Analysis of Protein Redox Modification by Hypoxia

Abstract

We examined hypoxia‐induced changes in global thiol proteome profile in human prostate cancer cells using a BIAM‐based display method. We analyzed the kinetics of protein thiol modification by using a pattern recognition algorithm, self‐organizing maps (SOM) clustering, and identified the BIAM‐labeled proteins by MALDI‐TOF and ESI‐tandem mass spectrometry. We found 99 out of 215 of total BIAM‐labeled proteins were affected by hypoxia treatment and, yet, with diverse patterns and kinetics of redox modification. Our study proved that proteomics analysis employing the BIAM‐labeling method can provide valuable information pertaining to global changes in the redox status of proteins in response to hypoxia.

Keywords:

• Hypoxia
• Oxidative stress
• Redox modification
• Proteomics

Acknowledgments

This work was supported by NIH CA109480, CA111846, CA09796, U.S. Army PC050127, and Korea Health 21 R & D project 01-PJ3-PG6-01GN07, Korea Ministry of Science and Technology KOSEF R11-2005-017.