DYSTROPHIN, 3 YEARS AFTER ITS DISCOVERY

We present the general features of the dystrophin molecule and the main immunological tools used for its study. The initial hypotheses on its structural arrangement in 4 different domains have now received experimental support [6]. Some residues of the N-terminal domain interacts with actin [25]. The long central domain has different discontinous, protease-sensitive areas [26]. Dystrophin molecules present the same capacity of self-association in oligomeric structures as other cytoskeletal proteins of the spectrin superfamily [16]. The C-terminal domain is arranged close to the cytoplasmic internal face of plasma membranes [32] and interacts with a few membrane integral glycoproteins [36]. Dystrophin molecules form a complex interconnecting meshwork essential to muscle cell function. Different dystrophin isoforms and/or dystrophin related proteins (DRP) are either exclusively expressed or co-expressed in different muscles or tissues like brain and liver... These isoproteins are issued from different transcripts either from genes located on at least two different chromosomes (X and 6), or through alternative splicing. The progressive development of monoclonal antibodies specific to the different dystrophin isoforms could enable more informative immunodiagnoses of the dystrophin deficiency in Duchenne and Becker patients.