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Endoplasmic reticulum stress response of Bombyx mori calreticulin
We isolated a calreticulin cDNA from the silkworm, Bombyx mori. The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology w...
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| Published in: | Molecular biology reports 2005-09, Vol.32 (3), p.133-139 |
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| Main Authors: | , , , , , , , |
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| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c357t-decbbc02b8c306672db09decd5f2317c74fccb7039af449e70bfd2ec48645f3b3 |
| container_end_page | 139 |
| container_issue | 3 |
| container_start_page | 133 |
| container_title | Molecular biology reports |
| container_volume | 32 |
| creator | Goo, Tae Won Park, Soojung Jin, Byung Rae Yun, Eun Young Kim, Iksoo Nho, Si-Kab Kang, Seok-Woo Kwon, O-Yu |
| description | We isolated a calreticulin cDNA from the silkworm, Bombyx mori. The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology with calreticulin from G. mellonella (88%), A. aegypti (71%), D. melanogaster (69%) and H. sapiens (63%). The highest level of mRNA expression of B. mori calreticulin was exhibited in the fat body of this insect. Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin. |
| doi_str_mv | 10.1007/s11033-004-5908-7 |
| format | article |
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The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology with calreticulin from G. mellonella (88%), A. aegypti (71%), D. melanogaster (69%) and H. sapiens (63%). The highest level of mRNA expression of B. mori calreticulin was exhibited in the fat body of this insect. Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-004-5908-7</identifier><identifier>PMID: 16172913</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Bombyx - genetics ; Bombyx - metabolism ; Bombyx mori ; Calreticulin - biosynthesis ; Calreticulin - genetics ; Endoplasmic Reticulum - drug effects ; Endoplasmic Reticulum - physiology ; Insect Proteins - biosynthesis ; Insect Proteins - genetics ; Molecular Sequence Data ; Phylogeny ; Proteins ; RNA, Messenger - metabolism ; Sequence Alignment</subject><ispartof>Molecular biology reports, 2005-09, Vol.32 (3), p.133-139</ispartof><rights>Springer 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-decbbc02b8c306672db09decd5f2317c74fccb7039af449e70bfd2ec48645f3b3</citedby><cites>FETCH-LOGICAL-c357t-decbbc02b8c306672db09decd5f2317c74fccb7039af449e70bfd2ec48645f3b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16172913$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goo, Tae Won</creatorcontrib><creatorcontrib>Park, Soojung</creatorcontrib><creatorcontrib>Jin, Byung Rae</creatorcontrib><creatorcontrib>Yun, Eun Young</creatorcontrib><creatorcontrib>Kim, Iksoo</creatorcontrib><creatorcontrib>Nho, Si-Kab</creatorcontrib><creatorcontrib>Kang, Seok-Woo</creatorcontrib><creatorcontrib>Kwon, O-Yu</creatorcontrib><title>Endoplasmic reticulum stress response of Bombyx mori calreticulin</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><description>We isolated a calreticulin cDNA from the silkworm, Bombyx mori. The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology with calreticulin from G. mellonella (88%), A. aegypti (71%), D. melanogaster (69%) and H. sapiens (63%). The highest level of mRNA expression of B. mori calreticulin was exhibited in the fat body of this insect. Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Bombyx - genetics</subject><subject>Bombyx - metabolism</subject><subject>Bombyx mori</subject><subject>Calreticulin - biosynthesis</subject><subject>Calreticulin - genetics</subject><subject>Endoplasmic Reticulum - drug effects</subject><subject>Endoplasmic Reticulum - physiology</subject><subject>Insect Proteins - biosynthesis</subject><subject>Insect