A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses
To adapt to different environmental conditions between poikilothermic and homeothermic hosts, the plerocercoid of Spirometra erinacei (sparganum) might express a variety of biologically active molecules. We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential...
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| Veröffentlicht in: | Parasitology 2004-12, Vol.129 (6), p.713-721 |
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| creator | YUN, D.-H. BAE, Y.-A. CHUNG, J.-Y. KANG, S.-Y. KANG, I. SOHN, W.-M. CHO, S.-H. KIM, T.-S. CHO, S.-Y. KONG, Y. |
| description | To adapt to different environmental conditions between poikilothermic and homeothermic hosts, the plerocercoid of Spirometra erinacei (sparganum) might express a variety of biologically active molecules. We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential display of mRNA, employing RNAs each from sparganum adjusted at 9 °C and 37 °C. A full-length cDNA of 2148 bp encodes for a protein of 651 amino acids with a predicted molecular mass of 71 610 Da and shares molecular characteristics with heat-shock protein 70, including a putative ATP binding site, signal peptide cleavage site and endoplasmic reticulum retention signal. Phylogenetic analysis revealed that SpGrp78 was mostly related to those of Echinococcus multilocularis and E. granulosus. Expression of SpGrp78 mRNA increased approximately 7-fold by inhibition of glycosylation by tunicamycin, 2-fold by temperature-shift from 9 °C to 37 °C and slightly by pH-shift to 4·0 or 5·5. These results suggested that induction of SpGrp78 mRNA is related to the functional role of SpGrp78 as a molecular chaperone when the parasite adapts to a new host environment. |
| doi_str_mv | 10.1017/S0031182004006158 |
| format | Article |
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We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential display of mRNA, employing RNAs each from sparganum adjusted at 9 °C and 37 °C. A full-length cDNA of 2148 bp encodes for a protein of 651 amino acids with a predicted molecular mass of 71 610 Da and shares molecular characteristics with heat-shock protein 70, including a putative ATP binding site, signal peptide cleavage site and endoplasmic reticulum retention signal. Phylogenetic analysis revealed that SpGrp78 was mostly related to those of Echinococcus multilocularis and E. granulosus. Expression of SpGrp78 mRNA increased approximately 7-fold by inhibition of glycosylation by tunicamycin, 2-fold by temperature-shift from 9 °C to 37 °C and slightly by pH-shift to 4·0 or 5·5. These results suggested that induction of SpGrp78 mRNA is related to the functional role of SpGrp78 as a molecular chaperone when the parasite adapts to a new host environment.</description><identifier>ISSN: 0031-1820</identifier><identifier>EISSN: 1469-8161</identifier><identifier>DOI: 10.1017/S0031182004006158</identifier><identifier>PMID: 15648694</identifier><identifier>CODEN: PARAAE</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Adaptation, Physiological ; Amino Acid Sequence ; Amino acids ; Animals ; Binding sites ; Biological activity ; Biological and medical sciences ; Biomedical research ; Cloning ; Deoxyribonucleic acid ; Differential display ; differential display PCR ; DNA ; Endoplasmic reticulum ; Environmental conditions ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation - drug effects ; Gene Expression Regulation - physiology ; General aspects ; General aspects and techniques. Study of several systematic groups. Models ; Glucose ; glucose-regulated protein ; Glycosylation ; Heat shock proteins ; heat-shock protein ; Heat-Shock Proteins - biosynthesis ; Heat-Shock Proteins - physiology ; Helminth Proteins - biosynthesis ; Helminth Proteins - physiology ; Host-Parasite Interactions ; Infections ; Invertebrates ; Mammals ; Medicine ; Molecular chains ; molecular chaperones ; Molecular Chaperones - biosynthesis ; Molecular Chaperones - physiology ; Molecular Sequence Data ; mRNA ; Organic chemistry ; Parasites ; Parasitic diseases ; Parasitology ; Phylogeny ; Physiology ; Proteins ; Research centers ; RNA, Messenger ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sparganum - drug effects ; Sparganum - genetics ; Sparganum - physiology ; Species Specificity ; Spirometra ; Spirometra erinacei plerocercoid (sparganum) ; Stress (physiology) ; stress protein ; Tropical diseases ; Tunicamycin</subject><ispartof>Parasitology, 2004-12, Vol.129 (6), p.713-721</ispartof><rights>2004 Cambridge University Press</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-fd4443a41b90bed9a0e699fca3a837016a9374330d602ccaf8ca419806b096183</citedby><cites>FETCH-LOGICAL-c439t-fd4443a41b90bed9a0e699fca3a837016a9374330d602ccaf8ca419806b096183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S0031182004006158/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,315,781,785,27929,27930,55633</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16318300$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15648694$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>YUN, D.-H.</creatorcontrib><creatorcontrib>BAE, Y.-A.</creatorcontrib><creatorcontrib>CHUNG, J.-Y.</creatorcontrib><creatorcontrib>KANG, S.-Y.</creatorcontrib><creatorcontrib>KANG, I.</creatorcontrib><creatorcontrib>SOHN, W.-M.</creatorcontrib><creatorcontrib>CHO, S.-H.</creatorcontrib><creatorcontrib>KIM, T.-S.</creatorcontrib><creatorcontrib>CHO, S.-Y.</creatorcontrib><creatorcontrib>KONG, Y.</creatorcontrib><title>A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses</title><title>Parasitology</title><addtitle>Parasitology</addtitle><description>To adapt to different environmental conditions between poikilothermic and homeothermic hosts, the plerocercoid of Spirometra erinacei (sparganum) might express a variety of biologically active molecules. We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential display of mRNA, employing RNAs each from sparganum adjusted at 9 °C and 37 °C. A full-length cDNA of 2148 bp encodes for a protein of 651 amino acids with a predicted molecular mass of 71 610 Da and shares molecular characteristics with heat-shock protein 70, including a putative ATP binding site, signal peptide cleavage site and endoplasmic reticulum retention signal. Phylogenetic analysis revealed that SpGrp78 was mostly related to those of Echinococcus multilocularis and E. granulosus. Expression of SpGrp78 mRNA increased approximately 7-fold by inhibition of glycosylation by tunicamycin, 2-fold by temperature-shift from 9 °C to 37 °C and slightly by pH-shift to 4·0 or 5·5. These results suggested that induction of SpGrp78 mRNA is related to the functional role of SpGrp78 as a molecular chaperone when the parasite adapts to a new host environment.</description><subject>Adaptation, Physiological</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Biological activity</subject><subject>Biological and medical sciences</subject><subject>Biomedical research</subject><subject>Cloning</subject><subject>Deoxyribonucleic acid</subject><subject>Differential display</subject><subject>differential display PCR</subject><subject>DNA</subject><subject>Endoplasmic reticulum</subject><subject>Environmental conditions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation - drug effects</subject><subject>Gene Expression Regulation - physiology</subject><subject>General aspects</subject><subject>General aspects and techniques. Study of several systematic groups. Models</subject><subject>Glucose</subject><subject>glucose-regulated protein</subject><subject>Glycosylation</subject><subject>Heat shock proteins</subject><subject>heat-shock protein</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>Heat-Shock Proteins - physiology</subject><subject>Helminth Proteins - biosynthesis</subject><subject>Helminth Proteins - physiology</subject><subject>Host-Parasite Interactions</subject><subject>Infections</subject><subject>Invertebrates</subject><subject>Mammals</subject><subject>Medicine</subject><subject>Molecular chains</subject><subject>molecular chaperones</subject><subject>Molecular Chaperones - biosynthesis</subject><subject>Molecular Chaperones - physiology</subject><subject>Molecular Sequence Data</subject><subject>mRNA</subject><subject>Organic chemistry</subject><subject>Parasites</subject><subject>Parasitic