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Journal articles on the topic 'Gangliosidosis'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Abdullahi, Sakina M., Hafsat W. Idris, Halima A. Sadiku, and El-ishaq Abubakar. "GM1-gangliosidosis in a Nigerian infant: A case report." Nigerian Journal of Paediatrics 48, no. 1 (February 4, 2021): 50–53. http://dx.doi.org/10.4314/njp.v48i1.10.

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Gangliosidoses belong to the group of genetic lipid metabolism disorders, caused by defects of lysosome enzymes, inherited as an autosomal recessive trait. Gangliosidosis GM1 is caused by the deficiency of the acid beta-galactosidase (GLB11) resulting in the storage of the substrate- GM1 ganglioside in brain and visceral organs. GM1 gangliosidosis comprises three phenotypes, depending on the age of onset: an infantile, juvenile and adult type. In the infantile type dysmorphic features, severe psychomotor retardation, hepatosplenomegaly, bone changes and a cherry red spot in the macular region are seen. The juvenile GM1 gangliosidosis has no such external distinguishing features. In the adult type behavioural problems, dementia, extrapyramidal problems are specifically prominent. The authors present symptoms, clinical course and laboratory findings of a one-year-old boy with a diagnosed GM1 gangliosidosis. He presented with skin rashes since birth, delay in achievement of developmental milestones, progressive weight loss and recurrent diarrhoea of six-months duration.

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2

Obradovic, Slobodan, Olivera Laban, Zoran Igrutinovic, Biljana Vuletic, Ana Vujic, and Jasmina Djindjic. "GM1 gangliosidosis: Case report." Medical review 63, no. 5-6 (2010): 427–30. http://dx.doi.org/10.2298/mpns1006427o.

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Introduction. Gangliosidoses occur due to inhereted deficiency of human ? - galaktosidase,resulting in the accumulation of glicophyngolipides within the lisosomes. Clinical manifestations of lysosomal storage disorders are remarkably heterogeneous, they can appear at any age and each of them can vary from mild to severe conditions. Case report. We present a patient with an early, infintile type of GM1 gangliosidosis. The facial features were coarse: hypertelorismus, wide nose, depressed nasal bridge with lingual protrusion. From the very first months of life she had severe generalized hypotonic, delayed development and hapatosplenomegaly. Before she died, when she was 13 months old, she had not had any spontaneus movements, she was deaf and blind, dispnoic, with apnoiccrises, with amimic face, but without seizures and decerebrate rigidity, which often accompanies the terminal stage of this illness. Conclusion. The absence of ?-galaktosidase enzyme activaty at the skin fibroblasts confirmed the definitive diagnosis. There has been no successful treatment so far, but increasingly better results of the gene therapy for other lysosomal storage disorders can make us optimistic.

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3

Millichap, J. Gordon. "Infantile Gangliosidosis." Pediatric Neurology Briefs 2, no. 8 (August 1, 1988): 59. http://dx.doi.org/10.15844/pedneurbriefs-2-8-4.

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4

Praamstra, P., R. A. Wevers, F. J. M. Gabreëls, J. J. Rotteveel, W. O. Renier, R. C. A. Sengers, and K. J. B. Lamers. "GM2-gangliosidosis." Clinical Neurology and Neurosurgery 92, no. 2 (January 1990): 143–48. http://dx.doi.org/10.1016/0303-8467(90)90090-r.

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5

Draïss, Ghizlane, Adil Fouad, Nourddine Rada, Ouafa Hocar, Naima Fdil, and Mohamed Bouskraoui. "Infantile GM1-Gangliosidosis Revealed by Slate-Grey Mongolian Spots." Open Pediatric Medicine Journal 9, no. 1 (January 31, 2019): 1–4. http://dx.doi.org/10.2174/1874309901909010001.

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Introduction: GM1-gangliosidosis is an inherited metabolic disease caused by mutations in the GLB1 gene resulting in deficiency of β-galactosidase. Three forms have been identified: Infantile, juvenile, and adult. The infantile type progresses rapidly and aggressively and a delayed diagnosis hampers the prevention of many neurological deficits. This delay in diagnosis may be due to the variability of clinical expression of the disorder. Hypothesis: Extensive Mongolian or slate-grey spots deserve special attention as possible indications of associated inborn errors of metabolism, especially GM1-gangliosidosis and mucopolysaccharidosis. Only symptomatic treatments are available for GM1-gangliosidosis; research is underway. Observation: In this article, we report a case of infantile GM1-gangliosidosis revealed by slate-grey Mongolian spots, a rare condition in Morocco, and a review of the literature. Conclusion: The finding of persistent and extensive slate-grey mongolian spots in infant could lead to early detection of GM1-gangliosidosis before irreversible organ damage occurs.

