We recently reported that the dystrophin-associated glycoprotein (DAG) complex is biochemically divided into two subcomplexes: one is the dystroglycan complex comprised of 156DAG and 43DAG and the other is the sarcoglycan complex comprised of 50DAG, A3b, and 35DAG. A3b is a novel dystrophin-associated glycoprotein with an approximate molecular mass of 43 kd but is distinct from 43DAG. In the present study, we examined the striated muscles of the dystrophic hamster with anti-A3b antibody in addition to anti-50DAG, anti-43DAG, anti-35DAG, anti-dystrophin, and anti-laminin antibodies by both immunohistochemistry and immunoblot analysis and found that 50DAG, A3b, and 35DAG are selectively lost. This selective defect of the sarcoglycan complex in dystrophic hamster muscles may give rise to dystrophic changes in striated muscles. Thus, the differentiation of the dystrophin-associated glycoprotein complex into the dystroglycan and sarcoglycan complexes is important not only from a biochemical standpoint but also in understanding the cause of muscular dystrophy in the hamster. Our findings further show that the dystrophic hamster may serve as an animal model for a human disease, severe childhood autosomal recessive muscular dystrophy, which has recently been shown to result from a selective defect in the sarcoglycan complex.