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Journal articles on the topic 'GM1 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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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

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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4

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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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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6

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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7

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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8

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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9

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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10

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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11

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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12

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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13

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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14

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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15

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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16

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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17

Eikelberg, Deborah, Annika Lehmbecker, Graham Brogden, Witchaya Tongtako, Kerstin Hahn, Andre Habierski, Julia B. Hennermann, et al. "Axonopathy and Reduction of Membrane Resistance: Key Features in a New Murine Model of Human GM1-Gangliosidosis." Journal of Clinical Medicine 9, no. 4 (April 2, 2020): 1004. http://dx.doi.org/10.3390/jcm9041004.

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GM1-gangliosidosis is caused by a reduced activity of β-galactosidase (Glb1), resulting in intralysosomal accumulations of GM1. The aim of this study was to reveal the pathogenic mechanisms of GM1-gangliosidosis in a new Glb1 knockout mouse model. Glb1−/− mice were analyzed clinically, histologically, immunohistochemically, electrophysiologically and biochemically. Morphological lesions in the central nervous system were already observed in two-month-old mice, whereas functional deficits, including ataxia and tremor, did not start before 3.5-months of age. This was most likely due to a reduced membrane resistance as a compensatory mechanism. Swollen neurons exhibited intralysosomal storage of lipids extending into axons and amyloid precursor protein positive spheroids. Additionally, axons showed a higher kinesin and lower dynein immunoreactivity compared to wildtype controls. Glb1−/− mice also demonstrated loss of phosphorylated neurofilament positive axons and a mild increase in non-phosphorylated neurofilament positive axons. Moreover, marked astrogliosis and microgliosis were found, but no demyelination. In addition to the main storage material GM1, GA1, sphingomyelin, phosphatidylcholine and phosphatidylserine were elevated in the brain. In summary, the current Glb1−/− mice exhibit a so far undescribed axonopathy and a reduced membrane resistance to compensate the functional effects of structural changes. They can be used for detailed examinations of axon–glial interactions and therapy trials of lysosomal storage diseases.

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18

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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19

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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21

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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22

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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23

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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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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Suzuki, Yoshiyuki, Seiichiro Ogawa, and Yasubumi Sakakibara. "Chaperone Therapy for Neuronopathic Lysosomal Diseases: Competitive Inhibitors as Chemical Chaperones for Enhancement of Mutant Enzyme Activities." Perspectives in Medicinal Chemistry 3 (January 2009): PMC.S2332. http://dx.doi.org/10.4137/pmc.s2332.

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Chaperone therapy is a newly developed molecular approach to lysosomal diseases, a group of human genetic diseases causing severe brain damage. We found two valienamine derivatives, N-octyl-4-epi-β-valienamine (NOEV) and N-octyl-β-valienamine (NOV), as promising therapeutic agents for human β-galactosidase deficiency disorders (mainly GM1-gangliosidosis) and β-glucosidase deficiency disorders (Gaucher disease), respectively. We briefly reviewed the historical background of research in carbasugar glycosidase inhibitors. Originally NOEV and NOV had been discovered as competitive inhibitors, and then their paradoxical bioactivities as chaperones were confirmed in cultured fibroblasts from patients with these disorders. Subsequently GM1-gangliosidosis model mice were developed and useful for experimental studies. Orally administered NOEV entered the brain through the blood-brain barrier, enhanced β-galactosidase activity, reduced substrate storage, and improved neurological deterioration clinically. Furthermore, we executed computational analysis for prediction of molecular interactions between β-galactosidase and NOEV. Some preliminary results of computational analysis of molecular interaction mechanism are presented in this article. NOV also showed the chaperone effect toward several β-glucosidase gene mutations in Gaucher disease. We hope chaperone therapy will become available for some patients with GM1-gangliosidosis, Gaucher disease, and potentially other lysosomal storage diseases with central nervous system involvement.

