Differential Retinal Protein Expressions During form Deprivation Myopia in Albino Guinea Pigs
Chi Ho To,
Rachel K.M. Chun,
Jessica F.J. Yu,
Thomas C. Lam.
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.
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