Targeted Disruption of Hsp110/105 Gene Protects Against Ischemic Stress
Hsp110/105 belongs to the HSP110 heat shock protein family, which is a subgroup of the HSP70 family. In mammals, Hsp110/105 is constitutively expressed but exhibits particularly high levels in the brain. It has recently been shown that both Hsp110/105 and Hsp70 are elevated after cerebral ischemia....
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| Veröffentlicht in: | Stroke (1970) 2008-10, Vol.39 (10), p.2853-2859 |
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| container_title | Stroke (1970) |
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| creator | NAKAMURA, Junji FUJIMOTO, Motoaki YASUDA, Kunihiko TAKEDA, Kiyoshi AKIRA, Shizuo HATAYAMA, Takumi TAKAGI, Yasushi NOZAKI, Kazuhiko HOSOKAWA, Nobuko NAGATA, Kazuhiro |
| description | Hsp110/105 belongs to the HSP110 heat shock protein family, which is a subgroup of the HSP70 family. In mammals, Hsp110/105 is constitutively expressed but exhibits particularly high levels in the brain. It has recently been shown that both Hsp110/105 and Hsp70 are elevated after cerebral ischemia. To study the physiological role of this protein in vivo, we generated hsp110/105 knockout (KO) mice and investigate the effect of reduced Hsp110/105 levels on focal cerebral ischemia.
hsp110/105 KO and wild-type mice were subjected to 30 minutes of transient middle cerebral artery occlusion followed by reperfusion for 24 hours. The infarct volume and neurological scores were measured and compared. The Hsp70 chaperone activity of thermally denatured firefly luciferase was measured in hsp110/105 KO embryonic fibroblasts.
The infarct volume and neurological deficit scores were significantly (P |
| doi_str_mv | 10.1161/STROKEAHA.107.506188 |
| format | Article |
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hsp110/105 KO and wild-type mice were subjected to 30 minutes of transient middle cerebral artery occlusion followed by reperfusion for 24 hours. The infarct volume and neurological scores were measured and compared. The Hsp70 chaperone activity of thermally denatured firefly luciferase was measured in hsp110/105 KO embryonic fibroblasts.
The infarct volume and neurological deficit scores were significantly (P<0.05) reduced in hsp110/105 KO mice compared with wild-type controls. In addition, hsp110/105 KO embryonic fibroblasts exhibited a dose-dependent suppression of Hsp70 chaperone activity by the presence of Hsp110/105.
These results demonstrate that hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70.</description><identifier>ISSN: 0039-2499</identifier><identifier>EISSN: 1524-4628</identifier><identifier>DOI: 10.1161/STROKEAHA.107.506188</identifier><identifier>PMID: 18658041</identifier><identifier>CODEN: SJCCA7</identifier><language>eng</language><publisher>Hagerstown, MD: Lippincott Williams & Wilkins</publisher><subject>Animals ; Biological and medical sciences ; Blood. Blood coagulation. Reticuloendothelial system ; Blotting, Western ; HSP110 Heat-Shock Proteins - genetics ; HSP110 Heat-Shock Proteins - metabolism ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; Infarction, Middle Cerebral Artery - genetics ; Infarction, Middle Cerebral Artery - pathology ; Male ; Medical sciences ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurology ; Pharmacology. Drug treatments ; Recovery of Function ; Vascular diseases and vascular malformations of the nervous system</subject><ispartof>Stroke (1970), 2008-10, Vol.39 (10), p.2853-2859</ispartof><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-75b62606d8ffb91cef3e466ca6c9ffa25bf10daa9c6df36f8b56ba839ed80e223</citedby><cites>FETCH-LOGICAL-c484t-75b62606d8ffb91cef3e466ca6c9ffa25bf10daa9c6df36f8b56ba839ed80e223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,3688,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20715113$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18658041$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>NAKAMURA, Junji</creatorcontrib><creatorcontrib>FUJIMOTO, Motoaki</creatorcontrib><creatorcontrib>YASUDA, Kunihiko</creatorcontrib><creatorcontrib>TAKEDA, Kiyoshi</creatorcontrib><creatorcontrib>AKIRA, Shizuo</creatorcontrib><creatorcontrib>HATAYAMA, Takumi</creatorcontrib><creatorcontrib>TAKAGI, Yasushi</creatorcontrib><creatorcontrib>NOZAKI, Kazuhiko</creatorcontrib><creatorcontrib>HOSOKAWA, Nobuko</creatorcontrib><creatorcontrib>NAGATA, Kazuhiro</creatorcontrib><title>Targeted Disruption of Hsp110/105 Gene Protects Against Ischemic Stress</title><title>Stroke (1970)</title><addtitle>Stroke</addtitle><description>Hsp110/105 belongs to the HSP110 heat shock protein family, which is a subgroup of the HSP70 family. In mammals, Hsp110/105 is constitutively expressed but exhibits particularly high levels in the brain. It has recently been shown that both Hsp110/105 and Hsp70 are elevated after cerebral ischemia. To study the physiological role of this protein in vivo, we generated hsp110/105 knockout (KO) mice and investigate the effect of reduced Hsp110/105 levels on focal cerebral ischemia.
