Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle
Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates...
Gespeichert in:
Veröffentlicht in: | Free radical research 2003-06, Vol.37 (6), p.621-630 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 630 |
---|---|
container_issue | 6 |
container_start_page | 621 |
container_title | Free radical research |
container_volume | 37 |
creator | Wang, Hong P. Schafer, Freya Q. Goswami, Prabhat C. Oberley, Larry W. Buettner, Garry R. |
description | Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r=0.95). The higher the PhGPx activity, the lower the plating efficiency (r=-0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by >60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth. |
doi_str_mv | 10.1080/1071576031000088283 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4638222</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73468737</sourcerecordid><originalsourceid>FETCH-LOGICAL-i286t-c24c2733b629231cef11b9f327eaf4efbeacc664dce7b507dc6994738bf4fbe33</originalsourceid><addsrcrecordid>eNp9kctu1TAQhi0Eohd4AiTkFbsU307sLEBCBzitVKldlAUry3HGxJWPHewEyNvjqoW2EsKbsTz_fDOeH6FXlJxQoshbSiTdyJZwSupRiin-BB1SwrqGCUme3twlbaqEHaCjUq4JoVxs5HN0QJlqlVDdIfp6OaYyjSn4yQ_4dB1ymiCnX34AvAvLbObRpwj48vbRFMBncVgsFGzwRwhmxT7iHcXJ4XkEvIUQ8Ha1AV6gZ86EAi_v4jH68vnT1fa0Ob_YnW0_nDe-DjE3lgnLJOd9yzrGqQVHad85ziQYJ8D1YKxtWzFYkP2GyMG2XSckV70TNcn5MXp_y52Wfg9VFudsgp6y35u86mS8fpyJftTf0g8tWq4YYxXw5g6Q0_cFyqz3vtj6DxMhLUVLLloluazC1w87_W3xZ5v3o_joUt6bnymHQc9mDSm7bKL1RVe39I19-h_2VcC7R4ARTJhHazLo67TkWPeo_1f_G-Gtn9M</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>73468737</pqid></control><display><type>article</type><title>Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle</title><source>MEDLINE</source><source>Taylor & Francis:Master (3349 titles)</source><creator>Wang, Hong P. ; Schafer, Freya Q. ; Goswami, Prabhat C. ; Oberley, Larry W. ; Buettner, Garry R.</creator><creatorcontrib>Wang, Hong P. ; Schafer, Freya Q. ; Goswami, Prabhat C. ; Oberley, Larry W. ; Buettner, Garry R.</creatorcontrib><description>Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r=0.95). The higher the PhGPx activity, the lower the plating efficiency (r=-0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by >60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth.</description><identifier>ISSN: 1071-5762</identifier><identifier>EISSN: 1029-2470</identifier><identifier>DOI: 10.1080/1071576031000088283</identifier><identifier>PMID: 12868489</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Antioxidant enzymes ; Antioxidants - metabolism ; Blotting, Western ; BrdU, bromodeoxyuridine ; Bromodeoxyuridine - pharmacology ; CAT, catalase ; Catalase - metabolism ; Cell Cycle ; Cell Differentiation ; Cell Line, Tumor ; CuZnSOD, copper zinc superoxide dismutase ; EDTA, disodium ethylenediaminetetraacetic acid ; EtOH, ethanol ; Flow Cytometry ; G1 Phase ; Glutathione - metabolism ; Glutathione peroxidase ; Glutathione Peroxidase - metabolism ; Glutathione Reductase - metabolism ; GPx-1, cytosolic glutathione peroxidase ; GR, glutathione reductase ; GSH, glutathione ; GSSG, glutathione disulfide ; HO, hydrogen peroxide ; Humans ; Immunoblotting ; L-PhGPx, mitochondrial phospholipid hydroperoxide glutathione peroxidase ; Lipid hydroperoxide ; Lipid Metabolism ; Lipid Peroxides - metabolism ; LOH, lipid alcohol ; LOOHs, lipid hydroperoxides ; MCF-7, human breast carcinoma cells ; MnSOD, manganese superoxide dismutase ; Models, Chemical ; Neo, MCF-7 cells with empty vector ; Oxidation-Reduction ; P-1, P-2, P-3, P-4, are MCF-7 clones stably transfected with PhGPx ; PBS, phosphate buffered saline ; PE, plating efficiency ; PI, propidium iodide ; PLOOH, phosphatidylcholine hydroperoxide ; Protein Biosynthesis ; RM, relative movement parameter ; Se-O-PhGPx, represents the oxidized enzyme ; Se-PhGPx, represents the reduced enzyme ; SOD, superoxide dismutase ; Superoxide Dismutase - metabolism ; TEMED, N,N,N′,N′-tetramethylethylene diamine ; Time Factors ; Transfection ; Wt, parental MCF-7 cells</subject><ispartof>Free radical research, 2003-06, Vol.37 (6), p.621-630</ispartof><rights>2003 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/1071576031000088283$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/1071576031000088283$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,59647,60436,61221,61402</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12868489$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Hong P.</creatorcontrib><creatorcontrib>Schafer, Freya Q.</creatorcontrib><creatorcontrib>Goswami, Prabhat C.</creatorcontrib><creatorcontrib>Oberley, Larry W.</creatorcontrib><creatorcontrib>Buettner, Garry R.</creatorcontrib><title>Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle</title><title>Free radical research</title><addtitle>Free Radic Res</addtitle><description>Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r=0.95). The higher the PhGPx activity, the lower the plating efficiency (r=-0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by >60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth.</description><subject>Antioxidant enzymes</subject><subject>Antioxidants - metabolism</subject><subject>Blotting, Western</subject><subject>BrdU, bromodeoxyuridine</subject><subject>Bromodeoxyuridine - pharmacology</subject><subject>CAT, catalase</subject><subject>Catalase - metabolism</subject><subject>Cell Cycle</subject><subject>Cell Differentiation</subject><subject>Cell Line, Tumor</subject><subject>CuZnSOD, copper zinc superoxide dismutase</subject><subject>EDTA, disodium ethylenediaminetetraacetic acid</subject><subject>EtOH, ethanol</subject><subject>Flow Cytometry</subject><subject>G1 Phase</subject><subject>Glutathione - metabolism</subject><subject>Glutathione peroxidase</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Glutathione Reductase - metabolism</subject><subject>GPx-1, cytosolic glutathione peroxidase</subject><subject>GR, glutathione reductase</subject><subject>GSH, glutathione</subject><subject>GSSG, glutathione disulfide</subject><subject>HO, hydrogen peroxide</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>L-PhGPx, mitochondrial phospholipid hydroperoxide glutathione peroxidase</subject><subject>Lipid hydroperoxide</subject><subject>Lipid Metabolism</subject><subject>Lipid Peroxides - metabolism</subject><subject>LOH, lipid alcohol</subject><subject>LOOHs, lipid hydroperoxides</subject><subject>MCF-7, human breast carcinoma cells</subject><subject>MnSOD, manganese superoxide dismutase</subject><subject>Models, Chemical</subject><subject>Neo, MCF-7 cells with empty vector</subject><subject>Oxidation-Reduction</subject><subject>P-1, P-2, P-3, P-4, are MCF-7 clones stably transfected with PhGPx</subject><subject>PBS, phosphate buffered saline</subject><subject>PE, plating efficiency</subject><subject>PI, propidium iodide</subject><subject>PLOOH, phosphatidylcholine hydroperoxide</subject><subject>Protein Biosynthesis</subject><subject>RM, relative movement parameter</subject><subject>Se-O-PhGPx, represents the oxidized enzyme</subject><subject>Se-PhGPx, represents