The first reported female patient with the Fukuyama type of congenital muscular dystrophy associated with a lack of C-terminal domain of dystrophin is presented.
By either mechanism the phenotype of congenital muscular dystrophy is believed to be the result of disruption of linkage between the extracellular matrix and the dystrophin glycoprotein complex.
Deficiencies of adhalin in a particular form of limb-girdle muscular dystrophy, and of merosin in a particular form of congenital muscular dystrophy as well as the newly discovered principle of abnormal tri-nucleotide repeats in myotonic dystrophy are evidence of progress that has also amplified the notion of the dystrophinopathies that the protein-deficient muscular dystrophies can now be considered examples of contributions of the dystrophin-glycoprotein complex across the muscle fiber plasma membrane.
Analogous to the putative perturbation of the anchoring function of the dystrophin-associated complex in congenital muscular dystrophy with mutations in the alpha 2-subunit of laminin, our observations suggest a similar mechanism in Bethlem myopathy.