Role of the Cellular Stress Response in the Biogenesis of Cysteamine‐Induced Astrocytic Inclusions in Primary Culture
— Cysteamine (CSH; 2‐mercaptoethylamine) stimulates the accumulation of peroxidase‐positive inclusions in cultured astroglia akin to those observed in the aging periventricular brain. Because CSH induces the synthesis of a stress protein (heme oxygenase) in rat liver, we hypothesized that aspects of...
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description | — Cysteamine (CSH; 2‐mercaptoethylamine) stimulates the accumulation of peroxidase‐positive inclusions in cultured astroglia akin to those observed in the aging periventricular brain. Because CSH induces the synthesis of a stress protein (heme oxygenase) in rat liver, we hypothesized that aspects of the cellular stress response may play a role in the biogenesis of CSH‐induced astro‐cyte granules. In the present study, we performed indirect immunofluorescent staining and immunoblotting for various stress proteins in rat neuroglial cultures. Exposure of astrocyte cultures to CSH enhanced immunostaining for heme oxygenase‐1 (HO‐1) and heat‐shock proteins 27, 72, and 90, but not glucose‐regulated protein 94, relative to untreated cultures. CSH‐pretreated astrocytes exhibited enhanced tolerance to H2O2 toxicity relative to untreated cells, providing physiological evidence of an antecedent stress response in the former. In addition, exposure for 12 days to H2O2, a known inducer of the stress response, elicited astrocyte granulation similar to that observed with CSH. Chronic induction of HO‐1 and other stress proteins may participate in the biogenesis of metal‐loporphyrin‐rich inclusions in CSH‐treated astroglial cultures and in astrocytes of the aging periventricular brain. |
doi_str_mv | 10.1111/j.1471-4159.1993.tb09813.x |
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Because CSH induces the synthesis of a stress protein (heme oxygenase) in rat liver, we hypothesized that aspects of the cellular stress response may play a role in the biogenesis of CSH‐induced astro‐cyte granules. In the present study, we performed indirect immunofluorescent staining and immunoblotting for various stress proteins in rat neuroglial cultures. Exposure of astrocyte cultures to CSH enhanced immunostaining for heme oxygenase‐1 (HO‐1) and heat‐shock proteins 27, 72, and 90, but not glucose‐regulated protein 94, relative to untreated cultures. CSH‐pretreated astrocytes exhibited enhanced tolerance to H2O2 toxicity relative to untreated cells, providing physiological evidence of an antecedent stress response in the former. In addition, exposure for 12 days to H2O2, a known inducer of the stress response, elicited astrocyte granulation similar to that observed with CSH. Chronic induction of HO‐1 and other stress proteins may participate in the biogenesis of metal‐loporphyrin‐rich inclusions in CSH‐treated astroglial cultures and in astrocytes of the aging periventricular brain.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1111/j.1471-4159.1993.tb09813.x</identifier><identifier>PMID: 8228991</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Animals, Newborn ; Astrocyt ; Astrocytes - drug effects ; Astrocytes - metabolism ; Astrocytes - ultrastructure ; Biological and medical sciences ; Cell Survival - drug effects ; Cells, Cultured ; Cysteamine - pharmacology ; Dose-Response Relationship, Drug ; eat‐shock protein ; Electrophoresis, Polyacrylamide Gel ; eme oxygenase ; eroxidase activity ; Fundamental and applied biological sciences. Psychology ; Heat-Shock Proteins - biosynthesis ; Heat-Shock Proteins - isolation & purification ; Heme Oxygenase (Decyclizing) - biosynthesis ; Hydrogen Peroxide - pharmacology ; Inclusion Bodies - drug effects ; Inclusion Bodies - ultrastructure ; Isolated neuron and nerve. Neuroglia ; Kinetics ; lucose‐regulated protei ; Molecular Weight ; Nerve Tissue Proteins - biosynthesis ; Nerve Tissue Proteins - isolation & purification ; Neuroglia - cytology ; Neuroglia - drug effects ; Rats ; Rats, Sprague-Dawley ; Vertebrates: nervous system and sense organs ; ysteamin</subject><ispartof>Journal of neurochemistry, 1993-11, Vol.61 (5), p.1755-1765</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4305-d5b431e1c7694da3e8b09c956b2e1d1e74b1917a67bbc32f88efef30b209113c3</citedby><cites>FETCH-LOGICAL-c4305-d5b431e1c7694da3e8b09c956b2e1d1e74b1917a67bbc32f88efef30b209113c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1471-4159.1993.tb09813.