A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation
Sericin is the silk protein enveloping fibroin fibers in cocoons. Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation; the activity depends on the repeats of 38 amino acids. A partial peptide from the 38 residues, SGGSSTYGYS, inhibited serum-deprivation deat...
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Veröffentlicht in: | Biotechnology letters 2005-07, Vol.27 (13), p.893-897 |
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creator | TAKAHASHI, Masakazu TSUJIMOTO, Kazuhisa KATO, Youichi YAMADA, Hideyuki TAKAGI, Hiroshi NAKAMORI, Shigeru |
description | Sericin is the silk protein enveloping fibroin fibers in cocoons. Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation; the activity depends on the repeats of 38 amino acids. A partial peptide from the 38 residues, SGGSSTYGYS, inhibited serum-deprivation death as well. Cell viabilities in the presence of 10% (v/v) foetal calf serum, no additives and 1 mM: SGGSSTYGYS were 96, 12 and 31% on the third day after inoculation, respectively. Aromatic residues seemed to be important because SGGSSTWGWS had the same activity as SGGSSTYGYS but SGGSSTAGAS had no activity. |
doi_str_mv | 10.1007/s10529-005-7177-5 |
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Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation; the activity depends on the repeats of 38 amino acids. A partial peptide from the 38 residues, SGGSSTYGYS, inhibited serum-deprivation death as well. Cell viabilities in the presence of 10% (v/v) foetal calf serum, no additives and 1 mM: SGGSSTYGYS were 96, 12 and 31% on the third day after inoculation, respectively. Aromatic residues seemed to be important because SGGSSTWGWS had the same activity as SGGSSTYGYS but SGGSSTAGAS had no activity.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-005-7177-5</identifier><identifier>PMID: 16091882</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Biological and medical sciences ; Biotechnology ; Cell Line ; Cell Proliferation - drug effects ; Cell Survival - drug effects ; Culture Media, Serum-Free - pharmacology ; Dose-Response Relationship, Drug ; Fibers ; Fundamental and applied biological sciences. Psychology ; Insects ; Molecular Sequence Data ; Mortality ; Peptide Fragments - pharmacology ; Proteins ; Sericins - chemistry ; Sericins - pharmacology ; Silk ; Spodoptera - cytology ; Spodoptera - drug effects ; Spodoptera frugiperda ; Time Factors</subject><ispartof>Biotechnology letters, 2005-07, Vol.27 (13), p.893-897</ispartof><rights>2005 INIST-CNRS</rights><rights>Springer 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-493dbbcbc6b9335d51c42fed750fa206f95d3fe724409090d584aa9bfb78d62a3</citedby><cites>FETCH-LOGICAL-c522t-493dbbcbc6b9335d51c42fed750fa206f95d3fe724409090d584aa9bfb78d62a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17062924$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16091882$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TAKAHASHI, Masakazu</creatorcontrib><creatorcontrib>TSUJIMOTO, Kazuhisa</creatorcontrib><creatorcontrib>KATO, Youichi</creatorcontrib><creatorcontrib>YAMADA, Hideyuki</creatorcontrib><creatorcontrib>TAKAGI, Hiroshi</creatorcontrib><creatorcontrib>NAKAMORI, Shigeru</creatorcontrib><title>A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><description>Sericin is the silk protein enveloping fibroin fibers in cocoons. Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation; the activity depends on the repeats of 38 amino acids. A partial peptide from the 38 residues, SGGSSTYGYS, inhibited serum-deprivation death as well. Cell viabilities in the presence of 10% (v/v) foetal calf serum, no additives and 1 mM: SGGSSTYGYS were 96, 12 and 31% on the third day after inoculation, respectively. Aromatic residues seemed to be important because SGGSSTWGWS had the same activity as SGGSSTYGYS but SGGSSTAGAS had no activity.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cell Line</subject><subject>Cell Proliferation - drug effects</subject><subject>Cell Survival - drug effects</subject><subject>Culture Media, Serum-Free - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Fibers</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Insects</subject><subject>Molecular Sequence Data</subject><subject>Mortality</subject><subject>Peptide Fragments - pharmacology</subject><subject>Proteins</subject><subject>Sericins - chemistry</subject><subject>Sericins - pharmacology</subject><subject>Silk</subject><subject>Spodoptera - cytology</subject><subject>Spodoptera - drug effects</subject><subject>Spodoptera frugiperda</subject><subject>Time