In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content
Heat shock proteins play an important role as molecular chaperones of the cell. Inducible heat shock protein 70 is rapidly synthesised in response to numerous stressors and monocytes are sensitive to changes in core temperature resulting in a circadian variation of Hsp70 expression. Monocytes were i...
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description | Heat shock proteins play an important role as molecular chaperones of the cell. Inducible heat shock protein 70 is rapidly synthesised in response to numerous stressors and monocytes are sensitive to changes in core temperature resulting in a circadian variation of Hsp70 expression. Monocytes were isolated via density centrifugation from nine healthy male volunteers at 5 am, 1 pm and 9 pm, representing the nadir (5 am), peak (9 pm) and intermediate (1 pm) of Hsp70 expression in the 24-h cycle. Analysis of freshly isolated monocytes for Hsp70 expression confirmed Hsp70 levels at the three selected time points. Monocytes were subjected to in vitro heat shock at 40°C (±0.1) for 90 min with a 90 min 37°C (±0.1) exposure acting as a control. A significant increase in Hsp70 was observed at 5 am (p < 0.001) and 1 pm (p = 0.028) at 40°C when compared to 37°C but not at 9 pm (p = 0.19). A significant increase was also observed from the basal levels of Hsp70, measured on freshly isolated monocytes and the levels detected after heat shock at 40°C at 5 am (p < 0.001) and 1 pm (p = 0.001), which was not observed at 9 pm (p = 0.15). Furthermore, a significant correlation was observed in the heat shock response at 40°C and that obtained at 37°C (p < 0.001). In conclusion, the heat shock response in monocytes is directly proportional to the amount of Hsp70 present in the cells and the stress response may be much higher at different times of the day. |
doi_str_mv | 10.1007/s00726-009-0354-4 |
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Inducible heat shock protein 70 is rapidly synthesised in response to numerous stressors and monocytes are sensitive to changes in core temperature resulting in a circadian variation of Hsp70 expression. Monocytes were isolated via density centrifugation from nine healthy male volunteers at 5 am, 1 pm and 9 pm, representing the nadir (5 am), peak (9 pm) and intermediate (1 pm) of Hsp70 expression in the 24-h cycle. Analysis of freshly isolated monocytes for Hsp70 expression confirmed Hsp70 levels at the three selected time points. Monocytes were subjected to in vitro heat shock at 40°C (±0.1) for 90 min with a 90 min 37°C (±0.1) exposure acting as a control. A significant increase in Hsp70 was observed at 5 am (p < 0.001) and 1 pm (p = 0.028) at 40°C when compared to 37°C but not at 9 pm (p = 0.19). A significant increase was also observed from the basal levels of Hsp70, measured on freshly isolated monocytes and the levels detected after heat shock at 40°C at 5 am (p < 0.001) and 1 pm (p = 0.001), which was not observed at 9 pm (p = 0.15). Furthermore, a significant correlation was observed in the heat shock response at 40°C and that obtained at 37°C (p < 0.001). In conclusion, the heat shock response in monocytes is directly proportional to the amount of Hsp70 present in the cells and the stress response may be much higher at different times of the day.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-009-0354-4</identifier><identifier>PMID: 19779802</identifier><language>eng</language><publisher>Vienna: Vienna : Springer Vienna</publisher><subject>Adolescent ; Adult ; Amino acids ; Analytical Chemistry ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Cellular biology ; Correlation ; Density ; diurnal variation ; Flow Cytometry ; Heat shock ; Heat shock proteins ; heat stress ; Hsp70 ; HSP70 Heat-Shock Proteins - metabolism ; Human ; Humans ; In Vitro Techniques ; In vitro testing ; Life Sciences ; Male ; Males ; monocytes ; Monocytes - metabolism ; Neurobiology ; Original Article ; Proteins ; Proteomics ; stress response ; Young Adult</subject><ispartof>Amino