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Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor

Farnesyl transferase inhibitors (FTIs) are novel antitumor drugs with clinical activity. FTIs inhibit cell growth not only by preventing direct Ras farnesylation but also through a Ras‐independent pathway. Proteomics has been shown to be a powerful tool to monitor and analyze molecular networks and...

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Published in:Proteomics (Weinheim) 2003-10, Vol.3 (10), p.1904-1911
Main Authors: Hu, Wei, Wu, WeiGuo, Verschraegen, Claire F., Chen, Ling, Mao, Li, Yeung, Sai-Ching Jim, Kudelka, Andrzej P., Freedman, Ralph S., Kavanagh, John J.
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creator Hu, Wei
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Kavanagh, John J.
description Farnesyl transferase inhibitors (FTIs) are novel antitumor drugs with clinical activity. FTIs inhibit cell growth not only by preventing direct Ras farnesylation but also through a Ras‐independent pathway. Proteomics has been shown to be a powerful tool to monitor and analyze molecular networks and fluxes within the living cells and to identify the proteins that participate in these networks upon perturbation of the cellular environment. To observe early and dynamic protein changes in the cellular response to FTI in ovarian cancer cells, total proteins were extracted from 2774 cells treated or not with 10 μM manumycin, an FTI, for 3, 6 and 16 h. The proteins in the cells that were differentially expressed following treatment with manumycin for 3, 6 and 16 h were noted by two‐dimensional electrophoresis and further identified by peptide mass fingerprinting as stress proteins. Both heat shock protein 70 (HSP70) and altered HSP70 were significantly up‐regulated as early as 16 h in 2774 cells after exposure to manumycin. Since HSP70 plays an important role in protecting cells under stress, we treated the 2774 cells with the HSP inhibitor quercetin in combination with FTI. Quercetin dramatically enhanced the manumycin‐mediated apoptosis in 2774 cells. Inducible HSP70 by manumycin in surviving ovarian cancer cells was also inhibited by quercetin as demonstrated by enzyme‐linked immunosorbent assay. The inhibition of HSP70 by quercetin was correlated with enhancement of manumycin‐induced mediated apoptosis in 2774 cells. The inhibition of HSP70 by 50 μM quercetin was also correlated with a decreased expression of procaspase‐3 and enhancement of specific cleavage of poly (ADP‐ribose) polymerase into apoptotic fragment in 2774 cells treated with manumycin. The interaction between the HSP70 inhibitor and FTI confirms the functional significance of the up‐regulation of HSP70 as a protective mechanism against FTI‐induced apoptosis and provides the framework for combination treatment of ovarian cancer.
doi_str_mv 10.1002/pmic.200300547
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FTIs inhibit cell growth not only by preventing direct Ras farnesylation but also through a Ras‐independent pathway. Proteomics has been shown to be a powerful tool to monitor and analyze molecular networks and fluxes within the living cells and to identify the proteins that participate in these networks upon perturbation of the cellular environment. To observe early and dynamic protein changes in the cellular response to FTI in ovarian cancer cells, total proteins were extracted from 2774 cells treated or not with 10 μM manumycin, an FTI, for 3, 6 and 16 h. The proteins in the cells that were differentially expressed following treatment with manumycin for 3, 6 and 16 h were noted by two‐dimensional electrophoresis and further identified by peptide mass fingerprinting as stress proteins. Both heat shock protein 70 (HSP70) and altered HSP70 were significantly up‐regulated as early as 16 h in 2774 cells after exposure to manumycin. Since HSP70 plays an important role in protecting cells under stress, we treated the 2774 cells with the HSP inhibitor quercetin in combination with FTI. Quercetin dramatically enhanced the manumycin‐mediated apoptosis in 2774 