Factors</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</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>eNqFkUtr3DAURkVpaCZpf0A3QQSSrNRePa-1DCEvCGSRdq3KehCHGXtq2YX8-8rMQKCLFC2uQOd-utIh5CuHbxwAvxcOWlgGoBlyRKY_kBXXKJlBNB_JCrjiTCsrDslRKS8AYBHwEznkBixvGrEivy5pSWMXup7FWv-kSLdpO3Ux0e04TClMhT5lS7u-1D0Nab0uNI_Dhsbkp2ca_FxqT_tKfZintITNy9m2ZvmpG_rP5CD7dUlf9vWY_Ly5_nF1xx4eb--vLh9Y0EJMTFkZ2za0wbRWSh01D0rkFFFD9gJMtjrKnFAoBbauqBvlvW1zi000wstjcrHLrWP_nlOZ3KYry7i-T8NcHCqpDCqtKnn-LmkaZYQG8V-QI-dWoq7g6T_gyzCPfX2uQ6kaVMou1_IdFMahlDFlV_9o48dXx8EtOt1Op6s63aLTLcEn--C53aT41rH3V4GzPeBL8Os8-j505Y1DMMIKJf8CbDSnIw</recordid><startdate>20050701</startdate><enddate>20050701</enddate><creator>TAKAHASHI, Masakazu</creator><creator>TSUJIMOTO, Kazuhisa</creator><creator>KATO, Youichi</creator><creator>YAMADA, Hideyuki</creator><creator>TAKAGI, Hiroshi</creator><creator>NAKAMORI, Shigeru</creator><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</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>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</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>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7QO</scope><scope>7SS</scope><scope>7X8</scope></search><sort><creationdate>20050701</creationdate><title>A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation</title><author>TAKAHASHI, Masakazu ; TSUJIMOTO, Kazuhisa ; KATO, Youichi ; YAMADA, Hideyuki ; TAKAGI, Hiroshi ; NAKAMORI, Shigeru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-493dbbcbc6b9335d51c42fed750fa206f95d3fe724409090d584aa9bfb78d62a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cell Line</topic><topic>Cell Proliferation - drug effects</topic><topic>Cell Survival - drug effects</topic><topic>Culture Media, Serum-Free - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Fibers</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Insects</topic><topic>Molecular Sequence Data</topic><topic>Mortality</topic><topic>Peptide Fragments - pharmacology</topic><topic>Proteins</topic><topic>Sericins - chemistry</topic><topic>Sericins - pharmacology</topic><topic>Silk</topic><topic>Spodoptera - cytology</topic><topic>Spodoptera - drug effects</topic><topic>Spodoptera frugiperda</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TAKAHASHI, Masakazu</creatorcontrib><creatorcontrib>TSUJIMOTO, Kazuhisa</creatorcontrib><creatorcontrib>KATO, Youichi</creatorcontrib><creatorcontrib>YAMADA, Hideyuki</creatorcontrib><creatorcontrib>TAKAGI, Hiroshi</creatorcontrib><creatorcontrib>NAKAMORI, Shigeru</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>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 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 One Sustainability</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>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>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering 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>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>TAKAHASHI, Masakazu</au><au>TSUJIMOTO, Kazuhisa</au><au>KATO, Youichi</au><au>YAMADA, Hideyuki</au><au>TAKAGI, Hiroshi</au><au>NAKAMORI, Shigeru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation</atitle><jtitle>Biotechnology letters</jtitle><addtitle>Biotechnol Lett</addtitle><date>2005-07-01</date><risdate>2005</risdate><volume>27</volume><issue>13</issue><spage>893</spage><epage>897</epage><pages>893-897</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>Sericin is the silk protein enveloping fibroin fibers in cocoons. Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation; the activity depends on the repeats of 38 amino acids. A partial peptide from the 38 residues, SGGSSTYGYS, inhibited serum-deprivation death as well. Cell viabilities in the presence of 10% (v/v) foetal calf serum, no additives and 1 mM: SGGSSTYGYS were 96, 12 and 31% on the third day after inoculation, respectively. Aromatic residues seemed to be important because SGGSSTWGWS had the same activity as SGGSSTYGYS but SGGSSTAGAS had no activity.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>16091882</pmid><doi>10.1007/s10529-005-7177-5</doi><tpages>5</tpages></addata></record> |
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subjects | Amino Acid Sequence Amino acids Animals Biological and medical sciences Biotechnology Cell Line Cell Proliferation - drug effects Cell Survival - drug effects Culture Media, Serum-Free - pharmacology Dose-Response Relationship, Drug Fibers Fundamental and applied biological sciences. Psychology Insects Molecular Sequence Data Mortality Peptide Fragments - pharmacology Proteins Sericins - chemistry Sericins - pharmacology Silk Spodoptera - cytology Spodoptera - drug effects Spodoptera frugiperda Time Factors |
title | A sericin-derived peptide protects Sf9 insect cells from death caused by acute serum deprivation |
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