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This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M900203-MCP200v1 8/10/2201    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Google Scholar Articles by Alcazar, O. Articles by Marin-Castano, M. E. PubMed PubMed Citation Articles by Alcazar, O. Articles by Marin-Castano, M. E. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 8:2201-2211, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteomics Characterization of Cell Membrane Blebs in Human Retinal Pigment Epithelium Cells^*,

Oscar Alcazar, Adam M. Hawkridge, Timothy S. Collier, Scott W. Cousins^¶, Sanjoy K. Bhattacharya^,||, David C. Muddiman and Maria E. Marin-Castano^,**

From the Bascom Palmer Eye Institute, University of Miami, Miami, Florida 33136,
W. M. Keck FT-ICR Mass Spectrometry Laboratory, Department of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, and
¶Duke Center for Macular Diseases, Duke University, Durham, North Carolina 27710

Age-related macular degeneration (AMD) is the leading cause of legal blindness among the elderly population in the industrialized world, affecting about 14 million people in the United States alone. Smoking is a major environmental risk factor for AMD, and hydroquinone is a major component in cigarette smoke. Hydroquinone induces the formation of cell membrane blebs in human retinal pigment epithelium (RPE). Blebs may accumulate and eventually contribute first to sub-RPE deposits and then drusen formation, which is a prominent histopathologic feature in eyes with AMD. As an attempt to better understand the mechanisms involved in early AMD, we sought to investigate the proteomic profile of RPE blebs. Isolated blebs were subjected to SDS-PAGE fractionation, and in-gel trypsin-digested peptides were analyzed by LC-MS/MS that lead to the identification of a total of 314 proteins. Identified proteins were predominantly involved in oxidative phosphorylation, cell junction, focal adhesion, cytoskeleton regulation, and immunogenic processes. Importantly basigin and matrix metalloproteinase-14, key proteins involved in extracellular matrix remodeling, were identified in RPE blebs and shown to be more prevalent in AMD patients. Altogether our findings suggest, for the first time, the potential involvement of RPE blebs in eye disease and shed light on the implication of cell-derived microvesicles in human pathology.

** To whom correspondence may be addressed:Center for Molecular Ophthalmology, Bascom Palmer Eye Inst., University of Miami, 1638 N. W. 10th Ave., Miami, FL 33136. Tel.:305-547-3660; E-mail:MCastano{at}med.miami.edu.

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