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6

Gascon, Generoso G., Pinar T. Ozand, and Robert E. Erwin. "G M1 Gangliosidosis Type 2 in Two Siblings." Journal of Child Neurology 7, no. 1_suppl (April 1992): S41—S50. http://dx.doi.org/10.1177/08830738920070010711.

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A sister and brother, now aged 7 and 9 years, presented with developmental arrest, gait disturbance, dementia, and a progressive myoclonic epilepsy syndrome with hyperacusis in the second year of life. Then, spastic quadriparesis led to a decerebrate state. In the absence of macular or retinal degeneration, organomegaly, and somatic-facial features suggesting mucopolysaccharidosis, the presence of hyperacusis together with sea-blue histiocytes in bone marrow biopsies and deficient β-galactosidase activity but normal glucosidase, hexosaminidase, and neuraminidase activity on lysosomal enzyme assays constitutes the clinical-pathologic-biochemical profile of GM1 gangliosidosis type 2. This is a rare, late infantile onset, progressive gray-matter disease in which β-galactosidase deficiency is largely localized to the brain, though it can be demonstrated in leukocytes and cultured skin fibroblasts. It must be distinguished from the Jansky-Bielschowsky presentation of neuronal ceroid lipofuscinosis, mitochondrial encephalopathy, lactic acidosis, strokelike episodes (MELAS) and myoclonic epilepsy with ragged-red fibers (MERRF) syndromes, atypical presentations of GM2 gangliosidoses (Tay-Sachs and Sandhoff's diseases), primary sialidosis (neuraminidase deficiency), galactosialidosis, and Alpers' disease. (J Child Neurol 1992;7(Suppl):S41-S50.)

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7

Murnane, R. D., A. J. Ahern-Rindell, and D. J. Prieur. "Ovine GM1 gangliosidosis." Small Ruminant Research 6, no. 1-2 (October 1991): 109–18. http://dx.doi.org/10.1016/0921-4488(91)90014-h.

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8

Luu, Amanda R., Cara Wong, Vishal Agrawal, Nathan Wise, Britta Handyside, Melanie J. Lo, Glenn Pacheco, et al. "Intermittent enzyme replacement therapy with recombinant human β-galactosidase prevents neuraminidase 1 deficiency." Journal of Biological Chemistry 295, no. 39 (July 28, 2020): 13556–69. http://dx.doi.org/10.1074/jbc.ra119.010794.

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Mutations in the galactosidase β 1 (GLB1) gene cause lysosomal β-galactosidase (β-Gal) deficiency and clinical onset of the neurodegenerative lysosomal storage disease, GM1 gangliosidosis. β-Gal and neuraminidase 1 (NEU1) form a multienzyme complex in lysosomes along with the molecular chaperone, protective protein cathepsin A (PPCA). NEU1 is deficient in the neurodegenerative lysosomal storage disease sialidosis, and its targeting to and stability in lysosomes strictly depend on PPCA. In contrast, β-Gal only partially depends on PPCA, prompting us to investigate the role that β-Gal plays in the multienzyme complex. Here, we demonstrate that β-Gal negatively regulates NEU1 levels in lysosomes by competitively displacing this labile sialidase from PPCA. Chronic cellular uptake of purified recombinant human β-Gal (rhβ-Gal) or chronic lentiviral-mediated GLB1 overexpression in GM1 gangliosidosis patient fibroblasts coincides with profound secondary NEU1 deficiency. A regimen of intermittent enzyme replacement therapy dosing with rhβ-Gal, followed by enzyme withdrawal, is sufficient to augment β-Gal activity levels in GM1 gangliosidosis patient fibroblasts without promoting NEU1 deficiency. In the absence of β-Gal, NEU1 levels are elevated in the GM1 gangliosidosis mouse brain, which are restored to normal levels following weekly intracerebroventricular dosing with rhβ-Gal. Collectively, our results highlight the need to carefully titrate the dose and dosing frequency of β-Gal augmentation therapy for GM1 gangliosidosis. They further suggest that intermittent intracerebroventricular enzyme replacement therapy dosing with rhβ-Gal is a tunable approach that can safely augment β-Gal levels while maintaining NEU1 at physiological levels in the GM1 gangliosidosis brain.

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9

Kochumon, Sheena, Dhanya Yesodharan, KP Vinayan, Natasha Radhakrishnan, Jayesh Sheth, and Sheela Nampoothiri. "GM2 activator protein deficiency, mimic of Tay-Sachs disease." International Journal of Epilepsy 04, no. 02 (December 2017): 184–87. http://dx.doi.org/10.1016/j.ijep.2017.08.001.