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Arthur, Julian R., Karie A. Heinecke, and Thomas N. Seyfried. "Filipin recognizes both GM1 and cholesterol in GM1 gangliosidosis mouse brain." Journal of Lipid Research 52, no. 7 (April 20, 2011): 1345–51. http://dx.doi.org/10.1194/jlr.m012633.

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Sano, Renata, Vera M. T. Trindade, Alessandra Tessitore, Alessandra d'Azzo, Matheus B. Vieira, Roberto Giugliani, and Janice C. Coelho. "GM1-ganglioside degradation and biosynthesis in human and murine GM1-gangliosidosis." Clinica Chimica Acta 354, no. 1-2 (April 2005): 131–39. http://dx.doi.org/10.1016/j.cccn.2004.11.035.

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Liu, Sichi, Yuyu Feng, Yonglan Huang, Xiaoling Jiang, Chengfang Tang, Fang Tang, Chunhua Zeng, and Li Liu. "A GM1 gangliosidosis mutant mouse model exhibits activated microglia and disturbed autophagy." Experimental Biology and Medicine 246, no. 11 (February 14, 2021): 1330–41. http://dx.doi.org/10.1177/1535370221993052.

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GM1 gangliosidosis is a rare lysosomal storage disease caused by a deficiency of β-galactosidase due to mutations in the GLB1 gene. We established a C57BL/6 mouse model with Glb1G455R mutation using CRISPR/Cas9 genome editing. The β-galactosidase enzyme activity of Glb1G455R mice measured by fluorometric assay was negligible throughout the whole body. Mutant mice displayed no marked phenotype at eight weeks. After 16 weeks, GM1 ganglioside accumulation in the brain of mutant mice was observed by immunohistochemical staining. Meanwhile, a declining performance in behavioral tests was observed among mutant mice from 16 to 32 weeks. As the disease progressed, the neurological symptoms of mutant mice worsened, and they then succumbed to the disease by 47 weeks of age. We also observed microglia activation and proliferation in the cerebral cortex of mutant mice at 16 and 32 weeks. In these activated microglia, the level of autophagy regulator LC3 was up-regulated but the mRNA level of LC3 was normal. In conclusion, we developed a novel murine model that mimicked the chronic phenotype of human GM1. This Glb1G455R murine model is a practical in vivo model for studying the pathogenesis of GM1 gangliosidosis and exploring potential therapies.

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Millichap, J. Gordon. "GM1 Gangliosidosis Type 1 and Mongolian Spots." Pediatric Neurology Briefs 27, no. 6 (June 1, 2013): 47. http://dx.doi.org/10.15844/pedneurbriefs-27-6-10.

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31

Burton Esterly, Nancy, Marc Weissbluth, and William A. Caro. "Mongolian spots and GM1 type 1 gangliosidosis." Journal of the American Academy of Dermatology 22, no. 2 (February 1990): 320. http://dx.doi.org/10.1016/s0190-9622(08)80773-6.

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Mano, T., S. Matsuda, M. Taira, T. Yamamoto, J. Shimizu, A. Iwata, and S. Tsuji. "Clinical features of GM1 gangliosidosis type 3." Journal of the Neurological Sciences 333 (October 2013): e97. http://dx.doi.org/10.1016/j.jns.2013.07.607.

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Ahern-Rindell, Amelia. "52 A unique model of GM1 gangliosidosis." Molecular Genetics and Metabolism 92, no. 4 (December 2007): 23. http://dx.doi.org/10.1016/j.ymgme.2007.08.057.

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34

Ida, Hiroyuki, Yoshikatsu Eto, and Kihei Maekawa. "Fetal GM1-gangliosidosis: Morphological and biochemical studies." Brain and Development 11, no. 6 (January 1989): 394–98. http://dx.doi.org/10.1016/s0387-7604(89)80023-3.

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35

Ohta, K., S. Tsuji, Y. Mizuno, T. Atsumi, T. Yahagi, and T. Miyatake. "Type 3 (adult) GM1 gangliosidosis: Case report." Neurology 35, no. 10 (October 1, 1985): 1490. http://dx.doi.org/10.1212/wnl.35.10.1490.