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1471-4159.1993.tb09813.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3798647$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8228991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mydlarski, Marc B.</creatorcontrib><creatorcontrib>Liang, Jin‐Jun</creatorcontrib><creatorcontrib>Schipper, Hyman M.</creatorcontrib><title>Role of the Cellular Stress Response in the Biogenesis of Cysteamine‐Induced Astrocytic Inclusions in Primary Culture</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>— Cysteamine (CSH; 2‐mercaptoethylamine) stimulates the accumulation of peroxidase‐positive inclusions in cultured astroglia akin to those observed in the aging periventricular brain. Because CSH induces the synthesis of a stress protein (heme oxygenase) in rat liver, we hypothesized that aspects of the cellular stress response may play a role in the biogenesis of CSH‐induced astro‐cyte granules. In the present study, we performed indirect immunofluorescent staining and immunoblotting for various stress proteins in rat neuroglial cultures. Exposure of astrocyte cultures to CSH enhanced immunostaining for heme oxygenase‐1 (HO‐1) and heat‐shock proteins 27, 72, and 90, but not glucose‐regulated protein 94, relative to untreated cultures. CSH‐pretreated astrocytes exhibited enhanced tolerance to H2O2 toxicity relative to untreated cells, providing physiological evidence of an antecedent stress response in the former. In addition, exposure for 12 days to H2O2, a known inducer of the stress response, elicited astrocyte granulation similar to that observed with CSH. Chronic induction of HO‐1 and other stress proteins may participate in the biogenesis of metal‐loporphyrin‐rich inclusions in CSH‐treated astroglial cultures and in astrocytes of the aging periventricular brain.</description><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Astrocyt</subject><subject>Astrocytes - drug effects</subject><subject>Astrocytes - metabolism</subject><subject>Astrocytes - ultrastructure</subject><subject>Biological and medical sciences</subject><subject>Cell Survival - drug effects</subject><subject>Cells, Cultured</subject><subject>Cysteamine - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>eat‐shock protein</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>eme oxygenase</subject><subject>eroxidase activity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>Heat-Shock Proteins - isolation & purification</subject><subject>Heme Oxygenase (Decyclizing) - biosynthesis</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Inclusion Bodies - drug effects</subject><subject>Inclusion Bodies - ultrastructure</subject><subject>Isolated neuron and nerve. Neuroglia</subject><subject>Kinetics</subject><subject>lucose‐regulated protei</subject><subject>Molecular Weight</subject><subject>Nerve Tissue Proteins - biosynthesis</subject><subject>Nerve Tissue Proteins - isolation & purification</subject><subject>Neuroglia - cytology</subject><subject>Neuroglia - drug effects</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Vertebrates: nervous system and sense organs</subject><subject>ysteamin</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM9u1DAQxi1EVZbCIyBFCHFL6rGTOOaCSkRhqwpQgbPlOBPwKptsPYnavfEIPGOfhKQb7Z25zOH7vvnzY-w18ASmOt8kkCqIU8h0AlrLZKi4LkAm90_Y6ig9ZSvOhYglT8Uz9pxowznkaQ6n7LQQotAaVuzupm8x6pto-I1RiW07tjZE34eARNEN0q7vCCPfPeoffP8LOyRPc6Lc04B26zt8-PN33dWjwzq6oCH0bj94F607147kpwFz_lvwWxv2UTm2wxjwBTtpbEv4culn7Oflxx_l5_j666d1eXEdu1TyLK6zKpWA4FSu09pKLKZPnc7ySiDUgCqtQIOyuaoqJ0VTFNhgI3kluAaQTp6xt4e5u9DfjkiD2Xpy05-2w34kA7nKlRIwGd8djC70RAEbsztcbICbmbrZmBmtmdGambpZqJv7Kfxq2TJWW6yP0QXzpL9ZdEvOtk2wnfN0tEmlizxVk-39wXbnW9z_xwHm6ksJKsvkP-jIoZ0</recordid><startdate>199311</startdate><enddate>199311</enddate><creator>Mydlarski, Marc B.</creator><creator>Liang, Jin‐Jun</creator><creator>Schipper, Hyman M.