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AbstractGM2 Gangliosidoses are a group of autosomal recessive genetic disorders caused by intra-lysosomal deposition of ganglioside GM2 mainly in the neuronal cells. GM2-Activator protein deficiency is an extremely rare type of GM2 gangliosidosis (AB variant) caused by the mutation of GM2A.We report a case of a female child who presented with clinical features similar to classical Tay-Sachs disease, but with normal beta hexosaminidase enzyme levels. Molecular study revealed a novel homozygous intronic mutation which confirmed the diagnosis of GM2 Activator protein deficiency. GM2 Activator protein deficiency is a mimic of Classical Tay-Sachs disease and should be a differential diagnosis in children who present with neuroregression, cherry red spots without hepatosplenomegaly and with normal beta hexosaminidase enzyme levels.

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10

Denis, Robert, Jean-Louis Wayemberg, Michèle Vermeulen, Frans Gorus, Inge Liebaers, and Esther Vamos. "Hyperphosphatasemia in GM1 gangliosidosis." Journal of Pediatrics 120, no. 1 (January 1992): 164. http://dx.doi.org/10.1016/s0022-3476(05)80630-4.

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11

Pavlu, Jiri, Marie Jackson, and Nicki Panoskaltsis. "GM1-gangliosidosis type I." British Journal of Haematology 135, no. 4 (November 2006): 422. http://dx.doi.org/10.1111/j.1365-2141.2006.06287.x.

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12

Alroy, J., L. S. Adelman, and C. D. Warren. "Lectin histochemistry of gangliosidosis." Acta Neuropathologica 76, no. 4 (1988): 359–65. http://dx.doi.org/10.1007/bf00686972.

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13

Kornfeld, Mario. "LATE ONSET GM2 GANGLIOSIDOSIS." Journal of Neuropathology and Experimental Neurology 58, no. 5 (May 1999): 561. http://dx.doi.org/10.1097/00005072-199905000-00221.

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14

Alroy, J., V. Goyal, and C. D. Warren. "Lectin histochemistry of gangliosidosis." Acta Neuropathologica 76, no. 2 (1988): 109–14. http://dx.doi.org/10.1007/bf00688094.

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15

Grosso, Salvatore, Maria Angela Farnetani, Rosario Berardi, Maria Margollicci, Paolo Galluzzi, Rossella Vivarelli, Guido Morgese, and Paolo Ballestri. "GM2 gangliosidosis variant B1." Journal of Neurology 250, no. 1 (January 1, 2003): 17–21. http://dx.doi.org/10.1007/s00415-003-0925-3.

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16

Roze, Emmanuel, Soledad Navarro, Philippe Cornu, Marie-Laure Welter, and Marie Vidailhet. "DEEP BRAIN STIMULATION OF THE GLOBUS PALLIDUS FOR GENERALIZED DYSTONIA IN GM1 TYPE 3 GANGLIOSIDOSIS." Neurosurgery 59, no. 6 (December 1, 2006): E1340. http://dx.doi.org/10.1227/01.neu.0000245620.24603.1b.

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Abstract OBJECTIVE GM1 Type 3 gangliosidosis is a lysosomal storage disorder for which no specific treatment is available. It is characterized by progressive generalized dystonia, which is refractory to pharmacological treatment and results in severe disability and life-threatening complications. We performed bilateral pallidal stimulation in a patient with GM1 gangliosidosis and report the 12-month postoperative course. CLINICAL PRESENTATION A 24-year old woman presented with genetically confirmed GM1 gangliosidosis, resulting in severe progressive generalized dystonia. INTERVENTION Leads were implanted bilaterally into the internal part of the globus pallidus under stereotactic guidance. At follow-up visits, both the patient and the neurologists who performed the assessment were unaware of whether the neurostimulator was on or off. The patient was videotaped with a standardized protocol and scored by an independent expert. CONCLUSION After 1 year of follow-up, double-blind comparison of the patient's status with and without neurostimulation showed a 20% improvement, with a significant functional benefit, but no change in disease progression. Although further studies are needed to evaluate this therapeutic approach, this report suggests that pallidal stimulation might be a promising treatment for dystonia caused by GM1 Type 3 gangliosidosis.

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17

Morena, Francesco, Vasileios Oikonomou, Chiara Argentati, Martina Bazzucchi, Carla Emiliani, Angela Gritti, and Sabata Martino. "Integrated Computational Analysis Highlights unique miRNA Signatures in the Subventricular Zone and Striatum of GM2 Gangliosidosis Animal Models." International Journal of Molecular Sciences 20, no. 13 (June 28, 2019): 3179. http://dx.doi.org/10.3390/ijms20133179.

