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KMID : 1023620120360010055
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Reproductive and Developmental Biology
2012 Volume.36 No. 1 p.55 ~ p.64
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Proteomic Analysis of the Increased Proteins in Peroxiredoxin ⅡDeficient RBCs
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Yang Hee-Young
Lee Tae-Hoon
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Abstract
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Peroxiredoxin Ⅱ (Prdx Ⅱ; a typical 2-Cys Prdx) has been originally isolated from erythrocytes, and its structure and peroxidase activity have been adequately studied. Prdx Ⅱ has been reported to protect a wide range of cellular environments as antioxidant enzyme, and its dysfunctions may be implicated in a variety of disease states associated with oxidative stress, including cancer and aging-associated pathologies. But, the precise mechanism is still obscure in various aspects of aging containing ovarian aging. Identification and relative quantification of the increased proteins affected by Prdx Ⅱ deficiency may help identify novel signaling mechanisms that are important for oxidative stress-related diseases. To identify the increased proteins in Prdx Ⅱ?/? mice, we performed RBC comparative roteome analysis in membrane fraction and cytosolic fractions by nano-UPLC-MS E shotgun proteomics. We found the increased 86 proteins in membrane (32 proteins) and cytosolic (54 proteins) fractions, and analyzed comparative expression pattern in healthy RBCs of Prdx Ⅱ+/+ mice, healthy RBCs of Prdx Ⅱ?/? mice, and abnormal RBCs of Prdx Ⅱ ?/? mice. These proteins belonged to cellular functions related with RBC lifespan maintain, such as cellular morphology and assembly, cell-cell interaction, metabolism, and stress-induced signaling. Moreover, protein networks among the creased proteins were analyzed to associate with various diseases. Taken together, RBC proteome may provide clues to understand the clue about redox-imbalanced diseases.
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KEYWORD
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Peroxiredoxin Ⅱ, Red blood cell, Shotgun proteomics, Canonical pathway
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