An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy
- Kazuhiro Kobayashi, Y. Nakahori, T. Toda
- Biology, MedicineNature
- 23 July 1998
There is a retrotransposal insertion of tandemly repeated sequences within this candidate-gene interval in all FCMD chromosomes carrying the founder haplotype (87%).
Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
- K. Matsumura, J. Ervasti, K. Ohlendieck, S. Kahl, K. Campbell
- Biology, MedicineNature
- 10 December 1992
The results could provide a basis for the upregulation of DRP as a potential therapeutic approach in Duchenne muscular dystrophy and mdx muscle.
Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle
- K. Ohlendieck, J. Ervasti, K. Matsumura, S. Kahl, C. Leveille, K. Campbell
- BiologyNeuron
- 1 September 1991
Dystrophin–glycoprotein complex: Its role in the molecular pathogenesis of muscular dystrophies
- K. Matsumura, K. Campbell
- Medicine, BiologyMuscle and Nerve
- 1 January 1994
These recent developments in the research concerning the function of the dystrophin–glycoprotein complex pave a way for the better understanding of the pathogenesis of muscular dyStrophies.
Characterization of the Transmembrane Molecular Architecture of the Dystroglycan Complex in Schwann Cells*
- F. Saito, T. Masaki, K. Matsumura
- BiologyJournal of Biological Chemistry
- 19 March 1999
The results indicate 1) that Dp116 is a component of the submembranous cytoskeletal system that anchors the dystroglycan complex in Schwann cells, and 2) that this fragility may be attributable to the absence of the sarcoglycan complex.
Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin.
- A. Chiba, K. Matsumura, T. Endo
- Biology, ChemistryJournal of Biological Chemistry
- 1997
The major sialylated O-glycosidically-linked oligosaccharide of the alpha-dystroglycan was a novel O-mannosyl-type oligosACcharide, the structure of which was Siaalpha2-3Gal beta1-4GlcNAcbeta1-2Man-Ser/Thr (where Sia is sialic acid).
Fukutin is required for maintenance of muscle integrity, cortical histiogenesis and normal eye development.
It is reported that chimeric mice generated using embryonic stem cells targeted for both fukutin alleles develop severe muscular dystrophy, with the selective deficiency of alpha-dystroglycan and its laminin-binding activity.
Structures of Sialylated O-Linked Oligosaccharides of Bovine Peripheral Nerve α-Dystroglycan
- A. Chiba, K. Matsumura, T. Endo
- Biology, ChemistryJournal of Biological Chemistry
- 24 January 1997
The major sialylated O-glycosidically-linked oligosaccharide of the α-dystroglycan was a novel O-mannosyl-type oligosACcharide, the structure of which was Siaα2-3Gal β1-4GlcNAcβ1-2Man-Ser/Thr (where Sia is sialic acid).
Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex.
- H. Yamada, F. Saito, K. Matsumura
- BiologyHuman Molecular Genetics
- 15 July 2001
The results indicate that the processing of beta-dystroglycan by MMP causes the disruption of the link between the ECM and cell membrane via the dystroglcan complex, which could have profound effects on cell viability.
LARGE glycans on dystroglycan function as a tunable matrix scaffold to prevent dystrophy
- M. Goddeeris, Biming Wu, K. Campbell
- BiologyNature
- 16 October 2013
The results reveal that the LARGE-glycan of dystroglycan serves as a tunable extracellular matrix protein scaffold, the extension of which is required for normal skeletal muscle function.
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