Proteomic analysis of post-mitochondrial fractions of young and old rat kidney.

Abstract:

:Proteomic analysis is defined as the characterization of the entire set of proteins encoded by a genome. Two-dimensional (2D) electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) are key technologies used in proteomic analysis to gain information about protein expression profiles and post-translational modifications. Knowledge about aging processes can be gained by recognizing changes in protein expression. Thus, to better understand the aging process through protein profiling, post-mitochondrial (PM) fractions of young (13-month) and old (31-month) male Fischer 344 rat kidney were differentially analyzed by 2D. We detected a total number of 380 spots on 2D gel images. Among them, 167 spots showed 2-fold significant alterations (p<0.05) between young and old PM fractions. Further, 103 proteins were identified by MALDI-TOF MS. The PM fraction of aged rat kidney showed increases in antioxidative and proteolytic proteins and decreases in cytoskeletal proteins. In addition, we found age-related changes in transport and homeostasis proteins. Thus, our results demonstrated that proteomic analysis can be effectively applied to the assessment of the age status of protein expression, and thereby provide valuable information on age-related changes of proteome.

journal_name

Exp Gerontol

journal_title

Experimental gerontology

authors

Kim CH,Park DU,Chung AS,Zou Y,Jung KJ,Sung BK,Yu BP,Chung HY

doi

10.1016/j.exger.2004.04.003

keywords:

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

1155-68

issue

8

eissn

0531-5565

issn

1873-6815

pii

S0531556504001731

journal_volume

39

pub_type

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