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Proteomic Analysis of Nitrated and 4-Hydroxy-2-Nonenal–Modified Serum Proteins During Aging

¹ Research Institute of Genetic Engineering, ² College of Pharmacy, and ³ Longevity Life Science and Technology Institute, Aging Tissue Bank, Pusan National University, Busan, Korea.
⁴ University of Texas Health Science Center at San Antonio.

Address correspondence to Hae Young Chung, PhD, College of Pharmacy, Pusan National University, 30 Jangjeon-dong, Geumjeong-gu, Busan 609-735, Korea. E-mail: hyjung{at}pusan.ac.kr

Using proteomic techniques, we investigated peroxynitrite (ONOO^–) and 4-hydroxy-2-nonenal (HNE) modified serum proteins from young and old Fischer 344 rats. Two-dimensional gel electrophoresis/western blot analysis of nitrotyrosine and HNE–histidine revealed that serum proteins were differentially modified by ONOO^– and HNE. Among them, 16 of the modified proteins, identified by matrix-assisted laser desorption/ionization–time of flight mass spectrometry (MALDI-TOF MS), are involved in blood coagulation, lipid transport, blood pressure regulation, and protease inhibition. Furthermore, nitration and HNE adduction were found to increase with age, lending support to the oxidative stress hypothesis of aging. Our data showed that proteomic techniques can be valuable tools in the study of protein profiling modifications during aging.