cells. Inducible HSP70 by manumycin in surviving ovarian cancer cells was also inhibited by quercetin as demonstrated by enzyme‐linked immunosorbent assay. The inhibition of HSP70 by quercetin was correlated with enhancement of manumycin‐induced mediated apoptosis in 2774 cells. The inhibition of HSP70 by 50 μM quercetin was also correlated with a decreased expression of procaspase‐3 and enhancement of specific cleavage of poly (ADP‐ribose) polymerase into apoptotic fragment in 2774 cells treated with manumycin. The interaction between the HSP70 inhibitor and FTI confirms the functional significance of the up‐regulation of HSP70 as a protective mechanism against FTI‐induced apoptosis and provides the framework for combination treatment of ovarian cancer.</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.200300547</identifier><identifier>PMID: 14625852</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Alkyl and Aryl Transferases - antagonists &amp; inhibitors ; Apoptosis ; Apoptosis - drug effects ; Blotting, Western ; Caspase 3 ; Caspases - analysis ; Caspases - drug effects ; Caspases - metabolism ; Cell Line, Tumor - drug effects ; Databases, Protein ; Electrophoresis, Gel, Two-Dimensional ; Enzyme Inhibitors - pharmacology ; Enzyme-Linked Immunosorbent Assay ; Farnesyl transferase inhibitor ; Farnesyltranstransferase ; Female ; Heat shock protein 70 ; HSP70 Heat-Shock Proteins - analysis ; HSP70 Heat-Shock Proteins - antagonists &amp; inhibitors ; HSP70 Heat-Shock Proteins - metabolism ; Humans ; Image Processing, Computer-Assisted ; In Situ Nick-End Labeling ; Ovarian cancers ; Ovarian Neoplasms - metabolism ; Ovarian Neoplasms - pathology ; Poly(ADP-ribose) Polymerases - analysis ; Poly(ADP-ribose) Polymerases - drug effects ; Poly(ADP-ribose) Polymerases - metabolism ; Polyenes - pharmacology ; Polyunsaturated Alkamides ; Proteomics ; Quercetin ; Quercetin - pharmacology ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Up-Regulation</subject><ispartof>Proteomics (Weinheim), 2003-10, Vol.3 (10), p.1904-1911</ispartof><rights>Copyright © 2003 WILEY‐VCH Verlag GmbH &amp; Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4457-38e0cbb5976074bca63a450192175d336092a4d1983dae85a05551d1813bd5fc3</citedby><cites>FETCH-LOGICAL-c4457-38e0cbb5976074bca63a450192175d336092a4d1983dae85a05551d1813bd5fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14625852$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hu, Wei</creatorcontrib><creatorcontrib>Wu, WeiGuo</creatorcontrib><creatorcontrib>Verschraegen, Claire F.</creatorcontrib><creatorcontrib>Chen, Ling</creatorcontrib><creatorcontrib>Mao, Li</creatorcontrib><creatorcontrib>Yeung, Sai-Ching Jim</creatorcontrib><creatorcontrib>Kudelka, Andrzej P.</creatorcontrib><creatorcontrib>Freedman, Ralph S.</creatorcontrib><creatorcontrib>Kavanagh, John J.</creatorcontrib><title>Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor</title><title>Proteomics (Weinheim)</title><addtitle>Proteomics</addtitle><description>Farnesyl transferase inhibitors (FTIs) are novel antitumor drugs with clinical activity. FTIs inhibit cell growth not only by preventing direct Ras farnesylation but also through a Ras‐independent pathway. Proteomics has been shown to be a powerful tool to monitor and analyze molecular networks and fluxes within the living cells and to identify the proteins that participate in these networks upon perturbation of the cellular environment. To observe early and dynamic protein changes in the cellular response to FTI in ovarian cancer cells, total proteins were extracted from 2774 cells treated or not with 10 μM manumycin, an FTI, for 3, 6 and 16 h. The proteins in the cells that were differentially expressed following treatment with manumycin for 3, 6 and 16 h were noted by two‐dimensional electrophoresis and further identified by peptide mass fingerprinting as stress proteins. Both heat shock protein 70 (HSP70) and altered HSP70 were significantly up‐regulated as early as 16 h in 2774 cells after exposure to manumycin. Since HSP70 plays an important role in protecting cells under stress, we treated