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Characterization of silk spun by the embiopteran, Antipaluria urichi
Silks are renowned for being lightweight materials with impressive mechanical properties. Though moth and spider silks have received the most study, silk production has evolved in many other arthropods. One insect group that has been little investigated is Embioptera (webspinners). Embiopterans prod...
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Published in: | Insect biochemistry and molecular biology 2009-02, Vol.39 (2), p.75-82 |
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creator | Collin, Matthew A. Garb, Jessica E. Edgerly, Janice S. Hayashi, Cheryl Y. |
description | Silks are renowned for being lightweight materials with impressive mechanical properties. Though moth and spider silks have received the most study, silk production has evolved in many other arthropods. One insect group that has been little investigated is Embioptera (webspinners). Embiopterans produce silk from unique tarsal spinning structures during all life stages. We characterize the molecular and mechanical properties of
Antipaluria urichi (Embioptera) silk through multiple approaches. First, we quantify the number of silk secretory structures on their forelimbs and the tensile properties of
Antipaluria silk. Second, we present silk protein (fibroin) transcripts from an embiopteran forelimb protarsomere cDNA library. We describe a fibroin that shares several features with other arthropod silks, including a subrepetitive core region, a non-repetitive carboxyl-terminal sequence, and a composition rich in glycine, alanine, and serine. Despite these shared attributes, embiopteran silk has several different tensile properties compared to previously measured silks. For example, the tensile strength of
Antipaluria silk is much lower than that of
Bombyx mori silk. We discuss the observed mechanical properties in relation to the fibroin sequence, spinning system, and embiopteran silk use. |
doi_str_mv | 10.1016/j.ibmb.2008.10.004 |
format | article |
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Antipaluria urichi (Embioptera) silk through multiple approaches. First, we quantify the number of silk secretory structures on their forelimbs and the tensile properties of
Antipaluria silk. Second, we present silk protein (fibroin) transcripts from an embiopteran forelimb protarsomere cDNA library. We describe a fibroin that shares several features with other arthropod silks, including a subrepetitive core region, a non-repetitive carboxyl-terminal sequence, and a composition rich in glycine, alanine, and serine. Despite these shared attributes, embiopteran silk has several different tensile properties compared to previously measured silks. For example, the tensile strength of
Antipaluria silk is much lower than that of
Bombyx mori silk. We discuss the observed mechanical properties in relation to the fibroin sequence, spinning system, and embiopteran silk use.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/j.ibmb.2008.10.004</identifier><identifier>PMID: 18996196</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>amino acid composition ; Amino Acid Sequence ; amino acid sequences ; animal anatomy ; Animals ; Antipaluria urichi ; Araneae ; Arthropoda ; Base Sequence ; Biomechanics ; Bombyx mori ; cDNA ; complementary DNA ; Embioptera ; Fibroin ; fibroins ; forelimbs ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Insecta - chemistry ; Insecta - genetics ; Insecta - metabolism ; mechanical properties ; messenger RNA ; Molecular Sequence Data ; nucleotide sequences ; Sequence Alignment ; Silk ; Silk - chemistry ; Silk - genetics ; Silk - metabolism ; Silk glands ; silk proteins ; Tensile Strength ; Webspinner</subject><ispartof>Insect biochemistry and molecular biology, 2009-02, Vol.39 (2), p.75-82</ispartof><rights>2008 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-820e6aaa3f7c0f79c0c9fff22b3a595e9c2e430561acb39cad296dec0c4f8dd73</citedby><cites>FETCH-LOGICAL-c409t-820e6aaa3f7c0f79c0c9fff22b3a595e9c2e430561acb39cad296dec0c4f8dd73</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/18996196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Collin, Matthew A.</creatorcontrib><creatorcontrib>Garb, Jessica E.</creatorcontrib><creatorcontrib>Edgerly, Janice S.</creatorcontrib><creatorcontrib>Hayashi, Cheryl Y.</creatorcontrib><title>Characterization of silk spun by the embiopteran, Antipaluria urichi</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>Silks are renowned for being lightweight materials with impressive mechanical properties. Though moth and spider silks have received the most study, silk production has evolved in many other arthropods. One insect group that has been little investigated is Embioptera (webspinners). Embiopterans produce silk from unique tarsal spinning structures during all life stages. We characterize the molecular and mechanical properties of
Antipaluria urichi (Embioptera) silk through multiple approaches. First, we quantify the number of silk secretory structures on their forelimbs and the tensile properties of
Antipaluria silk. Second, we present silk protein (fibroin) transcripts from an embiopteran forelimb protarsomere cDNA library. We describe a fibroin that shares several features with other arthropod silks, including a subrepetitive core region, a non-repetitive carboxyl-terminal sequence, and a composition rich in glycine, alanine, and serine. Despite these shared attributes, embiopteran silk has several different tensile properties compared to previously measured silks. For example, the tensile strength of
Antipaluria silk is much lower than that of