acids, 2010-05, Vol.38 (5), p.1423-1428</ispartof><rights>Springer-Verlag 2009</rights><rights>Springer-Verlag 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-9a106747e180a0a025192a8d3e903aac5df6bd902902c23f4d580a37728860883</citedby><cites>FETCH-LOGICAL-c428t-9a106747e180a0a025192a8d3e903aac5df6bd902902c23f4d580a37728860883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-009-0354-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-009-0354-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19779802$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vince, Rebecca V</creatorcontrib><creatorcontrib>Oliver, Katherine</creatorcontrib><creatorcontrib>Midgley, Adrian W</creatorcontrib><creatorcontrib>McNaughton, Lars R</creatorcontrib><creatorcontrib>Madden, Leigh A</creatorcontrib><title>In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>Heat shock proteins play an important role as molecular chaperones of the cell. Inducible heat shock protein 70 is rapidly synthesised in response to numerous stressors and monocytes are sensitive to changes in core temperature resulting in a circadian variation of Hsp70 expression. Monocytes were isolated via density centrifugation from nine healthy male volunteers at 5 am, 1 pm and 9 pm, representing the nadir (5 am), peak (9 pm) and intermediate (1 pm) of Hsp70 expression in the 24-h cycle. Analysis of freshly isolated monocytes for Hsp70 expression confirmed Hsp70 levels at the three selected time points. Monocytes were subjected to in vitro heat shock at 40°C (±0.1) for 90 min with a 90 min 37°C (±0.1) exposure acting as a control. A significant increase in Hsp70 was observed at 5 am (p < 0.001) and 1 pm (p = 0.028) at 40°C when compared to 37°C but not at 9 pm (p = 0.19). A significant increase was also observed from the basal levels of Hsp70, measured on freshly isolated monocytes and the levels detected after heat shock at 40°C at 5 am (p < 0.001) and 1 pm (p = 0.001), which was not observed at 9 pm (p = 0.15). Furthermore, a significant correlation was observed in the heat shock response at 40°C and that obtained at 37°C (p < 0.001). In conclusion, the heat shock response in monocytes is directly proportional to the amount of Hsp70 present in the cells and the stress response may be much higher at different times of the day.</description><subject>Adolescent</subject><subject>Adult</subject><subject>Amino acids</subject><subject>Analytical Chemistry</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cellular biology</subject><subject>Correlation</subject><subject>Density</subject><subject>diurnal variation</subject><subject>Flow Cytometry</subject><subject>Heat shock</subject><subject>Heat shock proteins</subject><subject>heat stress</subject><subject>Hsp70</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Human</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>In vitro testing</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Males</subject><subject>monocytes</subject><subject>Monocytes - metabolism</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>stress response</subject><subject>Young Adult</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kcGK1TAUhoMoznX0AdxowIVuqidJ2yTLYVBnYMCFzjrkpum9Hduk5qTivIDPbUovKIKSkAPJ9__hnJ-Q5wzeMgD5DsvB2wpAVyCauqofkB2rhao40_oh2YEWuqrrhp2RJ4h3AIwr1j4mZ0xLqRXwHfl5Hej3IadIj95misfovtLY0-My2UCnGKK7zx5p8riMGekQqKVzinNMeYjBjuXGJW_Rr6ohdIsb9qOnVzhLoP7HXIRYQGqdi6kbwoHmSPPR073FonYxZB_yU_KotyP6Z6d6Tm4_vP9yeVXdfPp4fXlxU7maq1xpy6CVtfRMgS2LN0xzqzrhNQhrXdP17b7TwMt2XPR11xRQSMmVakEpcU5eb76lhW-Lx2ymAZ0fRxt8XNBIITRvpIBCvvkvyYDpVnJgoqCv_kLv4pLKbFZKN21bRr1SbKNciojJ92ZOw2TTfYHMGqfZ4jQlTrPGaeqieXFyXvaT734rTvkVgG8Alqdw8OnPr__t-nIT9TYae0gDmtvPayfAVCFaIX4BGVuzIg</recordid><startdate>20100501</startdate><enddate>20100501</enddate><creator>Vince, Rebecca V</creator><creator>Oliver, Katherine</creator><creator>Midgley, Adrian W</creator><creator>McNaughton, Lars R</creator><creator>Madden, Leigh A</creator><general>Vienna : Springer Vienna</general><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20100501</creationdate><title>In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content</title><author>Vince, Rebecca