Muscular dystrophies in mice

Chapman, V.M., Miller, D.R., Armstrong, D., and Caskey, C.T., 1989, Recovery of induced mutations for X chromosome-linked muscular dystrophy in mice, Proc Natl Acad Sci USA, 86, pp 1292-1296. 

W8. Weinstock, I. M., Epstein, S., and Milhorat, A. T., Enzyme studies in muscular dystrophy. Ill, In hereditary muscular dystrophy in mice. Proc. Soc. Exptl. Biol. Med. 99, 272 (1958). 

Smoller, M., and Fineberg, R. A., Studies on myosin in hereditary muscular dystrophy in mice. J. Clin. Invest. 44, 615-622 (1965). 

The last paper of this session, that of Professor Dinning, brought forward the possibility of a completely different function for a-tocopherol. His work is based on the observations in vitamin E deficiency of multi-nucleated cells and a high DNA content of skeletal muscle and bone marrow. The RNA content is also increased, but, at least in rabbit skeletal muscle and monkey bone marrow, to a smaller extent than the DNA content. Studies with labeled precursors of nucleic acid have shown that in vitamin E deficiency there is a greatly increased rate of synthesis of DNA. Interestingly, this is not the case with genetic muscular dystrophy in mice. 

W9. West, W. T., and Murphy, E. D., Histopathology of hereditary, progressive muscular dystrophy in inbred strain 129 mice. Anat. Record 137, 279 (1960). 

Oxidative phosphorylation was found to be normal in muscle mitochondria from dystrophic mice (W18), but low P 0 ratios have been reported in muscular dystrophy in the Syrian hamster (L6). 

M4. Martonosi, A., Sarcoplasmic reticulum. VI. Microsomal Ca " transport in genetic muscular dystrophy of mice. Proc. Soc. Exp. Biol. Med. 127, 824-828 (1968). 

Muscular dystrophy in chickens (16) and mice (17) Renal tubular acidosis (18)... 

Derivatives. The most important derivatives of 1,2,3,4-benzenetetrol are the ubiquinones, eg, coenzyme Q, which are dimethoxytoluquinones with polyisoprenoid side chains (61). They occur in plants and animals. Mice with hereditary muscular dystrophy have a deficiency of coenzyme Q in their heart and hindleg muscles. Therapeutic administration of coenzyme Q [1339-63-5] produces physical improvement and a significandy prolonged lifespan (212). Coenzyme Q also has been used to treat deafness when administered either orally or parenterally (213). 

Wells, D. J., Wells, K. E., Asante, E. A., Turner, G., Sunada, Y., Campbell, K. P., Walsh, F. S., and Dickson, G. (1995). Expression of human full-length and minidystrophin in transgenic mdx mice Implications for gene therapy of Duchenne muscular dystrophy. Hum. Mol. Genet. 4, 1245-1250. 

Sunada, Y., Bernier, S. M., Utani, A., Yamada, Y. and Campbell, K. P. (1995) Identification of a novel mutant transcript of laminin a2 chain gene responsible for muscular dystrophy and dysmyelination in dy2J mice. Hum Mol Genet 4, 1055-1061. 

Bittner, R. E., Anderson, L. V., Burkhardt, E., Bashir, R., Vafiadaki, E., Ivanova, S., et al. (1999) Dysferlin deletion in SJL mice (SJL-Dysf) defines a natural model for limb girdle muscular dystrophy 2B. Nat Genet 23, 141-142. 

Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice. Mol Cell Biol 27, 244-252. 

Buj-Bello, A., Laugel, V., Messaddeq, N., Zahreddine, H., Laporte, J., Pellissier, J. F., et al. (2002) The lipid phosphatase myotubu-larin is essential for skeletal muscle maintenance but not for myogenesis in mice. Proc Natl Acad Sci USA 99, 15060-15065. Sullivan, T., Escalante-Alcalde, D., Bhatt, H., Anver, M., Bhat, N., Nagashima, K., et al. (1999) Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol 147, 913-920. 

Localization of dysbindin-1 near the sarcolemma is not dependent upon its association with a-dystrobrevin or myospryn. Benson et al. (2001) found that sarcolemmal levels of dysbindin-1 are increased in the mdx mouse, an animal model of Duchenne muscular dystrophy. Yet mdx mice also display decreased sarcolemmal levels of a-dystrobrevin (Benson et al., 2001) and myospryn (Reynolds et al., 2008). The sarcolemmal association is more likely due to other known or candidate-binding partners of dysbin-din-1, specifically pallidin, snapin, and rab 11, which are all increased along with dysbindin-1 in mdx muscle (Nazarian et al., 2006). But the increases in pallidin and dysbindin-1 are not related to muscular dystrophy since there are no apparent abnormalities in the muscles or motor behavior of pallid mice (Nazarian et al., 2006), which are deficient in pallidin and dysbindin-1 (Li et al., 2003). 

While most cells do not take up naked DNA in the absence of the physical or chemical treatments described above, muscle cells appear to be an exception. Direct injection of free nucleic acids in saline solutions into skeletal and cardiac muscles has been shown to result in prolonged expression (Wolff et al, 1991 Kitsis et al, 1991). By using this method, the 12 kilobase human dystrophin gene, defective in muscular dystrophy patients, has been introduced into the muscle cells of mice (Partridge, 1991 Ascadi et al, 1991). 

In 1955 the appearance of an inherited mammalian muscular dystrophy was reported in mice of the Bar Harbor 129 strain (M9), in which breeding experiments after ovarian transplantation confirmed its transmission by a single mutant autosomal recessive gene (S32). This disease is analogous to, though not necessarily identical with, human muscular... 

K13. Kruh, J., Dreyfus, J.-C., Schapira, G., and Gey, G. O., Jr., Abnormalities of muscle protein metabolism in mice with muscular dystrophy. ]. Clin. Invest. 39, 1180 (I960). 

Simon, E. J., Cross, C. S., and Lessell, I. M., Turnover of musde and liver proteins in mice with hereditary muscular dystrophy. Arch. Biochem. Biophys. 96, 41 (1962). 

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