Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells CARLA MARQUES * ,† , PAULO PEREIRA † , ALLEN TAYLOR * , JACK N. LIANG ‡ , VENKAT N. REDDY § , LUKE I. SZWEDA || and FU SHANG * ,1 * Jean Mayer USDA Human Nutrition Research Center on Aging, Tufts University, Boston, Massachusetts, USA; † Center of Ophthalmology, IBILI, University of Coimbra, Coimbra, Portugal; ‡ Ophthalmic Research Center, Brigham & Womens Hospital, Harvard University, Boston, Massachusetts, USA; § Department of Ophthalmology and Visual Sciences, Kellogg Eye Center, University of Michigan, Ann Arbor, Michigan, USA; and || Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio, USA 1 Correspondence: Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111, USA. E-mail: fu.shang@tufts.edu <h3>SPECIFIC AIMS</h3> Oxidative stress causes various forms of damage, including protein oxidation, DNA breaks, and lipid peroxidation, to most types of cells. 4-Hydroxynonenal (HNE), generated by peroxidation of polyunsaturated fatty acids, is the most reactive and cytotoxic product of lipid peroxidation. Lysine, histidine, and cysteine residues in proteins and nucleophilic groups in DNA are all potential targets for HNE. HNE-modified proteins have been
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Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells
MARQUES, CARLA; PEREIRA, PAULO; TAYLOR, ALLEN; LIANG, JACK N.; REDDY, VENKAT N.; SZWEDA, LUKE I.; SHANG, FU
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, Volume 18 (12): 1424
Fed of American Socs for Experimental Biology – Sep 1, 2004
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