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This work explores for the first time the potential contribution of microRNAs (miRNAs) to the pathophysiology of the GM2 gangliosidosis, a group of Lysosomal Storage Diseases. In spite of the genetic origin of GM2 gangliosidosis, the cascade of events leading from the gene/protein defects to the cell dysfunction and death is not fully elucidated. At present, there is no cure for patients. Taking advantage of the animal models of two forms of GM2 gangliosidosis, Tay-Sachs (TSD) and Sandhoff (SD) diseases, we performed a microRNA screening in the brain subventricular zone (SVZ) and striatum (STR), which feature the neurogenesis and neurodegeneration states, respectively, in adult mutant mice. We found abnormal expression of a panel of miRNAs involved in lipid metabolism, CNS development and homeostasis, and neuropathological processes, highlighting region- and disease-specific profiles of miRNA expression. Moreover, by using a computational analysis approach, we identified a unique disease- (SD or TSD) and brain region-specific (SVZ vs. STR) miRNAs signatures of predicted networks potentially related to the pathogenesis of the diseases. These results may contribute to the understanding of GM2 gangliosidosis pathophysiology, with the aim of developing effective treatments.

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18

Chen, Joseph C., Amanda R. Luu, Nathan Wise, Rolando De Angelis, Vishal Agrawal, Linley Mangini, Jon Vincelette, et al. "Intracerebroventricular enzyme replacement therapy with β-galactosidase reverses brain pathologies due to GM1 gangliosidosis in mice." Journal of Biological Chemistry 295, no. 39 (September 3, 2019): 13532–55. http://dx.doi.org/10.1074/jbc.ra119.009811.

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Autosomal recessive mutations in the galactosidase β1 (GLB1) gene cause lysosomal β-gal deficiency, resulting in accumulation of galactose-containing substrates and onset of the progressive and fatal neurodegenerative lysosomal storage disease, GM1 gangliosidosis. Here, an enzyme replacement therapy (ERT) approach in fibroblasts from GM1 gangliosidosis patients with recombinant human β-gal (rhβ-gal) produced in Chinese hamster ovary cells enabled direct and precise rhβ-gal delivery to acidified lysosomes. A single, low dose (3 nm) of rhβ-gal was sufficient for normalizing β-gal activity and mediating substrate clearance for several weeks. We found that rhβ-gal uptake by the fibroblasts is dose-dependent and saturable and can be competitively inhibited by mannose 6-phosphate, suggesting cation-independent, mannose 6-phosphate receptor–mediated endocytosis from the cell surface. A single intracerebroventricularly (ICV) administered dose of rhβ-gal (100 μg) resulted in broad bilateral biodistribution of rhβ-gal to critical regions of pathology in a mouse model of GM1 gangliosidosis. Weekly ICV dosing of rhβ-gal for 8 weeks substantially reduced brain levels of ganglioside and oligosaccharide substrates and reversed well-established secondary neuropathology. Of note, unlike with the ERT approach, chronic lentivirus-mediated GLB1 overexpression in the GM1 gangliosidosis patient fibroblasts caused accumulation of a prelysosomal pool of β-gal, resulting in activation of the unfolded protein response and endoplasmic reticulum stress. This outcome was unsurprising in light of our in vitro biophysical findings for rhβ-gal, which include pH-dependent and concentration-dependent stability and dynamic self-association. Collectively, our results highlight that ICV-ERT is an effective therapeutic intervention for managing GM1 gangliosidosis potentially more safely than with gene therapy approaches.

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19

Hasegawa, Daisuke, Osamu Yamato, Yuya Nakamoto, Tsuyoshi Ozawa, Akira Yabuki, Kazuhito Itamoto, Takayuki Kuwabara, et al. "Serial MRI Features of Canine GM1 Gangliosidosis: A Possible Imaging Biomarker for Diagnosis and Progression of the Disease." Scientific World Journal 2012 (2012): 1–10. http://dx.doi.org/10.1100/2012/250197.