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36

O'Brien, John S., Rainer Storb, Robert F. Raff, Jane Harding, Frederick Appelbaum, Satoshi Morimoto, Yasuo Kishimoto, Ted Graham, Amelia Ahern-Rindell, and Susan L. O'Brien. "Bone marrow transplantation in canine GM1 gangliosidosis." Clinical Genetics 38, no. 4 (June 28, 2008): 274–80. http://dx.doi.org/10.1111/j.1399-0004.1990.tb03581.x.

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37

Folkerth, R. D., I. Bhan, and J. Alroy. "DELAYED TELENCEPHALIC MYELINATION IN INFANTILE GM1 GANGLIOSIDOSIS." Journal of Neuropathology and Experimental Neurology 57, no. 5 (May 1998): 483. http://dx.doi.org/10.1097/00005072-199805000-00068.

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38

Barker, C. G., W. F. Blakemore, A. Dell, A. C. Palmer, P. R. Tiller, and B. G. Winchester. "GM1 gangliosidosis (type 1) in a cat." Biochemical Journal 235, no. 1 (April 1, 1986): 151–58. http://dx.doi.org/10.1042/bj2350151.

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Abstract:

A kitten with clinical and morphological symptoms of a neurovisceral lysosomal-storage disease has been shown to have a marked deficiency of acidic beta-D-galactosidase in the brain, kidney and spleen. Chromatography on concanavalin A-Sepharose and inhibition studies with 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine, a selective inhibitor of the neutral broad-specificity beta-D-galactosidase, have shown that the residual beta-D-galactosidase at pH 4.0 in the tissues of the affected cat is due to the neutral beta-D-galactosidase and that there is a complete deficiency of the acidic (lysosomal) beta-D-galactosidase. There is marked accumulation in all tissues and excretion in the urine of neutral oligosaccharides. Analysis of these oligosaccharides by fast-atom-bombardment mass spectrometry and g.l.c. suggests that they arise from the incomplete catabolism of N-glycans of glycoproteins. The ganglioside content of all the tissues is elevated, and it has been shown by t.l.c. that the concentration of a ganglioside fraction with a mobility similar to that of GM1 ganglioside is particularly increased. There is also some evidence of accumulation of glycosaminoglycans in the brain. The clinical symptoms, the complete deficiency of acidic beta-D-galactosidase and the storage products in visceral organs all suggest that this is a case of feline GM1-type gangliosidosis comparable with the severe infantile (Type 1) form of the disease in humans.

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39

Skelly, Barbara J., Martin Jeffrey, Robin J. M. Franklin, and Bryan G. Winchester. "A new form of ovine GM1-gangliosidosis." Acta Neuropathologica 89, no. 4 (April 1995): 374–79. http://dx.doi.org/10.1007/bf00309632.

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40

Kaye, Edward M., Joseph Alroy, Srinivasa S. Raghavan, Gerald A. Schwarting, Lester S. Adelman, Val Runge, Dafna Gelblum, Johann G. Thalhammer, and Gonzalo Zuniga. "Dysmyelinogenesis in animal model of GM1 gangliosidosis." Pediatric Neurology 8, no. 4 (July 1992): 255–61. http://dx.doi.org/10.1016/0887-8994(92)90361-2.

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41

Taketomi, T., A. Hara, K. Uemura, and E. Sugiyama. "Matrix-assisted laser desorption ionization time-of-flight mass spectrometric analysis of glycosphingolipids including gangliosides." Acta Biochimica Polonica 45, no. 4 (December 31, 1998): 987–99. http://dx.doi.org/10.18388/abp.1998_4356.

