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

Department of Biomedical Sciences

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

11 Citations (Scopus)

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
Publication status	Published - 2006 Feb 1

Keywords

Hypoxia
Oxidative stress
Proteomics
Redox modification

ASJC Scopus subject areas

Biotechnology
Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1080/10826060500388520

Cite this

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title = "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, Proteomics, Redox modification",

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

note = "Funding Information: 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.",

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doi = "10.1080/10826060500388520",

language = "English",

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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

N1 - Funding Information: 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.

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

UR - http://www.scopus.com/inward/record.url?scp=31544469548&partnerID=8YFLogxK

U2 - 10.1080/10826060500388520

DO - 10.1080/10826060500388520

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AN - SCOPUS:31544469548

SN - 1082-6068

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

ASJC Scopus subject areas

UN SDGs

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