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GM1 gangliosidosis is a fatal neurodegenerative lysosomal storage disease caused by an autosomal recessively inherited deficiency ofβ-galactosidase activity. Effective therapies need to be developed to treat the disease. In Shiba Inu dogs, one of the canine GM1 gangliosidosis models, neurological signs of the disease, including ataxia, start at approximately 5 months of age and progress until the terminal stage at 12 to 15 months of age. In the present study, serial MR images were taken of an affected dog from a model colony of GM1 gangliosidosis and 4 sporadic clinical cases demonstrating the same mutation in order to characterize the MRI features of this canine GM1 gangliosidosis. By 2 months of age at the latest and persisting until the terminal stage of the disease, the MR findings consistently displayed diffuse hyperintensity in the white matter of the entire cerebrum on T2-weighted images. In addition, brain atrophy manifested at 9 months of age and progressed thereafter. Although a definitive diagnosis depends on biochemical and genetic analyses, these MR characteristics could serve as a diagnostic marker in suspect animals with or without neurological signs. Furthermore, serial changes in MR images could be used as a biomarker to noninvasively monitor the efficacy of newly developed therapeutic strategies.

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20

Satoh, Hiroyuki, Toyofumi Yamauchi, Masahiro Yamasaki, Yoshimitsu Maede, Akira Yabuki, Hye-Sook Chang, Taketoshi Asanuma, and Osamu Yamato. "Rapid detection of GM1 ganglioside in cerebrospinal fluid in dogs with GM1 gangliosidosis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry." Journal of Veterinary Diagnostic Investigation 23, no. 6 (October 24, 2011): 1202–7. http://dx.doi.org/10.1177/1040638711425592.

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The concentration of GM1 (monosialotetrahexosyl ganglioside) in cerebrospinal fluid (CSF) is markedly increased in dogs with GM1 gangliosidosis due to GM1 accumulation in the central nervous system and leakage to the CSF. The present study established a rapid and simple method for detection of accumulated GM1 in the CSF in dogs with GM1 gangliosidosis using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI TOF MS) and discusses the usefulness of this method for the rapid diagnosis and/or high-risk screening of this disease in domestic animals. Cerebrospinal fluid was collected from normal dogs and 4- to 11-month-old Shiba dogs with GM1 gangliosidosis. The MALDI TOF MS analysis was carried out in combination with a special sample plate and a simple desalting step on the plate. Specific signs of GM1 could be detected in the standard GM1 solutions at concentrations of 50 nmol/l or more. The signs were also clearly detected in CSF (131–618 nmol/l) in affected dogs, but not in normal canine CSF (12 ± 5 nmol/l, mean ± standard deviation). The results demonstrated that MALDI TOF MS can detect GM1 accumulated in canine CSF even in the early stage of the disease. In conclusion, the rapid detection of increased CSF GM1 using MALDI TOF MS is a useful method for diagnosis and/or screening for canine GM1 gangliosidosis.

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21

Hasegawa, Daisuke, Osamu Yamato, Masanori Kobayashi, Michio Fujita, Shinichiro Nakamura, Kimimasa Takahashi, Hiroyuki Satoh, et al. "Clinical and molecular analysis of GM2 gangliosidosis in two apparent littermate kittens of the Japanese domestic cat." Journal of Feline Medicine and Surgery 9, no. 3 (June 2007): 232–37. http://dx.doi.org/10.1016/j.jfms.2006.11.003.

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This case report documents clinical and molecular findings in two littermate kittens of the Japanese domestic cat with GM2 gangliosidosis variant 0. Analysis included detailed physical, magnetic resonance imaging, biochemical, pathological and genetic examinations. At first, these littermate kittens showed typical cerebellar signs at approximately 2 months of age. About 2 months later, they progressively showed other neurological signs and subsequently died at about 7 months of age. Magnetic resonance imaging just before the death showed an enlarged ventricular system, T1 hyperintensity in the internal capsule, and T2 hyperintensity in the white matter of the whole brain. Histological findings suggested a type of lysosomal storage disease. Biochemical studies demonstrated that the kittens were affected with GM2 gangliosidosis variant 0, and a DNA assay finally demonstrated that these animals were homozygous for the mutation, which the authors had identified in a different family of the Japanese domestic cat. The findings in the present cases provide useful information about GM2 gangliosidosis variant 0 in Japanese domestic cats.

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22

D'Agrosa, R. M., M. Hubbes, S. Zhang, R. Shankaran, and J. W. Callahan. "Characteristics of the β-galactosidase-carboxypeptidase complex in GM1-gangliosidosis and β-galactosialidosis fibroblasts." Biochemical Journal 285, no. 3 (August 1, 1992): 833–38. http://dx.doi.org/10.1042/bj2850833.

