Overexpression of HSP70 prevents ultraviolet B-induced apoptosis of a human melanoma cell line
The heat shock response is a highly conserved reaction common to all cells and organisms. It has been reported that hyperthermic treatment can induce the expression of the heat shock protein (HSP) and can protect cells from ultraviolet (UV) B radiation. In this study, we evaluated the effects of ind...
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| Veröffentlicht in: | Archives of Dermatological Research 2000-10, Vol.292 (10), p.482-487 |
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| container_title | Archives of Dermatological Research |
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| creator | PARK, Kyoung-Chan KIM, Dong-Seok CHOI, Hyun-Ok KIM, Kyu-Han CHUNG, Jin-Ho EUN, Hee-Chul LEE, Jae-Seon SEO, Jeong-Sun |
| description | The heat shock response is a highly conserved reaction common to all cells and organisms. It has been reported that hyperthermic treatment can induce the expression of the heat shock protein (HSP) and can protect cells from ultraviolet (UV) B radiation. In this study, we evaluated the effects of induced HSP70 on resistance to UV radiation. G361 amelanotic human melanoma cells were irradiated with increasing doses of UVB. UVB irradiation caused apoptotic cell death in these cells. Following transfection with MFG.hsp70.puro plasmid, the expression of HSP70 was determined. Compared to control vector-transfected cells, hsp70-transfected cells showed significantly elevated levels of HSP70 and were highly resistant to UVB irradiation. In order to investigate the effects of HSP70 on the apoptotic pathway, the changes in caspase-3 and PARP were analyzed. Following UVB irradiation, activation of caspase-3 and cleavage of PARP were observed in control vector-transfected cells, and the changes in these molecules were inhibited in the hsp70-transfected cells. These results suggest that UVB-induced apoptosis of melanoma cells is accompanied by caspase-3 activation and PARP cleavage, which can be prevented by an overexpression of HSP70. |
| doi_str_mv | 10.1007/s004030000173 |
| format | Article |
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It has been reported that hyperthermic treatment can induce the expression of the heat shock protein (HSP) and can protect cells from ultraviolet (UV) B radiation. In this study, we evaluated the effects of induced HSP70 on resistance to UV radiation. G361 amelanotic human melanoma cells were irradiated with increasing doses of UVB. UVB irradiation caused apoptotic cell death in these cells. Following transfection with MFG.hsp70.puro plasmid, the expression of HSP70 was determined. Compared to control vector-transfected cells, hsp70-transfected cells showed significantly elevated levels of HSP70 and were highly resistant to UVB irradiation. In order to investigate the effects of HSP70 on the apoptotic pathway, the changes in caspase-3 and PARP were analyzed. Following UVB irradiation, activation of caspase-3 and cleavage of PARP were observed in control vector-transfected cells, and the changes in these molecules were inhibited in the hsp70-transfected cells. These results suggest that UVB-induced apoptosis of melanoma cells is accompanied by caspase-3 activation and PARP cleavage, which can be prevented by an overexpression of HSP70.</description><identifier>ISSN: 0340-3696</identifier><identifier>EISSN: 1432-069X</identifier><identifier>DOI: 10.1007/s004030000173</identifier><identifier>PMID: 11142769</identifier><identifier>CODEN: ADREDL</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Apoptosis - drug effects ; Biological and medical sciences ; Caspase 3 ; Caspases - analysis ; Dermatology ; Dose-Response Relationship, Radiation ; HSP70 Heat-Shock Proteins - biosynthesis ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - pharmacology ; Humans ; Immunoblotting ; Medical sciences ; Transfection ; Transformation, Genetic ; Tumor Cells, Cultured ; Tumors of the skin and soft tissue. Premalignant lesions ; Ultraviolet Rays</subject><ispartof>Archives of Dermatological Research, 2000-10, Vol.292 (10), p.482-487</ispartof><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c383t-23479863cc9b70f54778803ae20eb53d716939be5028d147b6eb23e2568a7e863</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=801329$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11142769$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>PARK, Kyoung-Chan</creatorcontrib><creatorcontrib>KIM, Dong-Seok</creatorcontrib><creatorcontrib>CHOI, Hyun-Ok</creatorcontrib><creatorcontrib>KIM, Kyu-Han</creatorcontrib><creatorcontrib>CHUNG, Jin-Ho</creatorcontrib><creatorcontrib>EUN, Hee-Chul</creatorcontrib><creatorcontrib>LEE, Jae-Seon</creatorcontrib><creatorcontrib>SEO, Jeong-Sun</creatorcontrib><title>Overexpression of HSP70 prevents ultraviolet B-induced apoptosis of a human melanoma cell line</title><title>Archives of Dermatological Research</title><addtitle>Arch Dermatol Res</addtitle><description>The heat shock response is a highly conserved reaction common to all cells and organisms. It has been reported that hyperthermic treatment can induce the expression of the heat shock protein (HSP) and can protect cells from ultraviolet (UV) B radiation. In this study, we evaluated the effects of induced HSP70 on resistance to UV radiation. G361 amelanotic human melanoma cells were