Abstract | PURPOSE OF REVIEW: RECENT FINDINGS: Owing to the mutated gene, it was expected that the pathomechanism of this myopathy would be based on hyposialylation, a highly controversial phenomenon. This concept has been supported by findings in two recently generated animal models. In addition, the intracellular amyloid-beta accumulation in a distal myopathy with rimmed vacuole mouse model is relevant to similar findings in patients. SUMMARY: Clarifying the role of hyposialylation in distal myopathy with rimmed vacuole/ hereditary inclusion body myopathy could potentially lead to a therapeutic strategy for this progressive myopathy. In addition, strategies aimed at preventing amyloid-beta deposition or enhancing its clearance could also be beneficial, as this epiphenomenon is now known to occur early in the course of the disease.
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Authors | May Christine V Malicdan, Satoru Noguchi, Ichizo Nishino |
Journal | Current opinion in neurology
(Curr Opin Neurol)
Vol. 21
Issue 5
Pg. 596-600
(Oct 2008)
ISSN: 1350-7540 [Print] England |
PMID | 18769255
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Amyloid
- Glycoproteins
- Multienzyme Complexes
- Sialic Acids
- UDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinase
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Topics |
- Amyloid
(metabolism)
- Animals
- Distal Myopathies
(genetics, pathology, physiopathology, therapy)
- Glycoproteins
(metabolism)
- Humans
- Multienzyme Complexes
(genetics, metabolism)
- Myositis, Inclusion Body
(genetics, pathology, physiopathology, therapy)
- Sialic Acids
(metabolism)
- Vacuoles
(metabolism)
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