Abstract
Purpose: :
This study aims at the distribution changes of rhodopsin, rhodopsin-kinase, caveolin-1 and cSrc-kinase during retinal development.
Methods: :
Syrian hamster retinas were used in various ages: 1-15 weeks young and adult. The newborn hamster’s retina is immature and has a special structure. The maturation of the retina is continuous in the following days. The eyes open on the 14th day, when the structure of the retina is similar to the adult. The changes in protein distribution were followed by immunocytochemistry with specific antibodies. Double-label immunocytochemistry and immunoprecipitation were used to prove the colocalization of the observed proteins.
Results: :
The localization of caveolin-1, cSrc-kinase, rhodopsin-kinase and rhodopsin shows a similar pattern during the development. The distribution of these molecules changes simultaneously with the eye opening and the initiation of visual function. Rhodopsin co-localizes and co-immunprecipitates with the other three proteins.
Conclusions: :
The expression and distribution of the examined phototransduction proteins change during the development of the retina. The synthesis is carried out in the cell body and the proteins are transported to the outer segment, where the phototransduction takes place. These molecules seem to be arranged together not only at the place of the synthesis, but also within the intracellular transport path. Since caveolin-1 and cSrc-kinase, well-known components of lipid rafts, are also associated with this complex, presumably these molecules are inserted in common lipid rafts. Caveolin-1 is known as an organizer protein in polarized transport, thus, caveolin-1 may be modulator in the transport of the phototransduction components to the outer segments. The latter protein probably also has an important function in the regulation of phototransduction.
Keywords: retina • development • photoreceptors