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7TK</scope></search><sort><creationdate>199311</creationdate><title>Role of the Cellular Stress Response in the Biogenesis of Cysteamine‐Induced Astrocytic Inclusions in Primary Culture</title><author>Mydlarski, Marc B. ; Liang, Jin‐Jun ; Schipper, Hyman M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4305-d5b431e1c7694da3e8b09c956b2e1d1e74b1917a67bbc32f88efef30b209113c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Astrocyt</topic><topic>Astrocytes - drug effects</topic><topic>Astrocytes - metabolism</topic><topic>Astrocytes - ultrastructure</topic><topic>Biological and medical sciences</topic><topic>Cell Survival - drug effects</topic><topic>Cells, Cultured</topic><topic>Cysteamine - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>eat‐shock protein</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>eme oxygenase</topic><topic>eroxidase activity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>Heat-Shock Proteins - isolation & purification</topic><topic>Heme Oxygenase (Decyclizing) - biosynthesis</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Inclusion Bodies - drug effects</topic><topic>Inclusion Bodies - ultrastructure</topic><topic>Isolated neuron and nerve. Neuroglia</topic><topic>Kinetics</topic><topic>lucose‐regulated protei</topic><topic>Molecular Weight</topic><topic>Nerve Tissue Proteins - biosynthesis</topic><topic>Nerve Tissue Proteins - isolation & purification</topic><topic>Neuroglia - cytology</topic><topic>Neuroglia - drug effects</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Vertebrates: nervous system and sense organs</topic><topic>ysteamin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mydlarski, Marc B.</creatorcontrib><creatorcontrib>Liang, Jin‐Jun</creatorcontrib><creatorcontrib>Schipper, Hyman M.</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>Neurosciences Abstracts</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mydlarski, Marc B.</au><au>Liang, Jin‐Jun</au><au>Schipper, Hyman M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of the Cellular Stress Response in the Biogenesis of Cysteamine‐Induced Astrocytic Inclusions in Primary Culture</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1993-11</date><risdate>1993</risdate><volume>61</volume><issue>5</issue><spage>1755</spage><epage>1765</epage><pages>1755-1765</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>— Cysteamine (CSH; 2‐mercaptoethylamine) stimulates the accumulation of peroxidase‐positive inclusions in cultured astroglia akin to those observed in the aging periventricular brain. Because CSH induces the synthesis of a stress protein (heme oxygenase) in rat liver, we hypothesized that aspects of the cellular stress response may play a role in the biogenesis of CSH‐induced astro‐cyte granules. In the present study, we performed indirect immunofluorescent staining and immunoblotting for various stress proteins in rat neuroglial cultures. Exposure of astrocyte cultures to CSH enhanced immunostaining for heme oxygenase‐1 (HO‐1) and heat‐shock proteins 27, 72, and 90, but not glucose‐regulated protein 94, relative to untreated cultures. CSH‐pretreated astrocytes exhibited enhanced tolerance to H2O2 toxicity relative to untreated cells, providing physiological evidence of an antecedent stress response in the former. In addition, exposure for 12 days to H2O2, a known inducer of the stress response, elicited astrocyte granulation similar to that observed with CSH. Chronic induction of HO‐1 and other stress proteins may participate in the biogenesis of metal‐loporphyrin‐rich inclusions in CSH‐treated astroglial cultures and in astrocytes of the aging periventricular brain.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8228991</pmid><doi>10.1111/j.1471-4159.1993.tb09813.x</doi><tpages>11</tpages></addata></record> |
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subjects | Animals Animals, Newborn Astrocyt Astrocytes - drug effects Astrocytes - metabolism Astrocytes - ultrastructure Biological and medical sciences Cell Survival - drug effects Cells, Cultured Cysteamine - pharmacology Dose-Response Relationship, Drug eat‐shock protein Electrophoresis, Polyacrylamide Gel eme oxygenase eroxidase activity Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - biosynthesis Heat-Shock Proteins - isolation & purification Heme Oxygenase (Decyclizing) - biosynthesis Hydrogen Peroxide - pharmacology Inclusion Bodies - drug effects Inclusion Bodies - ultrastructure Isolated neuron and nerve. Neuroglia Kinetics lucose‐regulated protei Molecular Weight Nerve Tissue Proteins - biosynthesis Nerve Tissue Proteins - isolation & purification Neuroglia - cytology Neuroglia - drug effects Rats Rats, Sprague-Dawley Vertebrates: nervous system and sense organs ysteamin |
title | Role of the Cellular Stress Response in the Biogenesis of Cysteamine‐Induced Astrocytic Inclusions in Primary Culture |
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