the 2774 cells with the HSP inhibitor quercetin in combination with FTI. Quercetin dramatically enhanced the manumycin‐mediated apoptosis in 2774 cells. Inducible HSP70 by manumycin in surviving ovarian cancer cells was also inhibited by quercetin as demonstrated by enzyme‐linked immunosorbent assay. The inhibition of HSP70 by quercetin was correlated with enhancement of manumycin‐induced mediated apoptosis in 2774 cells. The inhibition of HSP70 by 50 μM quercetin was also correlated with a decreased expression of procaspase‐3 and enhancement of specific cleavage of poly (ADP‐ribose) polymerase into apoptotic fragment in 2774 cells treated with manumycin. The interaction between the HSP70 inhibitor and FTI confirms the functional significance of the up‐regulation of HSP70 as a protective mechanism against FTI‐induced apoptosis and provides the framework for combination treatment of ovarian cancer.</description><subject>Alkyl and Aryl Transferases - antagonists &amp; inhibitors</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Blotting, Western</subject><subject>Caspase 3</subject><subject>Caspases - analysis</subject><subject>Caspases - drug effects</subject><subject>Caspases - metabolism</subject><subject>Cell Line, Tumor - drug effects</subject><subject>Databases, Protein</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Farnesyl transferase inhibitor</subject><subject>Farnesyltranstransferase</subject><subject>Female</subject><subject>Heat shock protein 70</subject><subject>HSP70 Heat-Shock Proteins - analysis</subject><subject>HSP70 Heat-Shock Proteins - antagonists &amp; inhibitors</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Image Processing, Computer-Assisted</subject><subject>In Situ Nick-End Labeling</subject><subject>Ovarian cancers</subject><subject>Ovarian Neoplasms - metabolism</subject><subject>Ovarian Neoplasms - pathology</subject><subject>Poly(ADP-ribose) Polymerases - analysis</subject><subject>Poly(ADP-ribose) Polymerases - drug effects</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Polyenes - pharmacology</subject><subject>Polyunsaturated Alkamides</subject><subject>Proteomics</subject><subject>Quercetin</subject><subject>Quercetin - pharmacology</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Up-Regulation</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkE2P0zAQhiMEYj_gyhH5xC1lHMdxckRl6a60wB5AK3GxJvZkaza1g-0K-hP416RqVbhxmpHmeR9p3qJ4xWHBAaq308aZRQUgAGStnhTnvOGy7NqGPz3tUpwVFyl9B-Cq7dTz4ozXTSVbWZ0Xv-9iyBRmC3OWfHaDM5hd8CwMbE2YWVoH88imPeY8U8AwMWQGvXUWM7GM8YEyG0Jk5NfojfMPDKcw5ZBcYs7brSHL-h0bMHpKu5HliD4NFDHRfF-73uUQXxTPBhwTvTzOy-Lrh6svy-vy9vPqZvnutjR1LVUpWgLT97JTDai6N9gIrCXwruJKWiEa6CqsLe9aYZFaiSCl5Ja3XPRWDkZcFm8O3vmlH1tKWW9cMjSO6Clsk1ZctMCbdgYXB9DEkFKkQU_RbTDuNAe9L1_vy9en8ufA66N522_I_sWPbc9AdwB-upF2_9Hpu483y3_l5SHrUqZfpyzGR90ooaS-_7TS9_w9rL5BrYX4A5AJodc</recordid><startdate>200310</startdate><enddate>200310</enddate><creator>Hu, Wei</creator><creator>Wu, WeiGuo</creator><creator>Verschraegen, Claire F.</creator><creator>Chen, Ling</creator><creator>Mao, Li</creator><creator>Yeung, Sai-Ching Jim</creator><creator>Kudelka, Andrzej P.</creator><creator>Freedman, Ralph S.</creator><creator>Kavanagh, John J.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200310</creationdate><title>Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor</title><author>Hu, Wei ; 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inhibitors</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Image Processing, Computer-Assisted</topic><topic>In Situ Nick-End Labeling</topic><topic>Ovarian cancers</topic><topic>Ovarian Neoplasms - metabolism</topic><topic>Ovarian Neoplasms - pathology</topic><topic>Poly(ADP-ribose) Polymerases - analysis</topic><topic>Poly(ADP-ribose) Polymerases - drug effects</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Polyenes - pharmacology</topic><topic>Polyunsaturated Alkamides</topic><topic>Proteomics</topic><topic>Quercetin</topic><topic>Quercetin - pharmacology</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hu, Wei</creatorcontrib><creatorcontrib>Wu, WeiGuo</creatorcontrib><creatorcontrib>Verschraegen, Claire F.