hsp110/105 KO and wild-type mice were subjected to 30 minutes of transient middle cerebral artery occlusion followed by reperfusion for 24 hours. The infarct volume and neurological scores were measured and compared. The Hsp70 chaperone activity of thermally denatured firefly luciferase was measured in hsp110/105 KO embryonic fibroblasts.
The infarct volume and neurological deficit scores were significantly (P<0.05) reduced in hsp110/105 KO mice compared with wild-type controls. In addition, hsp110/105 KO embryonic fibroblasts exhibited a dose-dependent suppression of Hsp70 chaperone activity by the presence of Hsp110/105.
These results demonstrate that hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood. Blood coagulation. Reticuloendothelial system</subject><subject>Blotting, Western</subject><subject>HSP110 Heat-Shock Proteins - genetics</subject><subject>HSP110 Heat-Shock Proteins - metabolism</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Infarction, Middle Cerebral Artery - genetics</subject><subject>Infarction, Middle Cerebral Artery - pathology</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Neurology</subject><subject>Pharmacology. Drug treatments</subject><subject>Recovery of Function</subject><subject>Vascular diseases and vascular malformations of the nervous system</subject><issn>0039-2499</issn><issn>1524-4628</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMFOwkAURSdGI4j-gTHd6K4wbzozTJdEEYgkGMF1M52-wRpocV678O-FQHB1k5tz7-Iwdg-8D6BhsFx9LN7Go-moD3zYV1yDMResC0rIWGphLlmX8ySNhUzTDrsh-uaci8Soa9YBo5XhErpssrJhjQ0W0UtJod01ZV1FtY-mtAPgA-AqmmCF0XuoG3QNRaO1LStqohm5L9yWLlo2AYlu2ZW3G8K7U_bY5-t49TyN54vJ7Hk0j500somHKtdCc10Y7_MUHPoEpdbOapd6b4XKPfDC2tTpwifam1zp3JokxcJwFCLpsafj7y7UPy1Sk21LcrjZ2ArrljKdaiG1OoDyCLpQEwX02S6UWxt-M-DZQWB2FrhvhtlR4H72cPpv8y0W_6OTsT3weAIsObvxwVaupDMn-BAUQJL8AfVrePM</recordid><startdate>20081001</startdate><enddate>20081001</enddate><creator>NAKAMURA, Junji</creator><creator>FUJIMOTO, Motoaki</creator><creator>YASUDA, Kunihiko</creator><creator>TAKEDA, Kiyoshi</creator><creator>AKIRA, Shizuo</creator><creator>HATAYAMA, Takumi</creator><creator>TAKAGI, Yasushi</creator><creator>NOZAKI, Kazuhiko</creator><creator>HOSOKAWA, Nobuko</creator><creator>NAGATA, Kazuhiro</creator><general>Lippincott Williams & Wilkins</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><scope>7X8</scope></search><sort><creationdate>20081001</creationdate><title>Targeted Disruption of Hsp110/105 Gene Protects Against Ischemic Stress</title><author>NAKAMURA, Junji ; FUJIMOTO, Motoaki ; YASUDA, Kunihiko ; TAKEDA, Kiyoshi ; AKIRA, Shizuo ; HATAYAMA, Takumi ; TAKAGI, Yasushi ; NOZAKI, Kazuhiko ; HOSOKAWA, Nobuko ; NAGATA, Kazuhiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-75b62606d8ffb91cef3e466ca6c9ffa25bf10daa9c6df36f8b56ba839ed80e223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood. Blood coagulation. Reticuloendothelial system</topic><topic>Blotting, Western</topic><topic>HSP110 Heat-Shock Proteins - genetics</topic><topic>HSP110 Heat-Shock Proteins - metabolism</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Infarction, Middle Cerebral Artery - genetics</topic><topic>Infarction, Middle Cerebral Artery - pathology</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Neurology</topic><topic>Pharmacology. Drug treatments</topic><topic>Recovery of Function</topic><topic>Vascular diseases and vascular malformations of the nervous