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Lysosomal beta-galactosidase (beta-Gal) occurs either alone in monomeric and dimeric forms, or in a high-M(r) complex with at least two additional proteins. One is neuraminidase and the second is the protective protein, which has also been shown to possess carboxypeptidase activity. beta-Gal activity is deficient in GM1-gangliosidosis as a primary defect, and is secondarily affected in galactosialidosis (GS), where the primary defect is the absence of protective protein activity. Fibroblasts from three patients with GM1-gangliosidosis, type 1, showed markedly reduced amounts of beta-Gal cross-reacting material (CRM), and a fourth appeared to have normal levels. A patient with type 2 GM1-gangliosidosis was also found to be CRM-normal. These findings demonstrate that patients with GM1-gangliosidosis type 1 are heterogeneous with respect to the level of residual beta-Gal protein. Fibroblasts from four patients with GS were strongly CRM-positive with an anti-beta-Gal antibody, as was a sample of brain from one of these patients, suggesting that the loss of beta-Gal activity is linked to a subtler change in the primary structure of the enzyme than has been previously thought. While three GS cell lines displayed reduced carboxypeptidase activity (to 32-42% of the control), one cell line was completely devoid of activity, demonstrating that while carboxypeptidase activity is a property of the protective protein this action is distinct and separate from its protective role. On direct immunoprecipitation with anti-beta-Gal antibody, a portion of the total carboxypeptidase activity co-precipitated with beta-Gal from extracts of normal and GM1-gangliosidosis cells, consistent with the presence of the complex in these cells. However, no carboxypeptidase activity was precipitable with this antibody from GS fibroblasts, suggesting the absence of complex from these cells. To examine this further, the various forms of beta-Gal were resolved by h.p.l.c. molecular-sieve chromatography. Three forms of beta-Gal activity were resolved in normal cells: a complex, a dimer and a monomer. Residual beta-Gal activity of GS cells resolved into two of these forms, the complex and the monomer. In normal and GM1-gangliosidosis cells a portion of the total carboxypeptidase activity co-chromatographed with the complex while the bulk of the activity occurred in a single 36,000-M(r) peak. Only the low-M(r) carboxypeptidase activity was detected in GS cells. This confirms our results on immunoprecipitation indicating that portions of the beta-Gal and the carboxypeptidase activities exist outside the complex in normal, GM1-gangliosidosis and GS cells. In summary, the loss of protective protein function from GS cells results in disproportionate loss of the dimeric and monomeric forms of beta-Gal activity, but does not result in the complete degradation of the protein.

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Zhurkova, N. V., K. V. Savostyanov, A. A. Pushkov, E. M. Mazurina, E. V. Uvakina, E. Y. Basargina, O. B. Kondakova, et al. "Russian patients with GM1-gangliosidosis." Molecular Genetics and Metabolism 129, no. 2 (February 2020): S166. http://dx.doi.org/10.1016/j.ymgme.2019.11.443.

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24

Hennermann, Julia B., Marlene Seegräber, Yasmina Amraoui, Seyfullah Gökce, Jörg Reinke, Andrea Dieckmann, Martin Smitka, et al. "Clinical variability of GM1 gangliosidosis." Molecular Genetics and Metabolism 123, no. 2 (February 2018): S62. http://dx.doi.org/10.1016/j.ymgme.2017.12.150.

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25

Bermudez, A. J., G. C. Johnson, M. T. Vanier, M. Schröder, K. Suzuki, P. L. Stogsdill, G. S. Johnson, et al. "Gangliosidosis in Emus (Dromaius novaehollandiae)." Avian Diseases 39, no. 2 (April 1995): 292. http://dx.doi.org/10.2307/1591870.

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26

Yamato, O., Y. Masuoka, M. Tajima, S. Omae, Y. Maede, K. Ochiai, E. Hayashida, T. Umemura, and M. lijima. "GM1 gangliosidosis in shiba dogs." Veterinary Record 146, no. 17 (April 22, 2000): 493–96. http://dx.doi.org/10.1136/vr.146.17.493.

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27

Lewis, Chris, Mark Wessels, Helen Carty, Pauline Baird, Timothy Cox, Begoña Cachón, Susan Wang, Paul Holmes, Adrienne Mackintosh, and Francesca Chianini. "Testing sheep for GM2 gangliosidosis." Veterinary Record 175, no. 10 (September 12, 2014): 260.1–260. http://dx.doi.org/10.1136/vr.g5560.

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28

Sakuraba, Hitoshi, Kohji Itoh, Masaharu Kotani, Tadashi Tai, Hideo Yamada, Kenji Kurosawa, Yoshikazu Kuroki, et al. "Prenatal diagnosis of GM2-gangliosidosis." Brain and Development 15, no. 4 (July 1993): 278–82. http://dx.doi.org/10.1016/0387-7604(93)90023-2.

