas.87.6.2334
50. Enquist IB, Nilsson E, Ooka A, et al. Effective cell and gene therapy in a murine model of Gaucher disease. Proc Natl Acad USA. 2006;103(37):13819-24. DOI:10.1073/pnas.0606016103
51. Du S, Ou H, Cui R, et al. Delivery of Glucosylceramidase Beta Gene Using AAV9 Vector Therapy as a Treatment Strategy in Mouse Models of Gaucher Disease. Hum Gene Ther. 2019;30:155-67. DOI:10.1089/hum.2018.072
Авторы
Р.В. Пономарев*, Е.А. Лукина
ФГБУ «Национальный медицинский исследовательский центр гематологии» Минздрава России, Москва, Россия
*ponomarev.r.v@icloud.com
National Research Center for Hematology, Moscow, Russia
*ponomarev.r.v@icloud.com
ФГБУ «Национальный медицинский исследовательский центр гематологии» Минздрава России, Москва, Россия
*ponomarev.r.v@icloud.com
________________________________________________
National Research Center for Hematology, Moscow, Russia
*ponomarev.r.v@icloud.com
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