diseases</subject><subject>Parasitology</subject><subject>Phylogeny</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Research centers</subject><subject>RNA, Messenger</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sparganum - drug effects</subject><subject>Sparganum - genetics</subject><subject>Sparganum - physiology</subject><subject>Species Specificity</subject><subject>Spirometra</subject><subject>Spirometra erinacei plerocercoid (sparganum)</subject><subject>Stress (physiology)</subject><subject>stress protein</subject><subject>Tropical diseases</subject><subject>Tunicamycin</subject><issn>0031-1820</issn><issn>1469-8161</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp1kVGL1DAUhYMo7jj6A3yRgLhv1ZsmTZPH3XVdhUWRVfAtpOntbHbbZkxacPz1ZpzigOJTIOe7h3PuJeQ5g9cMWP3mBoAzpkoAASBZpR6QFRNSF4pJ9pCs9nKx10_Ik5TuIENclo_JCaukUFKLFfl5RmtF799auulnFxIWETdzbyds6TaGCf1INzgiDR292foYBpyipRj9aB16uu0xBofRBd9SP7azy4PNjrpbHLyzPbVjNrrdJR_6sPn9k6aIKWF6Sh51tk_4bHnX5Ou7yy8X74vrT1cfLs6uCye4noquFUJwK1ijocFWW0Cpdecst4rXwKTVvBacQyuhdM52ymVYK5ANaMkUX5PTg2_u833GNJnBJ4d9b0cMczKyLstSMZHBl3-Bd2GOY85mSqgrUbKqlpliB8rFkFLEzmyjH2zcGQZmfxbzz1nyzIvFeW4GbI8Tyx0y8GoBbMo76qIdnU9HTvJcJNuuSXHgfJrwxx_dxvtcg9eVkVefzbfz6hzgIzNV5vkS1g5N9O0Gj53-H_cXYFyyZg</recordid><startdate>20041201</startdate><enddate>20041201</enddate><creator>YUN, D.-H.</creator><creator>BAE, Y.-A.</creator><creator>CHUNG, J.-Y.</creator><creator>KANG, S.-Y.</creator><creator>KANG, I.</creator><creator>SOHN, W.-M.</creator><creator>CHO, S.-H.</creator><creator>KIM, T.-S.</creator><creator>CHO, S.-Y.</creator><creator>KONG, Y.</creator><general>Cambridge University Press</general><scope>BSCLL</scope><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>3V.</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20041201</creationdate><title>A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses</title><author>YUN, D.-H. ; BAE, Y.-A. ; CHUNG, J.-Y. ; KANG, S.-Y. ; KANG, I. ; SOHN, W.-M. ; CHO, S.-H. ; KIM, T.-S. ; CHO, S.-Y. ; KONG, Y.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-fd4443a41b90bed9a0e699fca3a837016a9374330d602ccaf8ca419806b096183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adaptation, Physiological</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Biological activity</topic><topic>Biological and medical sciences</topic><topic>Biomedical research</topic><topic>Cloning</topic><topic>Deoxyribonucleic acid</topic><topic>Differential display</topic><topic>differential display PCR</topic><topic>DNA</topic><topic>Endoplasmic reticulum</topic><topic>Environmental conditions</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation - drug effects</topic><topic>Gene Expression Regulation - physiology</topic><topic>General aspects</topic><topic>General aspects and techniques. Study of several systematic groups. Models</topic><topic>Glucose</topic><topic>glucose-regulated protein</topic><topic>Glycosylation</topic><topic>Heat shock proteins</topic><topic>heat-shock protein</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>Heat-Shock Proteins - physiology</topic><topic>Helminth Proteins - biosynthesis</topic><topic>Helminth Proteins - physiology</topic><topic>Host-Parasite Interactions</topic><topic>Infections</topic><topic>Invertebrates</topic><topic>Mammals</topic><topic>Medicine</topic><topic>Molecular chains</topic><topic>molecular chaperones</topic><topic>Molecular Chaperones - biosynthesis</topic><topic>Molecular Chaperones - physiology</topic><topic>Molecular Sequence Data</topic><topic>mRNA</topic><topic>Organic chemistry</topic><topic>Parasites</topic><topic>Parasitic diseases</topic><topic>Parasitology</topic><topic>Phylogeny</topic><topic>Physiology</topic><topic>Proteins</topic><topic>Research centers</topic><topic>RNA, Messenger</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sparganum - drug effects</topic><topic>Sparganum - genetics</topic><topic>Sparganum - physiology</topic><topic>Species Specificity</topic><topic>Spirometra</topic><topic>Spirometra erinacei plerocercoid (sparganum)</topic><topic>Stress (physiology)</topic><topic>stress protein</topic><topic>Tropical diseases</topic><topic>Tunicamycin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>YUN, D.