Immunohistochemical studies show truncated dystrophins in the myotubes of three fetuses at risk for Duchenne muscular dystrophy.

We have performed immunohistochemical studies on muscle tissue of three 12 week old fetuses at risk for DMD, using antisera directed against regions located NH2-proximally and centrally in the rod shaped spectrin-like domain and against the COOH-terminus of dystrophin. All three fetuses had a family history of DMD. Truncated dystrophins were identified in all three cases by a positive reaction with the NH2-proximal antibody, different reactions with the central antibody, and a negative reaction with the COOH-terminal antibody.

Screening of male patients with autosomal recessive Duchenne dystrophy through dystrophin and DNA studies.

Previously we estimated that about 2.5-4% of isolated male patients diagnosed as Duchenne dystrophy (DMD) may have the autosomal recessive form (AR-DMD). Such cases can be distinguished from X-linked DMD through the analysis of dystrophin.

Differentiation of Duchenne and Becker muscular dystrophy phenotypes with amino- and carboxy-terminal antisera specific for dystrophin.

Antibodies directed against the amino- and carboxy-terminal regions of dystrophin have been used to characterize 25 Duchenne muscular dystrophy (DMD), two intermediate, and two Becker muscular dystrophy (BMD) patients. Western blot analysis revealed an altered-size (truncated) immunoreactive dystrophin band in 11 of the 25 DMD patients, in one of the two intermediate patients, and in both BMD patients, when immunostained with antiserum raised against the amino terminus of dystrophin. None of the DMD or intermediate patients demonstrated an immunoreactive dystrophin band when immunostained with an antiserum specific for the carboxy terminus of the protein.

Immunofluorescence dystrophin study in Duchenne dystrophy through the concomitant use of two antibodies directed against the carboxy-terminal and the amino-terminal region of the protein.

Dystrophin immunohistochemical studies in muscle from Duchenne patients (DMD) have shown a population of fibers with partial labelling. In order to determine whether this is related to a cross reaction or to the presence of dystrophin. 22 DMD patients were studied immunohistochemically, through the concomitant use of antibodies from the N-terminal and the C-terminal regions of the protein.

Dystrophin is tightly associated with the sarcolemma of mammalian skeletal muscle fibers.

Sarcolemmal vesicles with right-side-out configuration were prepared from normal fresh human and rabbit skeletal muscle bundles by incubation in 140 mM KCl solution containing collagenase. The vesicles were used to examine the association of dystrophin, the protein product of the Duchenne muscular dystrophy gene, with the sarcolemma. Western blot analysis, indirect immunofluorescence, and immunoperoxidase staining using specific antibodies raised against the N-terminal and the C-terminal domains show that dystrophin remains associated with the membrane of sarcolemmal vesicles.