V ; Oliver, Katherine ; Midgley, Adrian W ; McNaughton, Lars R ; Madden, Leigh A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-9a106747e180a0a025192a8d3e903aac5df6bd902902c23f4d580a37728860883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adolescent</topic><topic>Adult</topic><topic>Amino acids</topic><topic>Analytical Chemistry</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cellular biology</topic><topic>Correlation</topic><topic>Density</topic><topic>diurnal variation</topic><topic>Flow Cytometry</topic><topic>Heat shock</topic><topic>Heat shock proteins</topic><topic>heat stress</topic><topic>Hsp70</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Human</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>In vitro testing</topic><topic>Life Sciences</topic><topic>Male</topic><topic>Males</topic><topic>monocytes</topic><topic>Monocytes - metabolism</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>stress response</topic><topic>Young Adult</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vince, Rebecca V</creatorcontrib><creatorcontrib>Oliver, Katherine</creatorcontrib><creatorcontrib>Midgley, Adrian W</creatorcontrib><creatorcontrib>McNaughton, Lars R</creatorcontrib><creatorcontrib>Madden, Leigh A</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vince, Rebecca V</au><au>Oliver, Katherine</au><au>Midgley, Adrian W</au><au>McNaughton, Lars R</au><au>Madden, Leigh A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2010-05-01</date><risdate>2010</risdate><volume>38</volume><issue>5</issue><spage>1423</spage><epage>1428</epage><pages>1423-1428</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Heat shock proteins play an important role as molecular chaperones of the cell. Inducible heat shock protein 70 is rapidly synthesised in response to numerous stressors and monocytes are sensitive to changes in core temperature resulting in a circadian variation of Hsp70 expression. Monocytes were isolated via density centrifugation from nine healthy male volunteers at 5 am, 1 pm and 9 pm, representing the nadir (5 am), peak (9 pm) and intermediate (1 pm) of Hsp70 expression in the 24-h cycle. Analysis of freshly isolated monocytes for Hsp70 expression confirmed Hsp70 levels at the three selected time points. Monocytes were subjected to in vitro heat shock at 40°C (±0.1) for 90 min with a 90 min 37°C (±0.1) exposure acting as a control. A significant increase in Hsp70 was observed at 5 am (p < 0.001) and 1 pm (p = 0.028) at 40°C when compared to 37°C but not at 9 pm (p = 0.19). A significant increase was also observed from the basal levels of Hsp70, measured on freshly isolated monocytes and the levels detected after heat shock at 40°C at 5 am (p < 0.001) and 1 pm (p = 0.001), which was not observed at 9 pm (p = 0.15). Furthermore, a significant correlation was observed in the heat shock response at 40°C and that obtained at 37°C (p < 0.001). In conclusion, the heat shock response in monocytes is directly proportional to the amount of Hsp70 present in the cells and the stress response may be much higher at different times of the day.</abstract><cop>Vienna</cop><pub>Vienna : Springer Vienna</pub><pmid>19779802</pmid><doi>10.1007/s00726-009-0354-4</doi><tpages>6</tpages></addata></record> |
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subjects | Adolescent Adult Amino acids Analytical Chemistry Biochemical Engineering Biochemistry Biomedical and Life Sciences Cellular biology Correlation Density diurnal variation Flow Cytometry Heat shock Heat shock proteins heat stress Hsp70 HSP70 Heat-Shock Proteins - metabolism Human Humans In Vitro Techniques In vitro testing Life Sciences Male Males monocytes Monocytes - metabolism Neurobiology Original Article Proteins Proteomics stress response Young Adult |
title | In vitro heat shock of human monocytes results in a proportional increase of inducible Hsp70 expression according to the basal content |
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