-H.</creatorcontrib><creatorcontrib>BAE, Y.-A.</creatorcontrib><creatorcontrib>CHUNG, J.-Y.</creatorcontrib><creatorcontrib>KANG, S.-Y.</creatorcontrib><creatorcontrib>KANG, I.</creatorcontrib><creatorcontrib>SOHN, W.-M.</creatorcontrib><creatorcontrib>CHO, S.-H.</creatorcontrib><creatorcontrib>KIM, T.-S.</creatorcontrib><creatorcontrib>CHO, S.-Y.</creatorcontrib><creatorcontrib>KONG, Y.</creatorcontrib><collection>Istex</collection><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>ProQuest Central (Corporate)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YUN, D.-H.</au><au>BAE, Y.-A.</au><au>CHUNG, J.-Y.</au><au>KANG, S.-Y.</au><au>KANG, I.</au><au>SOHN, W.-M.</au><au>CHO, S.-H.</au><au>KIM, T.-S.</au><au>CHO, S.-Y.</au><au>KONG, Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses</atitle><jtitle>Parasitology</jtitle><addtitle>Parasitology</addtitle><date>2004-12-01</date><risdate>2004</risdate><volume>129</volume><issue>6</issue><spage>713</spage><epage>721</epage><pages>713-721</pages><issn>0031-1820</issn><eissn>1469-8161</eissn><coden>PARAAE</coden><abstract>To adapt to different environmental conditions between poikilothermic and homeothermic hosts, the plerocercoid of Spirometra erinacei (sparganum) might express a variety of biologically active molecules. We have identified a 78 kDa glucose-regulated protein of the sparganum (SpGrp78) by differential display of mRNA, employing RNAs each from sparganum adjusted at 9 °C and 37 °C. A full-length cDNA of 2148 bp encodes for a protein of 651 amino acids with a predicted molecular mass of 71 610 Da and shares molecular characteristics with heat-shock protein 70, including a putative ATP binding site, signal peptide cleavage site and endoplasmic reticulum retention signal. Phylogenetic analysis revealed that SpGrp78 was mostly related to those of Echinococcus multilocularis and E. granulosus. Expression of SpGrp78 mRNA increased approximately 7-fold by inhibition of glycosylation by tunicamycin, 2-fold by temperature-shift from 9 °C to 37 °C and slightly by pH-shift to 4·0 or 5·5. These results suggested that induction of SpGrp78 mRNA is related to the functional role of SpGrp78 as a molecular chaperone when the parasite adapts to a new host environment.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>15648694</pmid><doi>10.1017/S0031182004006158</doi><tpages>9</tpages></addata></record> |
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| ispartof | Parasitology, 2004-12, Vol.129 (6), p.713-721 |
| issn | 0031-1820 1469-8161 |
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| source | MEDLINE; Cambridge University Press Journals Complete |
| subjects | Adaptation, Physiological Amino Acid Sequence Amino acids Animals Binding sites Biological activity Biological and medical sciences Biomedical research Cloning Deoxyribonucleic acid Differential display differential display PCR DNA Endoplasmic reticulum Environmental conditions Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation - drug effects Gene Expression Regulation - physiology General aspects General aspects and techniques. Study of several systematic groups. Models Glucose glucose-regulated protein Glycosylation Heat shock proteins heat-shock protein Heat-Shock Proteins - biosynthesis Heat-Shock Proteins - physiology Helminth Proteins - biosynthesis Helminth Proteins - physiology Host-Parasite Interactions Infections Invertebrates Mammals Medicine Molecular chains molecular chaperones Molecular Chaperones - biosynthesis Molecular Chaperones - physiology Molecular Sequence Data mRNA Organic chemistry Parasites Parasitic diseases Parasitology Phylogeny Physiology Proteins Research centers RNA, Messenger Sequence Alignment Sequence Homology, Amino Acid Sparganum - drug effects Sparganum - genetics Sparganum - physiology Species Specificity Spirometra Spirometra erinacei plerocercoid (sparganum) Stress (physiology) stress protein Tropical diseases Tunicamycin |
| title | A 78 kDa glucose-regulated protein gene of Spirometra erinacei plerocercoid induced by chemical and physiological stresses |
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