Abstract: Proteomic analysis is a powerful tool to reveal the mechanisMOf functional changes of central nervous system and the origination, development and prognosis of central nervous disease. Human brain proteins were isolated from human occipital lobes at five ages from 23 to 94 years old, and separated by two dimensional gel electrophoresis. Over one thousand protein spots were resolved in one gel with commassie brilliant blue staining. Differential expression of proteins with increasing ages was analyzed by Image Master 2D Elite software processing. Seven protein spots were found to increase or decrease with increasing ages consistently. Taking advantage of the high sensitivity and accuracy of mass spectrometry, 11 proteins with significant changes were identified by peptide fingerprinting map(PMF) or peptide sequence tag(PST) obtained from MS or tandem MS(MS/MS). Among the identified proteins, the amount of 5 proteins were increased or decreased consistently, including neurofilament triplet Lprotein(NF-L), a protein involved in the maintenance of neuronal caliber; peroxiredoxin(EC 1.11.1.), an antioxidant enzyme; aconitate hydratase(EC 4.2.1.3), a key enzyme in tricarboxylic acid(TCA) cycle; enolase 2(EC 4.2.1.11), a key enzyme in glycolysis pathway; T-complex protein 1, a chaperone. In summary, the two dimensional map of human brain occipital lobe proteins was firstly established, significantly changed proteins during the course of aging were identified and their possible biological significance was discussed.

Key words: Proteome, 2D-PAGE, Mass spectrometry, Human brain occipital lobes, Aging