the reduced enzyme</subject><subject>SOD, superoxide dismutase</subject><subject>Superoxide Dismutase - metabolism</subject><subject>TEMED, N,N,N′,N′-tetramethylethylene diamine</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>Wt, parental MCF-7 cells</subject><issn>1071-5762</issn><issn>1029-2470</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kctu1TAQhi0Eohd4AiTkFbsU307sLEBCBzitVKldlAUry3HGxJWPHewEyNvjqoW2EsKbsTz_fDOeH6FXlJxQoshbSiTdyJZwSupRiin-BB1SwrqGCUme3twlbaqEHaCjUq4JoVxs5HN0QJlqlVDdIfp6OaYyjSn4yQ_4dB1ymiCnX34AvAvLbObRpwj48vbRFMBncVgsFGzwRwhmxT7iHcXJ4XkEvIUQ8Ha1AV6gZ86EAi_v4jH68vnT1fa0Ob_YnW0_nDe-DjE3lgnLJOd9yzrGqQVHad85ziQYJ8D1YKxtWzFYkP2GyMG2XSckV70TNcn5MXp_y52Wfg9VFudsgp6y35u86mS8fpyJftTf0g8tWq4YYxXw5g6Q0_cFyqz3vtj6DxMhLUVLLloluazC1w87_W3xZ5v3o_joUt6bnymHQc9mDSm7bKL1RVe39I19-h_2VcC7R4ARTJhHazLo67TkWPeo_1f_G-Gtn9M</recordid><startdate>200306</startdate><enddate>200306</enddate><creator>Wang, Hong P.</creator><creator>Schafer, Freya Q.</creator><creator>Goswami, Prabhat C.</creator><creator>Oberley, Larry W.</creator><creator>Buettner, Garry R.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200306</creationdate><title>Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle</title><author>Wang, Hong P. ; Schafer, Freya Q. ; Goswami, Prabhat C. ; Oberley, Larry W. ; Buettner, Garry R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i286t-c24c2733b629231cef11b9f327eaf4efbeacc664dce7b507dc6994738bf4fbe33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Antioxidant enzymes</topic><topic>Antioxidants - metabolism</topic><topic>Blotting, Western</topic><topic>BrdU, bromodeoxyuridine</topic><topic>Bromodeoxyuridine - pharmacology</topic><topic>CAT, catalase</topic><topic>Catalase - metabolism</topic><topic>Cell Cycle</topic><topic>Cell Differentiation</topic><topic>Cell Line, Tumor</topic><topic>CuZnSOD, copper zinc superoxide dismutase</topic><topic>EDTA, disodium ethylenediaminetetraacetic acid</topic><topic>EtOH, ethanol</topic><topic>Flow Cytometry</topic><topic>G1 Phase</topic><topic>Glutathione - metabolism</topic><topic>Glutathione peroxidase</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Glutathione Reductase - metabolism</topic><topic>GPx-1, cytosolic glutathione peroxidase</topic><topic>GR, glutathione reductase</topic><topic>GSH, glutathione</topic><topic>GSSG, glutathione disulfide</topic><topic>HO, hydrogen peroxide</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>L-PhGPx, mitochondrial phospholipid hydroperoxide glutathione peroxidase</topic><topic>Lipid hydroperoxide</topic><topic>Lipid Metabolism</topic><topic>Lipid Peroxides - metabolism</topic><topic>LOH, lipid alcohol</topic><topic>LOOHs, lipid hydroperoxides</topic><topic>MCF-7, human breast carcinoma cells</topic><topic>MnSOD, manganese superoxide dismutase</topic><topic>Models, Chemical</topic><topic>Neo, MCF-7 cells with empty vector</topic><topic>Oxidation-Reduction</topic><topic>P-1, P-2, P-3, P-4, are MCF-7 clones stably transfected with PhGPx</topic><topic>PBS, phosphate buffered saline</topic><topic>PE, plating efficiency</topic><topic>PI, propidium iodide</topic><topic>PLOOH, phosphatidylcholine hydroperoxide</topic><topic>Protein Biosynthesis</topic><topic>RM, relative movement parameter</topic><topic>Se-O-PhGPx, represents the oxidized enzyme</topic><topic>Se-PhGPx, represents the reduced enzyme</topic><topic>SOD, superoxide dismutase</topic><topic>Superoxide Dismutase - metabolism</topic><topic>TEMED, N,N,N′,N′-tetramethylethylene diamine</topic><topic>Time Factors</topic><topic>Transfection</topic><topic>Wt, parental MCF-7 cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Hong P.