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Ushiyama, Masao, Shu-ichi Ikeda, Jun Nakayama, Nobuo Yanagisawa, Norinao Hanyu, and Tsutomu Katsuyama. "Type III (chronic) GM1-gangliosidosis." Journal of the Neurological Sciences 71, no. 2-3 (December 1985): 209–23. http://dx.doi.org/10.1016/0022-510x(85)90060-7.

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30

Rha, Allisandra K., Anne S. Maguire, and Douglas R. Martin. "GM1 Gangliosidosis: Mechanisms and Management." Application of Clinical Genetics Volume 14 (April 2021): 209–33. http://dx.doi.org/10.2147/tacg.s206076.

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31

Streifler, J., M. Golomb, and N. Gadoth. "Psychiatric Features of Adult GM2 Gangliosidosis." British Journal of Psychiatry 155, no. 3 (September 1989): 410–13. http://dx.doi.org/10.1192/bjp.155.3.410.

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The report describes three unrelated Ashkenazi Jewish women with adult GM2 gangliosidosis in whom mental symptoms were prominent, mimicking different psychiatric disorders, and thus delaying accurate diagnosis.

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32

Zyukina, Z. V., and T. A. Lobaeva. "LIPID METABOLISM DISEASES BY EXAMPLE GM2 GANGLIOZIDOSIS AND PREDISPOSITION TO THEM OF CERTAIN ETHNIC GROUPS OF PEOPLE." EurasianUnionScientists 3, no. 2(71) (2020): 34–36. http://dx.doi.org/10.31618/esu.2413-9335.2020.3.71.592.

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The relevance of the study is due to the fact that the scientific literature does not have sufficient data on the predisposition of certain ethnic groups of people to metabolic diseases on the example of GM2 gangliosidosis, so the purpose of the work is to clarify and analyze this predisposition of some ethnic groups of people to Tey — Sachs disease (GM2 gangliosidosis, amaurotic idiocy). The research materials and methods are a scientific and analytical review of modern publications on this topic. Research result: a review of the scientific literature has shown that the Jewish population of Eastern European origin (Ashkenazi Jews) has a higher incidence of TaySachs disease and other lipid accumulation diseases. Conclusions: the frequency of hereditary metabolic diseases ranges from 1: 2000 newborns to 1:1000000, and many of these diseases are characterized by differences in the frequency of occurrence in different ethnic groups and populations. In relation to GM2 gangliosidosis, it is shown that 1 in 27-30 Ashkenazi Jews in the United States is a recessive carrier of this disease. BTS affects 1 in 3,600 newborn Jews. One in 20 Jews have a hereditary predisposition to the disease.

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Gualdrón-Frías, Carlos Andrés, and Laura Tatiana Calderón-Nossa. "Tay-Sachs disease." Revista de la Facultad de Medicina 67, no. 3 (July 1, 2019): 323–29. http://dx.doi.org/10.15446/revfacmed.v67n3.69742.

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Introduction: Lysosomal storage disease is caused by the deficiency of a single hydrolase (lysosomal enzymes). GM2 gangliosidoses are autosomal recessive disorders caused by deficiency of β-hexosaminidase and Tay-Sachs disease (TSD) is one of its three forms.Objective: To perform a review of the state of the art on TSD describing its definition, epidemiology, etiology, physiopathology, clinical manifestations and news in diagnosis and treatment.Materials and methods: A literature search was carried out in PubMed using the MeSH terms “Tay-Sachs Disease”.Results: 1 233 results were retrieved in total, of which 53 articles were selected. TSD is caused by the deficiency of the lysosomal enzyme β-hexosaminidase A (HexA), and is characterized by neurodevelopmental regression, hypotonia, hyperacusis and cherry-red spots in the macula. Research on molecular pathogenesis and the development of possible treatments has been limited, consequently there is no treatment established to date.Conclusion: TSD is an autosomal recessive neurodegenerative disorder. Death usually occurs before the age of five. More research and studies on this type of gangliosidosis are needed in order to find an adequate treatment.

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Cachon-Gonzalez, Maria Begona, Eva Zaccariotto, and Timothy Martin Cox. "Genetics and Therapies for GM2 Gangliosidosis." Current Gene Therapy 18, no. 2 (May 7, 2018): 68–89. http://dx.doi.org/10.2174/1566523218666180404162622.

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Eichler, Florian, Ourania Giannikopoulos, Swati Sathe, Kim Crawford, and Cynthia Tifft. "48. Diagnostic delay in GM2 gangliosidosis." Molecular Genetics and Metabolism 96, no. 2 (February 2009): S22. http://dx.doi.org/10.1016/j.ymgme.2008.11.049.