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Long chain base compositions of gangliosides containing mainly stearic acid could be determined without any chemical modification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry with delayed ion extraction (DE MALDI-TOF MS). The analytical results for the long chain base compositions of various samples of GM1 from the brain tissues of patients with different diseases at different ages confirmed that the proportion of d20:1 (icosasphingosine) and d20 (icosa-sphinganine) of the total sphingosine bases increased quickly until adolescent or adult age and then remained constant slightly exceeding 50%; this value was evidently higher than the proportion of d20:1 and d20 of GM1 in various adult mammalian brains. A long chain base composition of GM1 from the brain tissue of a patient with infantile type of GM1-gangliosidosis at 4y2m was abnormal and so was in two sibling patients with Spielmeyer-Vogt type of juvenile amaurotic idiocy at 19y and 21y in spite of that in the latter there was no accumulation of GM1 in the brain tissue. On the other hand, a patient with adult type of GM1 gangliosidosis at 66y showed a local accumulation of GM1 in the putamen and caudate nucleus, but its long chain base composition was found to be normal. It was of interest that the white matter of Eker rat with hereditary renal carcinoma contained a large amount of plasmalocerebroside as compared with the amount of cerebroside and sphingomyelin. The individual molecular species of plasmalocerebroside were identified by DE MALDI-TOF MS.

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Maeda, Yuki, Keiichi Motoyama, Taishi Higashi, Yuka Horikoshi, Toru Takeo, Naomi Nakagata, Yuki Kurauchi, et al. "Effects of cyclodextrins on GM1-gangliosides in fibroblasts from GM1-gangliosidosis patients." Journal of Pharmacy and Pharmacology 67, no. 8 (April 7, 2015): 1133–42. http://dx.doi.org/10.1111/jphp.12405.

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43

Kordysz, Ewa, and Bogdan Woźniewicz. "Landing Disease, Gm1 Generalized Gangliosidosis, and Malabsorption Syndrome." Pediatric Pathology 9, no. 4 (January 1989): 467–73. http://dx.doi.org/10.3109/15513818909022367.

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Lawrence, Roger, Jeremy L. Van Vleet, Linley Mangini, Adam Harris, Nathan Martin, Wyatt Clark, Sanjay Chandriani, et al. "Characterization of glycan substrates accumulating in GM1 Gangliosidosis." Molecular Genetics and Metabolism Reports 21 (December 2019): 100524. http://dx.doi.org/10.1016/j.ymgmr.2019.100524.

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Ahern-Rindell, Amelia. "2. Characterization of ovine GM1 gangliosidosis using immunofluoresence." Molecular Genetics and Metabolism 93, no. 2 (February 2008): 14. http://dx.doi.org/10.1016/j.ymgme.2007.10.014.

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Kolodny, Edwin, Brian Frankel, Paola Torres, Joseph Alroy, and Srinivasa Raghavan. "56. GM1-gangliosidosis in an American Black Bear." Molecular Genetics and Metabolism 93, no. 2 (February 2008): 28. http://dx.doi.org/10.1016/j.ymgme.2007.10.068.

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Mishra, Shivani, Pranita Pai, Anusha Uttarilli, and Katta Mohan Girisha. "Mongolian spots in GM1 gangliosidosis: a pictorial report." Clinical Dysmorphology 30, no. 1 (October 7, 2020): 6–9. http://dx.doi.org/10.1097/mcd.0000000000000353.

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48

Geotting, Mark G., and Majed J. Dasouki. "Cerebral atrophy, macrosomia, andcutaneous telangiectasia in GM1 gangliosidosis." Journal of Pediatrics 107, no. 4 (October 1985): 644–45. http://dx.doi.org/10.1016/s0022-3476(85)80046-9.

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Teresa Sinelli, Maria, Mario Motta, Donatella Cattarelli, Maria Luisa Cardone, and Gaetano Chirico. "Fetal hydrops in GM1 gangliosidosis: A case report." Acta Paediatrica 94, no. 12 (January 2, 2007): 1847–49. http://dx.doi.org/10.1111/j.1651-2227.2005.tb01867.x.

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50

Hultberg, Bjourn, and Sture Sjoublad. "β -D-galactosidase activities in juvenile GM1-gangliosidosis." Acta Neurologica Scandinavica 58, no. 4 (January 29, 2009): 221–29. http://dx.doi.org/10.1111/j.1600-0404.1978.tb02882.x.

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