Proteins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Proteins</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Alignment</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkU9LxDAQxYMo7rr6AbxI8eAtOtMkTXtcl_UPLHjRc2jSFLq0TU1a0G9vli0IXjwNPH7zmDePkGuEewSQDwERGKMAnIoCcipPyBKFZJQXMj8lS2CAlOcCF-QihD1EEKU4JwvMUKYFsiVZb_vKDW0ZusYk3o6NmdqpS8LobQhRCIPrg01cnTy6Tn9_JZ3zTWLKdmab_pKc1WUb7NU8V-Tjafu-eaG7t-fXzXpHDRNypJU1WhtIdW4YZJlMKw1FFCtRpwylkbw2RktgRVlzXlgJuq5Sa3iecVEzzVbk7ug7ePc52TCqrgnGtm3ZWzcFleUZsJjrXxAlFlxGeEVu_4B7N_k-hlCSc0gRuYgQHiHjXQje1mrwTVf6b4WgDi2oYwsqPlcdWlCHC25m40l3tvrdmN_OfgBALoLQ</recordid><startdate>200509</startdate><enddate>200509</enddate><creator>Goo, Tae Won</creator><creator>Park, Soojung</creator><creator>Jin, Byung Rae</creator><creator>Yun, Eun Young</creator><creator>Kim, Iksoo</creator><creator>Nho, Si-Kab</creator><creator>Kang, Seok-Woo</creator><creator>Kwon, O-Yu</creator><general>Springer Nature B.V</general><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>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7SS</scope><scope>7X8</scope></search><sort><creationdate>200509</creationdate><title>Endoplasmic reticulum stress response of Bombyx mori calreticulin</title><author>Goo, Tae Won ; Park, Soojung ; Jin, Byung Rae ; Yun, Eun Young ; Kim, Iksoo ; Nho, Si-Kab ; Kang, Seok-Woo ; Kwon, O-Yu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-decbbc02b8c306672db09decd5f2317c74fccb7039af449e70bfd2ec48645f3b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Bombyx - genetics</topic><topic>Bombyx - metabolism</topic><topic>Bombyx mori</topic><topic>Calreticulin - biosynthesis</topic><topic>Calreticulin - genetics</topic><topic>Endoplasmic Reticulum - drug effects</topic><topic>Endoplasmic Reticulum - physiology</topic><topic>Insect Proteins - biosynthesis</topic><topic>Insect Proteins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Proteins</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goo, Tae Won</creatorcontrib><creatorcontrib>Park, Soojung</creatorcontrib><creatorcontrib>Jin, Byung Rae</creatorcontrib><creatorcontrib>Yun, Eun Young</creatorcontrib><creatorcontrib>Kim, Iksoo</creatorcontrib><creatorcontrib>Nho, Si-Kab</creatorcontrib><creatorcontrib>Kang, Seok-Woo</creatorcontrib><creatorcontrib>Kwon, O-Yu</creatorcontrib><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>Nucleic Acids Abstracts</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</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>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Science Database</collection><collection>Biological Science Database</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>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goo, Tae Won</au><au>Park, Soojung</au><au>Jin, Byung Rae</au><au>Yun, Eun Young</au><au>Kim, Iksoo</au><au>Nho, Si-Kab</au><au>Kang, Seok-Woo</au><au>Kwon, O-Yu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endoplasmic reticulum stress response of Bombyx mori calreticulin</atitle><jtitle>Molecular biology reports</jtitle><addtitle>Mol Biol Rep</addtitle><date>2005-09</date><risdate>2005</risdate><volume>32</volume><issue>3</issue><spage>133</spage><epage>139</epage><pages>133-139</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>We isolated a calreticulin cDNA from the silkworm, Bombyx mori. The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology with calreticulin from G. mellonella (88%), A. aegypti (71%), D. melanogaster (69%) and H. sapiens (63%). The highest level of mRNA expression of B. mori calreticulin was exhibited in the fat body of this insect. Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>16172913</pmid><doi>10.1007/s11033-004-5908-7</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0301-4851 |
| ispartof | Molecular biology reports, 2005-09, Vol.32 (3), p.133-139 |
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| source | Springer Nature |
| subjects | Amino Acid Sequence Animals Base Sequence Bombyx - genetics Bombyx - metabolism Bombyx mori Calreticulin - biosynthesis Calreticulin - genetics Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - physiology Insect Proteins - biosynthesis Insect Proteins - genetics Molecular Sequence Data Phylogeny Proteins RNA, Messenger - metabolism Sequence Alignment |
| title | Endoplasmic reticulum stress response of Bombyx mori calreticulin |
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