Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice
Abstract
Neuraminidase initiates the hydrolysis of sialo-glycoconjugates by removing their terminal sialic acid residues. In humans, primary or secondary deficiency of this enzyme leads to two clinically similar neurodegenerative lysosomal storage disorders: sialidosis and galactosialidosis (GS). Mice nullizygous at the Neu1 locus develop clinical abnormalities reminiscent of early-onset sialidosis in children, including severe nephropathy, progressive edema, splenomegaly, kyphosis and urinary excretion of sialylated oligosaccharides. Although the sialidosis mouse model shares clinical and histopathological features with GS mice and GS patients, we have identified phenotypic abnormalities that seem specific for sialidosis mice. These include progressive deformity of the spine, high incidence of premature death, age-related extramedullary hematopoiesis, and lack of early degeneration of cerebellar Purkinje cells. The differences and similarities identified in these sialidosis and GS mice may help to better understand the pathophysiology of these diseases in children and to identify more targeted therapies for each of these diseases.
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Early in life Ppca−/− mice acquire acute and progressive ataxia associated with regional loss of cerebellar Purkinje cells and impaired motor coordination, a phenotype not observed in Neu1−/− mice at least not until the end of their lifespan (5-7 months).
“The most overt difference is seen in the cerebellum; early in life Ppca−/− mice acquire acute and progressive ataxia that is associated with regional loss of cerebellar Purkinje cells and impaired motor coordination (Figure 3) 56.”
From Galactosialidosis: historic aspects and overview of investigated and emerging treatment options (2017) · cites this paper as [56]
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Annunziata, I., Patterson, A., Helton, D., Hu, H., Moshiach, S., Gomero, E., Nixon, R., & d’Azzo, A. (2013) · Nature Communications · doi:10.1038/ncomms3734 · Cited by 146 · see citing works
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Tejwani, V., Andersen, M. R., Nam, J. H., & Sharfstein, S. T. (2018) · Biotechnology Journal · doi:10.1002/biot.201700234 · Cited by 70 · see citing works
Galactosialidosis: historic aspects and overview of investigated and emerging treatment options
Annunziata, I., & d’Azzo, A. (2017) · Expert Opinion on Orphan Drugs · doi:10.1080/21678707.2016.1266933 · Cited by 50 · see citing works
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Fremuth, L. E., van de Vlekkert, D., Hu, H., Weesner, J. A., Annunziata, I., Yogalingam, G., & d’Azzo, A. (2025) · doi:10.1101/2025.04.28.651121 · Cited by 1 · see citing works
- Authors
- de Geest, N.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-06-01
- Volume
- 11
- Issue
- 12
- Pages
- 1455-1464
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2107811485
- Cited by
- 127
- References
- 0
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 5 · 2023: 3 · 2022: 8 · 2021: 7 · 2020: 9 · 2019: 6 · 2018: 7 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 6 · 2012: 2
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed (publishedVersion)
- Human Molecular Genetics
- Funders
- American Lebanese Syrian Associated Charities
- National Institutes of Health
- National Cancer Institute (CA21765, P30CA021765)
- National Institute of General Medical Sciences (GM-60950, R01GM060950)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-52025)
- Topics
- Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- sialidosis, galactosialidosis, neuraminidase deficiency, NEU1, lysosomal storage disease, sialic acid, mouse model, neurodegeneration, spinal deformity, extramedullary hematopoiesis, Purkinje cell degeneration, kidney disease, splenomegaly, edema, kyphosis
- MeSH terms
- Animals, beta-Galactosidase, Carboxypeptidases, Disease Models, Animal, Hematopoiesis, Extramedullary, Humans, Mucolipidoses, Neuraminidase, Organ Specificity, Cathepsin A, Mice
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