Time course of changes in plasma membrane permeability in the dystrophin‐deficient mdx mouse

Control C57BI/10 and mutant, dystrophin‐deficient mdx mice of different ages were used to study the permeability of the plasma membrane to cytosolic components, to a vital stain (procion orange) and to extra‐cellular 45calcium. Prenecrotic, 14 ± 2‐day‐old mdx mice had normal serum activities of creatine kinase (CK) and pyruvate kinase (PK). Muscles from these animals also had no increased permeability to procion orange or extracellular 45calcium. Serum activities of CK and PK had risen acutely in the 21‐day‐old mdx mouse compared with control and remained elevated up to 6 months of age. The influx of procion orange and 45calcium content were abnormally elevated in the 40 ± 4‐day‐old mdx mouse. These data provide no evidence for an increase in muscle plasma membrane permeability as a primary pathogenic effect of a lack of dystrophin, but results suggest that some factor expressed or deexpressed during mouse development may be necessary for the full expression of the dystrophic process. © 1994 John Wiley & Sons, Inc.

[1]  R. Edwards,et al.  Release of creatine kinase and prostaglandin E2 from regenerating skeletal muscle fibers. , 1994, Journal of applied physiology.

[2]  Y. Hayashi,et al.  Dystrophin-associated glycoprotein and dystrophin co-localisation at sarcolemma in Fukuyama congenital muscular dystrophy , 1993, The Lancet.

[3]  S. Head.  Membrane potential, resting calcium and calcium transients in isolated muscle fibres from normal and dystrophic mice. , 1993, The Journal of physiology.

[4]  L. Kunkel,et al.  The structural and functional diversity of dystrophin , 1993, Nature Genetics.

[5]  J. Ervasti,et al.  Dystrophin-associated glycoproteins: their possible roles in the pathogenesis of Duchenne muscular dystrophy. , 1993, Molecular and cell biology of human diseases series.

[6]  K. Davies,et al.  Primary structure of dystrophin-related protein , 1992, Nature.

[7]  J. Ervasti,et al.  Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle , 1992, Nature.

[8]  K. Campbell,et al.  Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy , 1992, Nature.

[9]  F. Gros,et al.  Modulation of embryonic and muscle-specific enolase gene products in the developing mouse hindlimb. , 1992, Differentiation; research in biological diversity.

[10]  R. Edwards,et al.  Accumulation of calcium by normal and dystrophin-deficient mouse muscle during contractile activity in vitro. , 1992, Clinical science.

[11]  Simon C Watkins,et al.  Immunolocalization and developmental expression of dystrophin related protein in skeletal muscle , 1991, Neuromuscular Disorders.

[12]  W. Denetclaw,et al.  Increased calcium influx in dystrophic muscle , 1991, The Journal of cell biology.

[13]  K. Davies,et al.  Localization of the DMDL gene-encoded dystrophin-related protein using a panel of nineteen monoclonal antibodies: presence at neuromuscular junctions, in the sarcolemma of dystrophic skeletal muscle, in vascular and other smooth muscles, and in proliferating brain cell lines , 1991, The Journal of cell biology.

[14]  K. Campbell,et al.  Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice , 1991, The Journal of cell biology.

[15]  J. Ervasti,et al.  Membrane organization of the dystrophin-glycoprotein complex , 1991, Cell.

[16]  J. Ervasti,et al.  Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle , 1991, Neuron.

[17]  D. Jones,et al.  Muscle damage in mdx mice , 1991, Nature.

[18]  R. Edwards,et al.  Effects of contractile activity on muscle damage in the dystrophin-deficient mdx mouse. , 1991, Clinical science.

[19]  H. Jockusch,et al.  Decreased osmotic stability of dystrophin-less muscle cells from the mdx mouse , 1991, Nature.

[20]  M. Brooke,et al.  Creatine kinase and prostaglandin E, release from isolated Duchenne muscle , 1991, Neurology.

[21]  R. Hodges,et al.  Dystrophin is tightly associated with the sarcolemma of mammalian skeletal muscle fibers. , 1991, Experimental cell research.

[22]  J. Lansman,et al.  Calcium entry through stretch-inactivated ion channels in mdx myotubes , 1990, Nature.

[23]  R. Steinhardt,et al.  Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice , 1988, Nature.

[24]  Simon C Watkins,et al.  Immunoelectron microscopic localization of dystrophin in myofibres , 1988, Nature.

[25]  A. Monaco,et al.  The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein , 1988, Cell.

[26]  Eric P. Hoffman,et al.  Dystrophin: The protein product of the duchenne muscular dystrophy locus , 1987, Cell.

[27]  A. Monaco,et al.  Detection of deletions spanning the Duchenne muscular dystrophy locus using a tightly linked DNA segment , 1985, Nature.

[28]  D. Jones,et al.  Release of intracellular enzymes from an isolated mammalian skeletal muscle preparation. , 1983, Clinical science.

[29]  L. Rowland.  Biochemistry of muscle membranes in Duchenne muscular dystrophy , 1980, Muscle & nerve.

[30]  J. Bodensteiner,et al.  Intracellular calcium accumulation in Duchenne dystrophy and other myopathies , 1978, Neurology.