system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NAKAMURA, Junji</creatorcontrib><creatorcontrib>FUJIMOTO, Motoaki</creatorcontrib><creatorcontrib>YASUDA, Kunihiko</creatorcontrib><creatorcontrib>TAKEDA, Kiyoshi</creatorcontrib><creatorcontrib>AKIRA, Shizuo</creatorcontrib><creatorcontrib>HATAYAMA, Takumi</creatorcontrib><creatorcontrib>TAKAGI, Yasushi</creatorcontrib><creatorcontrib>NOZAKI, Kazuhiko</creatorcontrib><creatorcontrib>HOSOKAWA, Nobuko</creatorcontrib><creatorcontrib>NAGATA, Kazuhiro</creatorcontrib><collection>Pascal-Francis</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>Stroke (1970)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>NAKAMURA, Junji</au><au>FUJIMOTO, Motoaki</au><au>YASUDA, Kunihiko</au><au>TAKEDA, Kiyoshi</au><au>AKIRA, Shizuo</au><au>HATAYAMA, Takumi</au><au>TAKAGI, Yasushi</au><au>NOZAKI, Kazuhiko</au><au>HOSOKAWA, Nobuko</au><au>NAGATA, Kazuhiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Targeted Disruption of Hsp110/105 Gene Protects Against Ischemic Stress</atitle><jtitle>Stroke (1970)</jtitle><addtitle>Stroke</addtitle><date>2008-10-01</date><risdate>2008</risdate><volume>39</volume><issue>10</issue><spage>2853</spage><epage>2859</epage><pages>2853-2859</pages><issn>0039-2499</issn><eissn>1524-4628</eissn><coden>SJCCA7</coden><abstract>Hsp110/105 belongs to the HSP110 heat shock protein family, which is a subgroup of the HSP70 family. In mammals, Hsp110/105 is constitutively expressed but exhibits particularly high levels in the brain. It has recently been shown that both Hsp110/105 and Hsp70 are elevated after cerebral ischemia. To study the physiological role of this protein in vivo, we generated hsp110/105 knockout (KO) mice and investigate the effect of reduced Hsp110/105 levels on focal cerebral ischemia.
hsp110/105 KO and wild-type mice were subjected to 30 minutes of transient middle cerebral artery occlusion followed by reperfusion for 24 hours. The infarct volume and neurological scores were measured and compared. The Hsp70 chaperone activity of thermally denatured firefly luciferase was measured in hsp110/105 KO embryonic fibroblasts.
The infarct volume and neurological deficit scores were significantly (P<0.05) reduced in hsp110/105 KO mice compared with wild-type controls. In addition, hsp110/105 KO embryonic fibroblasts exhibited a dose-dependent suppression of Hsp70 chaperone activity by the presence of Hsp110/105.
These results demonstrate that hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70.</abstract><cop>Hagerstown, MD</cop><pub>Lippincott Williams & Wilkins</pub><pmid>18658041</pmid><doi>10.1161/STROKEAHA.107.506188</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Stroke (1970), 2008-10, Vol.39 (10), p.2853-2859 |
| issn | 0039-2499 1524-4628 |
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| source | MEDLINE; American Heart Association Journals; Journals@Ovid Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Blood. Blood coagulation. Reticuloendothelial system Blotting, Western HSP110 Heat-Shock Proteins - genetics HSP110 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Infarction, Middle Cerebral Artery - genetics Infarction, Middle Cerebral Artery - pathology Male Medical sciences Mice Mice, Inbred C57BL Mice, Knockout Neurology Pharmacology. Drug treatments Recovery of Function Vascular diseases and vascular malformations of the nervous system |
| title | Targeted Disruption of Hsp110/105 Gene Protects Against Ischemic Stress |
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