Abstract
The molecular mechanisms that cause myopia are largely unknown. However, signaling pathways originating in the retina are implicated in regulating refractive development. The study of retinal protein expression profiles ("proteomics") in animal eyes is a powerful approach to unraveling these molecular mechanisms. Previously, we used this proteomics approach in the chick model to identify a number of proteins whose expression was either up or down regulated during myopia development, compared to untreated contralateral "control" eyes. In order to search for mechanisms conserved between animal species, here we applied proteomic techniques to study retinal protein changes induced by form deprivation using the mammalian albino guinea pig model. We identified 8 differentially expressed retinal proteins in myopic eyes: Significant increases in protein levels were found in myopic eyes for Septin-6, Fascin-1, Collapsin response mediator protein, Preproalbumin precursor, Succinate dehydrogenase complex subunit A and Vimentin; whereas protein levels were found to be decreased for β-soluble NSF attachment protein and Phosphoglycerate mutase 1. Four of these proteins (Septin-6, Collapsin response mediator protein and Phosphoglycerate mutase 1 and Vimentin) were found previously to be differentially expressed – in the same direction – in the retina of chicks developing lens-induced myopia, thus providing independent replication of their differential abundance in myopia, and the conservation of molecular changes in the myopic retina between birds and mammals, as well as across myopia-inducing paradigms. The eight differentially expressed proteins identified here are potential candidates with roles in the regulation of myopic eye growth.
Keywords: Formdeprivation myopia, guinea pigs, mass spectrometry, proteomics, retina, two-dimensional gel electrophoresis.