Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies
نویسندگان
چکیده
منابع مشابه
Chimeric protein repair of laminin polymerization ameliorates muscular dystrophy phenotype.
Mutations in laminin α2-subunit (Lmα2, encoded by LAMA2) are linked to approximately 30% of congenital muscular dystrophy cases. Mice with a homozygous mutation in Lama2 (dy2J mice) express a nonpolymerizing form of laminin-211 (Lm211) and are a model for ambulatory-type Lmα2-deficient muscular dystrophy. Here, we developed transgenic dy2J mice with muscle-specific expression of αLNNd, a lamini...
متن کاملBortezomib Does Not Reduce Muscular Dystrophy in the dy2J/dy2J Mouse Model of Laminin α2 Chain-Deficient Muscular Dystrophy
Congenital muscular dystrophy with laminin α2 chain-deficiency, also known as MDC1A, is a severe neuromuscular disorder for which there is no cure. Patients with complete laminin α2 chain-deficiency typically have an early onset disease with a more severe muscle phenotype while patients with residual laminin α2 chain expression usually have a milder disease course. Similar genotype-phenotype co...
متن کاملLoss of basement membrane, receptor and cytoskeletal lattices in a laminin-deficient muscular dystrophy.
Basement membrane laminins bearing the alpha2-subunit interact with alpha-dystroglycan and beta1-integrins, cell-surface receptors that are found within the rectilinear costameric lattices of skeletal muscle sarcolemma. Mutations of the alpha2 subunit are a major cause of congenital muscular dystrophy. To determine whether the costameres are altered as a result of laminin alpha2-mutations, the ...
متن کاملLaminin alpha 2 (merosin)-deficient muscular dystrophy and demyelinating neuropathy in two cats.
We report laminin alpha 2 (merosin) deficiency associated with muscular dystrophy and demyelinating neuropathy in two cats. The cats developed progressive muscle weakness, and atrophy. Either hypotonia or contractures resulted in recumbency, necessitating euthanasia. Muscle biopsies showed dystrophic changes including marked endomysial fibrosis, myofiber necrosis, variability of fiber size, and...
متن کاملLinker molecules between laminins and dystroglycan ameliorate laminin-α2–deficient muscular dystrophy at all disease stages
Mutations in laminin-alpha2 cause a severe congenital muscular dystrophy, called MDC1A. The two main receptors that interact with laminin-alpha2 are dystroglycan and alpha7beta1 integrin. We have previously shown in mouse models for MDC1A that muscle-specific overexpression of a miniaturized form of agrin (mini-agrin), which binds to dystroglycan but not to alpha7beta1 integrin, substantially a...
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ژورنال
عنوان ژورنال: Matrix Biology
سال: 2018
ISSN: 0945-053X
DOI: 10.1016/j.matbio.2017.11.009