</creatorcontrib><creatorcontrib>Chen, Ling</creatorcontrib><creatorcontrib>Mao, Li</creatorcontrib><creatorcontrib>Yeung, Sai-Ching Jim</creatorcontrib><creatorcontrib>Kudelka, Andrzej P.</creatorcontrib><creatorcontrib>Freedman, Ralph S.</creatorcontrib><creatorcontrib>Kavanagh, John J.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hu, Wei</au><au>Wu, WeiGuo</au><au>Verschraegen, Claire F.</au><au>Chen, Ling</au><au>Mao, Li</au><au>Yeung, Sai-Ching Jim</au><au>Kudelka, Andrzej P.</au><au>Freedman, Ralph S.</au><au>Kavanagh, John J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2003-10</date><risdate>2003</risdate><volume>3</volume><issue>10</issue><spage>1904</spage><epage>1911</epage><pages>1904-1911</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>Farnesyl transferase inhibitors (FTIs) are novel antitumor drugs with clinical activity. FTIs inhibit cell growth not only by preventing direct Ras farnesylation but also through a Ras‐independent pathway. Proteomics has been shown to be a powerful tool to monitor and analyze molecular networks and fluxes within the living cells and to identify the proteins that participate in these networks upon perturbation of the cellular environment. To observe early and dynamic protein changes in the cellular response to FTI in ovarian cancer cells, total proteins were extracted from 2774 cells treated or not with 10 μM manumycin, an FTI, for 3, 6 and 16 h. The proteins in the cells that were differentially expressed following treatment with manumycin for 3, 6 and 16 h were noted by two‐dimensional electrophoresis and further identified by peptide mass fingerprinting as stress proteins. Both heat shock protein 70 (HSP70) and altered HSP70 were significantly up‐regulated as early as 16 h in 2774 cells after exposure to manumycin. Since HSP70 plays an important role in protecting cells under stress, we treated the 2774 cells with the HSP inhibitor quercetin in combination with FTI. Quercetin dramatically enhanced the manumycin‐mediated apoptosis in 2774 cells. Inducible HSP70 by manumycin in surviving ovarian cancer cells was also inhibited by quercetin as demonstrated by enzyme‐linked immunosorbent assay. The inhibition of HSP70 by quercetin was correlated with enhancement of manumycin‐induced mediated apoptosis in 2774 cells. The inhibition of HSP70 by 50 μM quercetin was also correlated with a decreased expression of procaspase‐3 and enhancement of specific cleavage of poly (ADP‐ribose) polymerase into apoptotic fragment in 2774 cells treated with manumycin. The interaction between the HSP70 inhibitor and FTI confirms the functional significance of the up‐regulation of HSP70 as a protective mechanism against FTI‐induced apoptosis and provides the framework for combination treatment of ovarian cancer.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>14625852</pmid><doi>10.1002/pmic.200300547</doi><tpages>8</tpages></addata></record>
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subjects Alkyl and Aryl Transferases - antagonists & inhibitors
Apoptosis
Apoptosis - drug effects
Blotting, Western
Caspase 3
Caspases - analysis
Caspases - drug effects
Caspases - metabolism
Cell Line, Tumor - drug effects
Databases, Protein
Electrophoresis, Gel, Two-Dimensional
Enzyme Inhibitors - pharmacology
Enzyme-Linked Immunosorbent Assay
Farnesyl transferase inhibitor
Farnesyltranstransferase
Female
Heat shock protein 70
HSP70 Heat-Shock Proteins - analysis
HSP70 Heat-Shock Proteins - antagonists & inhibitors
HSP70 Heat-Shock Proteins - metabolism
Humans
Image Processing, Computer-Assisted
In Situ Nick-End Labeling
Ovarian cancers
Ovarian Neoplasms - metabolism
Ovarian Neoplasms - pathology
Poly(ADP-ribose) Polymerases - analysis
Poly(ADP-ribose) Polymerases - drug effects
Poly(ADP-ribose) Polymerases - metabolism
Polyenes - pharmacology
Polyunsaturated Alkamides
Proteomics
Quercetin
Quercetin - pharmacology
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Up-Regulation
title Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor
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