Department of Cell & Neurobiology
Department of Ophthalmology
Zilkha Neurogenetic Institute
Keck School of Medicine of USC
- Signal transduction
- Photoreceptor function
- Retinal degeneration
Research OverviewPhotoreceptor cells are light sensitive neurons in the retina that initiate the first step in vision. These cells initiate an intracellular G-protein cascade to amplify the signal generated following photon absorption. One of the main objectives of my laboratory is to understand how this signaling cascade is regulated within rod and cone photoreceptor cells which underlies their specialized ability to detect dim light and bright light, respectively. Another aspect of these studies is to understand how defects in signaling and protein mis-expression results in retinal degeneration. We utilize a multidisciplinary approach in our studies, combining transgenic mouse technology with electrophysiologic, morphologic and biochemical analyses.
Protein misfolding is an underlying cause of many neurodegenerative diseases. These diseases are characterized by insoluble protein aggregates and lipid deposits within amyloid plaques of diseased tissue. Drusen is an extracellular deposit commonly present in aging eyes and eyes affected with age related macular degeneration (AMD). Another goal of my laboratory is to understand how protein misfolding may participate in the etiology of AMD.
- Mailing Address:
- Zilkha Neurogenetic Institute
1501 San Pablo Street, ZNI-227
Los Angeles, CA 90089-2821
- Office Location:
- Office Phone:
- (323) 442-4479
- Lab Location:
- Lab Phone:
- (323) 442-4359
- (323) 442-4433
- B.A., Occidental College, 1983.
- Ph.D. USC, 1990.
- Post-Doctoral Scholar, Caltech, 1995.
Concepcion F, Chen J. (2010) Q344ter mutation causes mislocalization of rhodopsin moleculesthat are catalytically active: a mouse model of Q344ter-induced retinal degendration. PLoS One 5(6):e10904
Isas JM, Luibl V, Johnson LV, Kayed R, Wetzel R, Glabe CG, Langen R, Chen J. (2010) Soluble and mature amyloid fibrils in drusen deposits. Invest Ophthalmol Vis Sci. 51(3):1304-10. -PubMed
Chen J, Woodruff ML, Wang T, Concepcion F, Tranchina D, Fain GL. (2010) Channel modulation and the mechanism of light adaptation in mouse rods. J Neurosci. 30:16232-16240. -PubMed
Chen J, Mao, W. (2010) G protein alpha transducin, cone. UCSD-Nature Molecule Pages. doi:10.1038/mp.a000980.01
Shin TM, Isas JM, Hsieh CL, Keyed R, Glabe CG, Langen R, Chen J. (2008) Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin, Mol Neurodegener. 3:16. -PubMed
Shi G, Yau KW, Chen J, Kefalov VJ. (2007) Signaling properties of a short-wave cone visual pigment and its role in phototransduction. J Neurosci. 27(38):10084-10093. -PubMed
Doan, T., Mendez, A., Detwiler, P.B., Chen, J. and Rieke, F. (2006) Multiple phosphorylation sites confer reproducibility of the rod's single photon response. Science. 313:530-533. -PubMed
Burns ME, Mendez A, Chen CK, Almuete A, Quillinan N, Simon MI, Baylor DA, Chen J. (2006) Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants. J Neurosci. 26(3):1036-44. -PubMed
Luibl V, Isas JM, Kayed R, Glabe CG, Langen R, Chen J. (2006) Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers. J Clin Invest. 116(2):378-85. -PubMed
Chen,J., Shi, G., Concepcion, F. A., Xie, G., Oprian, D., Chen, J. (2006) Stable rhodopsin/arrestin complex leads to retinal degeneration in a transgenic mouse model of ADRP. J. Neurosci. 26:11929-37. -PubMed