Analysis of protein redox modification by hypoxia

Kyoung Soo Choi; Soo Yeon Park; Sun Hee Baek; Rama Dey-Rao; Young Mee Park; Haitao Zhang; Clement Ip; Eun Mi Park; Hong Kim Yeul; Hoon Park Jong

doi:10.1080/10826060500388520

Analysis of protein redox modification by hypoxia

Kyoung Soo Choi
, Soo Yeon Park
, Sun Hee Baek
, Rama Dey-Rao
, Young Mee Park
, Haitao Zhang
, Clement Ip
, Eun Mi Park
, Hong Kim Yeul
, Hoon Park Jong

Microbiology and Immunology

Roswell Park Cancer Institute
Incheon National University
Korea University
Sookmyung Women's University

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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.

Original language	English
Pages (from-to)	65-79
Number of pages	15
Journal	Preparative Biochemistry and Biotechnology
Volume	36
Issue number	1
DOIs	https://doi.org/10.1080/10826060500388520
State	Published - Feb 1 2006

Keywords

Hypoxia
Oxidative stress
Proteomics
Redox modification

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10.1080/10826060500388520

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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, Proteomics, Redox modification",

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AU - Choi, Kyoung Soo

AU - Park, Soo Yeon

AU - Baek, Sun Hee

AU - Dey-Rao, Rama

AU - Park, Young Mee

AU - Zhang, Haitao

AU - Ip, Clement

AU - Park, Eun Mi

AU - Yeul, Hong Kim

AU - Jong, Hoon Park

PY - 2006/2/1

Y1 - 2006/2/1

N2 - 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.

AB - 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.

KW - Hypoxia

KW - Oxidative stress

KW - Proteomics

KW - Redox modification

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DO - 10.1080/10826060500388520

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AN - SCOPUS:31544469548

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VL - 36

SP - 65

EP - 79

JO - Preparative Biochemistry and Biotechnology

JF - Preparative Biochemistry and Biotechnology

IS - 1

ER -

Analysis of protein redox modification by hypoxia

Abstract

Keywords

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