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Pan, Jessica, Paul Caruso, Daniel Loes, Kim Kubilus, Douglas Hayden, and Florian Eichler. "Brain MRI abnormalities in GM2-gangliosidosis." Molecular Genetics and Metabolism 108, no. 2 (February 2013): S71—S72. http://dx.doi.org/10.1016/j.ymgme.2012.11.187.

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Freischütz, Bettina, Akira Tokuda, Toshio Ariga, Alex J. Bermudez, and Robert K. Yu. "Unusual Gangliosidosis in Emu (Dromaius novaehollandiae)." Journal of Neurochemistry 68, no. 5 (November 18, 2002): 2070–78. http://dx.doi.org/10.1046/j.1471-4159.1997.68052070.x.

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Stieb, N., and M. Beck. "Infantile GM1 gangliosidosis without dysmorphic features." Acta Paediatrica 91 (January 2, 2007): 155–56. http://dx.doi.org/10.1111/j.1651-2227.2002.tb03192.x.

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Cox, N. R., S. J. Ewald, N. E. Morrison, A. S. Gentry, M. Schuler, and H. J. Baker. "Thymic alterations in feline GM1 gangliosidosis." Veterinary Immunology and Immunopathology 63, no. 4 (June 1998): 335–53. http://dx.doi.org/10.1016/s0165-2427(98)00113-5.

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Ohno, Kousaku, and Kunihiko Suzuki. "Mutation in GM2-Gangliosidosis B1 Variant." Journal of Neurochemistry 50, no. 1 (January 1988): 316–18. http://dx.doi.org/10.1111/j.1471-4159.1988.tb13266.x.

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Bley, A. E., O. A. Giannikopoulos, D. Hayden, K. Kubilus, C. J. Tifft, and F. S. Eichler. "Natural History of Infantile GM2 Gangliosidosis." PEDIATRICS 128, no. 5 (October 24, 2011): e1233-e1241. http://dx.doi.org/10.1542/peds.2011-0078.

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Kotagal, Suresh. "Diagnosis of AB variant, GM2 gangliosidosis." Annals of Neurology 19, no. 1 (January 1986): 102. http://dx.doi.org/10.1002/ana.410190129.

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Bieber, F. R., G. Mortimer, E. H. Kolodny, and S. G. Driscoll. "Pathologic Findings in Fetal GM1 Gangliosidosis." Archives of Neurology 43, no. 7 (July 1, 1986): 736–38. http://dx.doi.org/10.1001/archneur.1986.00520070090027.

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Inzelberg, R., and A. D. Korczyn. "Parkinsonism in adult-onset GM2 gangliosidosis." Movement Disorders 9, no. 3 (1994): 375–77. http://dx.doi.org/10.1002/mds.870090325.

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Cummings, J. F., P. A. Wood, S. U. Walkley, A. de Lahunta, and M. E. DeForest. "GM2 gangliosidosis in a Japanese Spaniel." Acta Neuropathologica 67, no. 3-4 (September 1985): 247–53. http://dx.doi.org/10.1007/bf00687809.

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Lynch, David T., and David R. Czuchlewski. "Peripheral blood findings in GM1 gangliosidosis." Blood 127, no. 17 (April 28, 2016): 2161. http://dx.doi.org/10.1182/blood-2016-02-699215.

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Erol, Ilknur, Füsun Alehan, M. Ali Pourbagher, Oguz Canan, and S. Vefa Yildirim. "Neuroimaging findings in infantile GM1 gangliosidosis." European Journal of Paediatric Neurology 10, no. 5-6 (September 2006): 245–48. http://dx.doi.org/10.1016/j.ejpn.2006.08.005.

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Wessels, M. E., J. P. Holmes, M. Jeffrey, M. Jackson, A. Mackintosh, E. H. Kolodny, B. J. Zeng, C. B. Wang, and S. F. E. Scholes. "GM2 Gangliosidosis in British Jacob Sheep." Journal of Comparative Pathology 150, no. 2-3 (February 2014): 253–57. http://dx.doi.org/10.1016/j.jcpa.2013.10.003.

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Tuteja, Moni, Abdul Mueed Bidchol, Katta Mohan Girisha, and Shubha R. Phadke. "White matter changes in GM1 gangliosidosis." Indian Pediatrics 52, no. 2 (February 2015): 155–56. http://dx.doi.org/10.1007/s13312-015-0593-2.

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Suzuki, Y. "Chemical chaperone therapy for GM1-gangliosidosis." Cellular and Molecular Life Sciences 65, no. 3 (January 19, 2008): 351–53. http://dx.doi.org/10.1007/s00018-008-7470-2.

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