Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells
To study the cytoprotective capacity of Hsp27 under various cellular stresses, we compared the effects of heating and energy deprivation on its distribution and isoform composition. Cultured endothelial cells from human aorta or umbilical vein were subjected to heat shock (45°C) and ATP-depleting me...
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| Veröffentlicht in: | FEBS letters 1996-08, Vol.392 (2), p.100-104 |
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| creator | Loktionova, Svetlana A. Ilyinskaya, Olga P. Gabai, Vladimir L. Kabakov, Alexander E. |
| description | To study the cytoprotective capacity of Hsp27 under various cellular stresses, we compared the effects of heating and energy deprivation on its distribution and isoform composition. Cultured endothelial cells from human aorta or umbilical vein were subjected to heat shock (45°C) and ATP-depleting metabolic stress (CCCP or rotenone in a glucose-free medium). Both exposures led to the translocation of Hsp27 into the Triton X-100-insoluble cellular fraction, whereas the immunofluorescent Hsp27 pattern was characteristic for each stress employed. Heating (5–30 min) caused unexpected association of Hsp27 with thick bundles of actin microfilaments (stress fibers). ATP depletion within 30–120 min resulted in the appearance of Hsp27-containing compact granules in the nucleus. The insolubilization and relocalization of Hsp27 were reversible in both cases. The stress-induced shifts in the Hsp27 isoform spectrum indicate an increase in phosphorylation of Hsp27 in heat-shocked cells and its dephosphorylation in ATP-depleted cells. We suggest that these stresses diversely affect the phosphorylation status of endothelial Hsp27, thus altering its localization, supramolecular organization and functional activity toward actin. |
| doi_str_mv | 10.1016/0014-5793(96)00792-2 |
| format | Article |
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Cultured endothelial cells from human aorta or umbilical vein were subjected to heat shock (45°C) and ATP-depleting metabolic stress (CCCP or rotenone in a glucose-free medium). Both exposures led to the translocation of Hsp27 into the Triton X-100-insoluble cellular fraction, whereas the immunofluorescent Hsp27 pattern was characteristic for each stress employed. Heating (5–30 min) caused unexpected association of Hsp27 with thick bundles of actin microfilaments (stress fibers). ATP depletion within 30–120 min resulted in the appearance of Hsp27-containing compact granules in the nucleus. The insolubilization and relocalization of Hsp27 were reversible in both cases. The stress-induced shifts in the Hsp27 isoform spectrum indicate an increase in phosphorylation of Hsp27 in heat-shocked cells and its dephosphorylation in ATP-depleted cells. We suggest that these stresses diversely affect the phosphorylation status of endothelial Hsp27, thus altering its localization, supramolecular organization and functional activity toward actin.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(96)00792-2</identifier><identifier>PMID: 8772183</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Actin ; Adenosine Triphosphate - metabolism ; ATP depletion ; carbonyl cyanide m-chlorophenylhydrazone ; CCCP ; ECL ; endothelial cells ; Endothelium, Vascular - cytology ; Endothelium, Vascular - metabolism ; enhanced chemiluminiscence ; FITC ; fluorescein isothiocyanate ; Heat shock ; heat shock protein ; Heat-Shock Proteins - metabolism ; Hot Temperature ; Hsp ; Hsp27 ; Humans ; PBS ; phosphate-buffered saline ; SDS ; Signal Transduction ; sodium dodecyl sulfate ; Stress protein ; Subcellular Fractions - metabolism ; Vascular endothelial cell</subject><ispartof>FEBS letters, 1996-08, Vol.392 (2), p.100-104</ispartof><rights>1996</rights><rights>FEBS Letters 392 (1996) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4202-ba77257b2bb1810adc488206bef40a10bb1f2b74f81c41f1424492e4697bb83f3</citedby><cites>FETCH-LOGICAL-c4202-ba77257b2bb1810adc488206bef40a10bb1f2b74f81c41f1424492e4697bb83f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2F0014-5793%2896%2900792-2$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(96)00792-2$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,3550,27924,27925,45574,45575,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8772183$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Loktionova, Svetlana A.</creatorcontrib><creatorcontrib>Ilyinskaya, Olga P.</creatorcontrib><creatorcontrib>Gabai, Vladimir L.</creatorcontrib><creatorcontrib>Kabakov, Alexander E.</creatorcontrib><title>Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>To study the cytoprotective capacity of Hsp27 under various cellular stresses, we compared the effects of heating and energy deprivation on its distribution and isoform composition. Cultured endothelial cells from human aorta or umbilical vein were subjected to heat shock (45°C) and ATP-depleting metabolic stress (CCCP or rotenone in a glucose-free medium). Both exposures led to the translocation of Hsp27 into the Triton X-100-insoluble cellular fraction, whereas the immunofluorescent Hsp27 pattern was characteristic for each stress employed. Heating (5–30 min) caused unexpected association of Hsp27 with thick bundles of actin microfilaments (stress fibers). ATP depletion within 30–120 min resulted in the appearance of Hsp27-containing compact granules in the nucleus. The insolubilization and relocalization of Hsp27 were reversible in both cases. The stress-induced shifts in the Hsp27 isoform spectrum indicate an increase in phosphorylation of Hsp27 in heat-shocked cells and its dephosphorylation in ATP-depleted cells. We suggest that these stresses diversely affect the phosphorylation status of endothelial Hsp27, thus altering its localization, supramolecular organization and functional activity toward actin.