Molecular diversity of the dystrophin-like protein complex in the developing and adult avian retina.

Mutations in dystrophin cause muscular dystrophy but also affect the CNS, including information processing in the retina. To better understand the molecular basis of these CNS deficits, we analyzed the molecular composition and developmental appearance of dystrophin and of the dystrophin-associated protein complex (DPC) in the embryonic and adult avian retina. We detected a concentration of the DPC at the vitreal border and in the outer plexiform layer of the adult retina. At both locations the complex had a different molecular composition and different developmental expression pattern. At the vitreal border, the complex was composed of utrophin, alpha-dystrobrevin-1, and dystroglycan, and was present at all stages of retinal development even before neurogenesis and gliogenesis. On the other hand, the complex in the outer plexiform layer consisted of dystrophin, beta-dystrobrevin and dystroglycan. The distribution of this complex changed from a diffusely distributed to an aggregated form during development concomitant with synapse formation in the outer plexiform layer. Solubilization of the retinal extracellular matrix by intravitreal injection of collagenase resulted in a redistribution of the complex at the retinal vitreal border but had no influence on the distribution of the dystrophin-associated proteins in the outer plexiform layer. These results demonstrate two types of dystrophin-like complexes in the chick retina with differential molecular compositions, different anchorage to the extracellular matrix, and different developmental expression patterns, suggesting distinct functions for the DPC at both locations.