irradiated with increasing doses of UVB. UVB irradiation caused apoptotic cell death in these cells. Following transfection with MFG.hsp70.puro plasmid, the expression of HSP70 was determined. Compared to control vector-transfected cells, hsp70-transfected cells showed significantly elevated levels of HSP70 and were highly resistant to UVB irradiation. In order to investigate the effects of HSP70 on the apoptotic pathway, the changes in caspase-3 and PARP were analyzed. Following UVB irradiation, activation of caspase-3 and cleavage of PARP were observed in control vector-transfected cells, and the changes in these molecules were inhibited in the hsp70-transfected cells. These results suggest that UVB-induced apoptosis of melanoma cells is accompanied by caspase-3 activation and PARP cleavage, which can be prevented by an overexpression of HSP70.</description><subject>Apoptosis - drug effects</subject><subject>Biological and medical sciences</subject><subject>Caspase 3</subject><subject>Caspases - analysis</subject><subject>Dermatology</subject><subject>Dose-Response Relationship, Radiation</subject><subject>HSP70 Heat-Shock Proteins - biosynthesis</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - pharmacology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Medical sciences</subject><subject>Transfection</subject><subject>Transformation, Genetic</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors of the skin and soft tissue. Premalignant lesions</subject><subject>Ultraviolet Rays</subject><issn>0340-3696</issn><issn>1432-069X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpV0E1LAzEQBuAgii21R68S8Lw6-dhkc9SiVihUUMGTSzY7iyvZD5Jt0X_vlhbFuQwMzzuHl5BzBlcMQF9HAAkCxmFaHJEpk4InoMzbMZmCkJAIZdSEzGP83CENkoM-JRPGmORamSl5X28x4FcfMMa6a2lX0eXzkwY6XrbYDpFu_BDstu48DvQ2qdty47Cktu_6oYt13CUs_dg0tqUNett2jaUOvae-bvGMnFTWR5wf9oy83t-9LJbJav3wuLhZJU5kYki4kNpkSjhnCg1VKrXOMhAWOWCRilIzZYQpMAWelUzqQmHBBfJUZVbjGJyRZP_XhS7GgFXeh7qx4TtnkO-qyv9VNfqLve83RYPlnz4UM4LLA7DRWV8F27o6_roMmOBG_ADapG8T</recordid><startdate>20001001</startdate><enddate>20001001</enddate><creator>PARK, Kyoung-Chan</creator><creator>KIM, Dong-Seok</creator><creator>CHOI, Hyun-Ok</creator><creator>KIM, Kyu-Han</creator><creator>CHUNG, Jin-Ho</creator><creator>EUN, Hee-Chul</creator><creator>LEE, Jae-Seon</creator><creator>SEO, Jeong-Sun</creator><general>Springer</general><scope>IQODW</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></search><sort><creationdate>20001001</creationdate><title>Overexpression of HSP70 prevents ultraviolet B-induced apoptosis of a human melanoma cell line</title><author>PARK, Kyoung-Chan ; KIM, Dong-Seok ; CHOI, Hyun-Ok ; KIM, Kyu-Han ; CHUNG, Jin-Ho ; EUN, Hee-Chul ; LEE, Jae-Seon ; SEO, Jeong-Sun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-23479863cc9b70f54778803ae20eb53d716939be5028d147b6eb23e2568a7e863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Apoptosis - drug effects</topic><topic>Biological and medical sciences</topic><topic>Caspase 3</topic><topic>Caspases - analysis</topic><topic>Dermatology</topic><topic>Dose-Response Relationship, Radiation</topic><topic>HSP70 Heat-Shock Proteins - biosynthesis</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - pharmacology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Medical sciences</topic><topic>Transfection</topic><topic>Transformation, Genetic</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors of the skin and soft tissue. 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It has been reported that hyperthermic treatment can induce the expression of the heat shock protein (HSP) and can protect cells from ultraviolet (UV) B radiation. In this study, we evaluated the effects of induced HSP70 on resistance to UV radiation. G361 amelanotic human melanoma cells were irradiated with increasing doses of UVB. UVB irradiation caused apoptotic cell death in these cells. Following transfection with MFG.hsp70.puro plasmid, the expression of HSP70 was determined. Compared to control vector-transfected cells, hsp70-transfected cells showed significantly elevated levels of HSP70 and were highly resistant to UVB irradiation. In order to investigate the effects of HSP70 on the apoptotic pathway, the changes in caspase-3 and PARP were analyzed. Following UVB irradiation, activation of caspase-3 and cleavage of PARP were observed in control vector-transfected cells, and the changes in these molecules were inhibited in the hsp70-transfected cells. These results suggest that UVB-induced apoptosis of melanoma cells is accompanied by caspase-3 activation and PARP cleavage, which can be prevented by an overexpression of HSP70.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>11142769</pmid><doi>10.1007/s004030000173</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; SpringerNature Journals |
| subjects | Apoptosis - drug effects Biological and medical sciences Caspase 3 Caspases - analysis Dermatology Dose-Response Relationship, Radiation HSP70 Heat-Shock Proteins - biosynthesis HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - pharmacology Humans Immunoblotting Medical sciences Transfection Transformation, Genetic Tumor Cells, Cultured Tumors of the skin and soft tissue. Premalignant lesions Ultraviolet Rays |
| title | Overexpression of HSP70 prevents ultraviolet B-induced apoptosis of a human melanoma cell line |
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