</description><subject>Actin</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>ATP depletion</subject><subject>carbonyl cyanide m-chlorophenylhydrazone</subject><subject>CCCP</subject><subject>ECL</subject><subject>endothelial cells</subject><subject>Endothelium, Vascular - cytology</subject><subject>Endothelium, Vascular - metabolism</subject><subject>enhanced chemiluminiscence</subject><subject>FITC</subject><subject>fluorescein isothiocyanate</subject><subject>Heat shock</subject><subject>heat shock protein</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Hot Temperature</subject><subject>Hsp</subject><subject>Hsp27</subject><subject>Humans</subject><subject>PBS</subject><subject>phosphate-buffered saline</subject><subject>SDS</subject><subject>Signal Transduction</subject><subject>sodium dodecyl sulfate</subject><subject>Stress protein</subject><subject>Subcellular Fractions - metabolism</subject><subject>Vascular endothelial cell</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhS0EKtuFfwCST4geQm3HjZ0LUmm7FKkSHMrZsp2x1pDEwXao9t_XaVY9IiRL1ryZeX76jNA7Sj5RQptzQiivLkRbf2ybM0JEyyr2Am2oFHVV80a-RJvnkdfoNKVfpNSStifoRArBqKw36HDtU_ajzRicA5sTDg7vQWec9sH-xnrs8OX9D9zB1EP2YcTldGUnejM_1cuET8GFOOBJ5wxxXE3mQY_4Nk1MYD9iGLuQ99B73WMLfZ_eoFdO9wneHu8t-rm7ub-6re6-f_12dXlXWc4Iq4wuUS-EYcaU7ER3lkvJSGPAcaIpKbJjRnAnqeXUUc44bxnwphXGyNrVW_Rh9Z1i-DNDymrwaUmgRwhzUkIyIWiBsUV8HbQxpBTBqSn6QceDokQtxNWCUy04VbsUhbhiZe390X82A3TPS0fEpb9b-w--h8N_eardzRe2NBa9bZ7U5aHPqxEUWn89RJWsh9FC52P5OdUF_--kjyI5o24</recordid><startdate>19960826</startdate><enddate>19960826</enddate><creator>Loktionova, Svetlana A.</creator><creator>Ilyinskaya, Olga P.</creator><creator>Gabai, Vladimir L.</creator><creator>Kabakov, Alexander E.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19960826</creationdate><title>Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells</title><author>Loktionova, Svetlana A. ; Ilyinskaya, Olga P. ; Gabai, Vladimir L. ; Kabakov, Alexander E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4202-ba77257b2bb1810adc488206bef40a10bb1f2b74f81c41f1424492e4697bb83f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Actin</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>ATP depletion</topic><topic>carbonyl cyanide m-chlorophenylhydrazone</topic><topic>CCCP</topic><topic>ECL</topic><topic>endothelial cells</topic><topic>Endothelium, Vascular - cytology</topic><topic>Endothelium, Vascular - metabolism</topic><topic>enhanced chemiluminiscence</topic><topic>FITC</topic><topic>fluorescein isothiocyanate</topic><topic>Heat shock</topic><topic>heat shock protein</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Hot Temperature</topic><topic>Hsp</topic><topic>Hsp27</topic><topic>Humans</topic><topic>PBS</topic><topic>phosphate-buffered saline</topic><topic>SDS</topic><topic>Signal Transduction</topic><topic>sodium dodecyl sulfate</topic><topic>Stress protein</topic><topic>Subcellular Fractions - metabolism</topic><topic>Vascular endothelial cell</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Loktionova, Svetlana A.</creatorcontrib><creatorcontrib>Ilyinskaya, Olga P.</creatorcontrib><creatorcontrib>Gabai, Vladimir L.</creatorcontrib><creatorcontrib>Kabakov, Alexander E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Loktionova, Svetlana A.</au><au>Ilyinskaya, Olga P.</au><au>Gabai, Vladimir L.</au><au>Kabakov, Alexander E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-08-26</date><risdate>1996</risdate><volume>392</volume><issue>2</issue><spage>100</spage><epage>104</epage><pages>100-104</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>To study the cytoprotective capacity of Hsp27 under various cellular stresses, we compared the effects of heating and energy deprivation on its distribution and isoform composition. Cultured endothelial cells from human aorta or umbilical vein were subjected to heat shock (45°C) and ATP-depleting metabolic stress (CCCP or rotenone in a glucose-free medium). Both exposures led to the translocation of Hsp27 into the Triton X-100-insoluble cellular fraction, whereas the immunofluorescent Hsp27 pattern was characteristic for each stress employed. Heating (5–30 min) caused unexpected association of Hsp27 with thick bundles of actin microfilaments (stress fibers). ATP depletion within 30–120 min resulted in the appearance of Hsp27-containing compact granules in the nucleus. The insolubilization and relocalization of Hsp27 were reversible in both cases. The stress-induced shifts in the Hsp27 isoform spectrum indicate an increase in phosphorylation of Hsp27 in heat-shocked cells and its dephosphorylation in ATP-depleted cells. We suggest that these stresses diversely affect the phosphorylation status of endothelial Hsp27, thus altering its localization, supramolecular organization and functional activity toward actin.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8772183</pmid><doi>10.1016/0014-5793(96)00792-2</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; Access via ScienceDirect (Elsevier); Alma/SFX Local Collection |
| subjects | Actin Adenosine Triphosphate - metabolism ATP depletion carbonyl cyanide m-chlorophenylhydrazone CCCP ECL endothelial cells Endothelium, Vascular - cytology Endothelium, Vascular - metabolism enhanced chemiluminiscence FITC fluorescein isothiocyanate Heat shock heat shock protein Heat-Shock Proteins - metabolism Hot Temperature Hsp Hsp27 Humans PBS phosphate-buffered saline SDS Signal Transduction sodium dodecyl sulfate Stress protein Subcellular Fractions - metabolism Vascular endothelial cell |
| title | Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells |
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