Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima Fatty (OLETF) rat.
Oxidative stress is implicated in a broad variety of chronic and acute diseases, including such age-related diseases as diabetes. To understand at the protein level cellular damage caused by the stress, we developed a proteomic method, in which protein carbonyls were derivatized with biotin hydrazide followed by two-dimensional gel electrophoresis. The method, being capable of analyzing high-molecular-mass proteins as large as myosin heavy chains (molecular mass approximately 200 kDa), was applied to detecting protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima Fatty (OLETF) rat and a control Long-Evans Tokushima Otsuka (LETO) rat. A number of proteins, including mitochondrial ATP synthase beta-chain, desmin, actin, and myosin, were found carbonylated. Our method would provide a means toward clarifying a comprehensive view of oxidative modifications of proteins during a long progression of age-related diseases and understanding the mechanism of the onset, progression, and complication of the diseases.
Oh-Ishi
Masamichi
M
Department of Physics, Kitasato University School of Science, Sagamihara-shi, Kanagawa, Japan. oishi@walrus.sci.kitasato-u.ac.jp
Ueno
Takeshi
T
Maeda
Tadakazu
T
D000818:Animals; D015153:Blotting, Western; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D005609:Free Radicals; D008297:Male; D009124:Muscle Proteins / Q000378:metabolism; D018384:Oxidative Stress; D020543:Proteome; D051381:Rats
D005609:Free Radicals; D009124:Muscle Proteins; D020543:Proteome