</creatorcontrib><creatorcontrib>Schafer, Freya Q.</creatorcontrib><creatorcontrib>Goswami, Prabhat C.</creatorcontrib><creatorcontrib>Oberley, Larry W.</creatorcontrib><creatorcontrib>Buettner, Garry R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Free radical research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Hong P.</au><au>Schafer, Freya Q.</au><au>Goswami, Prabhat C.</au><au>Oberley, Larry W.</au><au>Buettner, Garry R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle</atitle><jtitle>Free radical research</jtitle><addtitle>Free Radic Res</addtitle><date>2003-06</date><risdate>2003</risdate><volume>37</volume><issue>6</issue><spage>621</spage><epage>630</epage><pages>621-630</pages><issn>1071-5762</issn><eissn>1029-2470</eissn><abstract>Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r=0.95). The higher the PhGPx activity, the lower the plating efficiency (r=-0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by >60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>12868489</pmid><doi>10.1080/1071576031000088283</doi><tpages>10</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1071-5762 |
ispartof | Free radical research, 2003-06, Vol.37 (6), p.621-630 |
issn | 1071-5762 1029-2470 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4638222 |
source | MEDLINE; Taylor & Francis:Master (3349 titles) |
subjects | Antioxidant enzymes Antioxidants - metabolism Blotting, Western BrdU, bromodeoxyuridine Bromodeoxyuridine - pharmacology CAT, catalase Catalase - metabolism Cell Cycle Cell Differentiation Cell Line, Tumor CuZnSOD, copper zinc superoxide dismutase EDTA, disodium ethylenediaminetetraacetic acid EtOH, ethanol Flow Cytometry G1 Phase Glutathione - metabolism Glutathione peroxidase Glutathione Peroxidase - metabolism Glutathione Reductase - metabolism GPx-1, cytosolic glutathione peroxidase GR, glutathione reductase GSH, glutathione GSSG, glutathione disulfide HO, hydrogen peroxide Humans Immunoblotting L-PhGPx, mitochondrial phospholipid hydroperoxide glutathione peroxidase Lipid hydroperoxide Lipid Metabolism Lipid Peroxides - metabolism LOH, lipid alcohol LOOHs, lipid hydroperoxides MCF-7, human breast carcinoma cells MnSOD, manganese superoxide dismutase Models, Chemical Neo, MCF-7 cells with empty vector Oxidation-Reduction P-1, P-2, P-3, P-4, are MCF-7 clones stably transfected with PhGPx PBS, phosphate buffered saline PE, plating efficiency PI, propidium iodide PLOOH, phosphatidylcholine hydroperoxide Protein Biosynthesis RM, relative movement parameter Se-O-PhGPx, represents the oxidized enzyme Se-PhGPx, represents the reduced enzyme SOD, superoxide dismutase Superoxide Dismutase - metabolism TEMED, N,N,N′,N′-tetramethylethylene diamine Time Factors Transfection Wt, parental MCF-7 cells |
title | Phospholipid Hydroperoxide Glutathione Peroxidase Induces a Delay in G1 of the Cell Cycle |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T19%3A30%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phospholipid%20Hydroperoxide%20Glutathione%20Peroxidase%20Induces%20a%20Delay%20in%20G1%20of%20the%20Cell%20Cycle&rft.jtitle=Free%20radical%20research&rft.au=Wang,%20Hong%20P.&rft.date=2003-06&rft.volume=37&rft.issue=6&rft.spage=621&rft.epage=630&rft.pages=621-630&rft.issn=1071-5762&rft.eissn=1029-2470&rft_id=info:doi/10.1080/1071576031000088283&rft_dat=%3Cproquest_pubme%3E73468737%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=73468737&rft_id=info:pmid/12868489&rfr_iscdi=true |