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Mol Cells. 2013 Jun;35(6):533-42. doi: 10.1007/s10059-013-0058-1. Epub 2013 May 14.

Comparative proteomic analysis of cysteine oxidation in colorectal cancer patients.

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  • 1Department of Oral Biochemistry, Dental Science Research Institute and the Brain Korea 21 Project, Medical Research Center for Biomineralization Disorders, School of Dentistry, Chonnam National University, Hwasun, Korea.

Abstract

Oxidative stress promotes damage to cellular proteins, lipids, membranes and DNA, and plays a key role in the development of cancer. Reactive oxygen species disrupt redox homeostasis and promote tumor formation by initiating aberrant activation of signaling pathways that lead to tumorigenesis. We used shotgun proteomics to identify proteins containing oxidation-sensitive cysteines in tissue specimens from colorectal cancer patients. We then compared the patterns of cysteine oxidation in the membrane fractions between the tumor and non-tumor tissues. Using nano-UPLC-MS(E) proteomics, we identified 31 proteins containing 37 oxidation-sensitive cysteines. These proteins were observed with IAM-binding cysteines in non-tumoral region more than tumoral region of CRC patients. Then using the Ingenuity pathway program, we evaluated the cellular canonical networks connecting those proteins. Within the networks, proteins with multiple connections were related with organ morphology, cellular metabolism, and various disorders. We have thus identified networks of proteins whose redox status is altered by oxidative stress, perhaps leading to changes in cellular functionality that promotes tumorigenesis.

PMID:
23677378
[PubMed - indexed for MEDLINE]
PMCID:
PMC3887873
Free PMC Article
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