Melatonin reprogrammes proteomic profile in light-exposed retina in vivo
Document Type
Article
Publication Date
8-1-2010
Department
Department of Biological Sciences
Abstract
Melatonin, a small organic molecule synthesized by the pineal gland and the retina, has a variety of physiologic functions such as circadian clock pacemaker and antioxidant. Retinal melatonin is down-regulated by light and is barely detectable during the day. The absence of melatonin in the retina during prolonged light exposure may contribute to light-induced retinal degeneration. We sought to investigate the impact of melatonin in the light-exposed retina using proteomic approaches. We exposed mice to either light (250-300lux) for 12h followed by 12h of darkness or the same intensity of continuous light for 7 days. In half of the animals exposed to continuous light, melatonin was injected each night. Proteomic analysis of the retina from these three groups of animals showed that five proteins prominently up-regulated by constant light were down-regulated by melatonin treatment. These five proteins were identified as vimentin, serine/threonine-protein phosphatase 2A, Rab GDP dissociation inhibitor alpha, guanine nucleotide-binding protein Go alpha, and retinaldehyde-binding protein.These five proteins are known to be involved in several cellular processes that may contribute to light-induced retinal degeneration. Identification of melatonin target proteins in our study provides a basis for future studies on melatonin's potential in preventing or treating light-induced retinal degeneration.
Publication Title
International Journal of Biological Macromolecules
Recommended Citation
Zhang, R.,
Hrushesky, W.,
Wood, P.,
Lee, S.,
Hunt, R.,
&
Jahng, W.
(2010).
Melatonin reprogrammes proteomic profile in light-exposed retina in vivo.
International Journal of Biological Macromolecules,
47(2), 255-260.
http://doi.org/10.1016/j.ijbiomac.2010.04.013
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/6513