Bombyx mori silk. We discuss the observed mechanical properties in relation to the fibroin sequence, spinning system, and embiopteran silk use.</description><subject>amino acid composition</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>animal anatomy</subject><subject>Animals</subject><subject>Antipaluria urichi</subject><subject>Araneae</subject><subject>Arthropoda</subject><subject>Base Sequence</subject><subject>Biomechanics</subject><subject>Bombyx mori</subject><subject>cDNA</subject><subject>complementary DNA</subject><subject>Embioptera</subject><subject>Fibroin</subject><subject>fibroins</subject><subject>forelimbs</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Insecta - chemistry</subject><subject>Insecta - genetics</subject><subject>Insecta - metabolism</subject><subject>mechanical properties</subject><subject>messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequences</subject><subject>Sequence Alignment</subject><subject>Silk</subject><subject>Silk - chemistry</subject><subject>Silk - genetics</subject><subject>Silk - metabolism</subject><subject>Silk glands</subject><subject>silk proteins</subject><subject>Tensile Strength</subject><subject>Webspinner</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkE2LFDEQhoMo7rj6BzxonzzZYyXpTjrgZRk_YcGD7jlUpytOxv4y6RbWX2-aGfCmlyoonveleBh7zmHPgas3p31oh3YvAJp82ANUD9iON9qUICp4yHZgVF1yXTVX7ElKJ8hEVevH7Io3xihu1I69Oxwxolsoht-4hGksJl-k0P8o0ryORXtfLEcqaGjDNGcIx9fFzbiEGfs1BizycMfwlD3y2Cd6dtnX7O7D-2-HT-Xtl4-fDze3pavALGUjgBQiSq8deG0cOOO9F6KVWJuajBNUSagVR9dK47ATRnWUsco3XaflNXt17p3j9HOltNghJEd9jyNNa7JKGS1lzf8LCpBa60pkUJxBF6eUInk7xzBgvLcc7CbZnuwm2W6St1tWmEMvLu1rO1D3N3KxmoGXZ8DjZPF7DMnefRXAZS7kIPRGvD0TlHX9ChRtcoFGR12I5BbbTeFfH_wBwn2XVg</recordid><startdate>20090201</startdate><enddate>20090201</enddate><creator>Collin, Matthew A.</creator><creator>Garb, Jessica E.</creator><creator>Edgerly, Janice S.</creator><creator>Hayashi, Cheryl Y.</creator><general>Elsevier Ltd</general><scope>FBQ</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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20090201</creationdate><title>Characterization of silk spun by the embiopteran, Antipaluria urichi</title><author>Collin, Matthew A. ; Garb, Jessica E. ; Edgerly, Janice S. ; Hayashi, Cheryl Y.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-820e6aaa3f7c0f79c0c9fff22b3a595e9c2e430561acb39cad296dec0c4f8dd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>amino acid composition</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>animal anatomy</topic><topic>Animals</topic><topic>Antipaluria urichi</topic><topic>Araneae</topic><topic>Arthropoda</topic><topic>Base Sequence</topic><topic>Biomechanics</topic><topic>Bombyx mori</topic><topic>cDNA</topic><topic>complementary DNA</topic><topic>Embioptera</topic><topic>Fibroin</topic><topic>fibroins</topic><topic>forelimbs</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Insecta - chemistry</topic><topic>Insecta - genetics</topic><topic>Insecta - metabolism</topic><topic>mechanical properties</topic><topic>messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequences</topic><topic>Sequence Alignment</topic><topic>Silk</topic><topic>Silk - chemistry</topic><topic>Silk - genetics</topic><topic>Silk - metabolism</topic><topic>Silk glands</topic><topic>silk proteins</topic><topic>Tensile Strength</topic><topic>Webspinner</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Collin, Matthew A.</creatorcontrib><creatorcontrib>Garb, Jessica E.</creatorcontrib><creatorcontrib>Edgerly, Janice S.</creatorcontrib><creatorcontrib>Hayashi, Cheryl Y.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Collin, Matthew A.</au><au>Garb, Jessica E.</au><au>Edgerly, Janice S.</au><au>Hayashi, Cheryl Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of silk spun by the embiopteran, Antipaluria urichi</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2009-02-01</date><risdate>2009</risdate><volume>39</volume><issue>2</issue><spage>75</spage><epage>82</epage><pages>75-82</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>Silks are renowned for being lightweight materials with impressive mechanical properties. Though moth and spider silks have received the most study, silk production has evolved in many other arthropods. One insect group that has been little investigated is Embioptera (webspinners). Embiopterans produce silk from unique tarsal spinning structures during all life stages. We characterize the molecular and mechanical properties of
Antipaluria urichi (Embioptera) silk through multiple approaches. First, we quantify the number of silk secretory structures on their forelimbs and the tensile properties of
Antipaluria silk. Second, we present silk protein (fibroin) transcripts from an embiopteran forelimb protarsomere cDNA library. We describe a fibroin that shares several features with other arthropod silks, including a subrepetitive core region, a non-repetitive carboxyl-terminal sequence, and a composition rich in glycine, alanine, and serine. Despite these shared attributes, embiopteran silk has several different tensile properties compared to previously measured silks. For example, the tensile strength of
Antipaluria silk is much lower than that of
Bombyx mori silk. We discuss the observed mechanical properties in relation to the fibroin sequence, spinning system, and embiopteran silk use.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>18996196</pmid><doi>10.1016/j.ibmb.2008.10.004</doi><tpages>8</tpages></addata></record> |
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subjects | amino acid composition Amino Acid Sequence amino acid sequences animal anatomy Animals Antipaluria urichi Araneae Arthropoda Base Sequence Biomechanics Bombyx mori cDNA complementary DNA Embioptera Fibroin fibroins forelimbs Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - metabolism Insecta - chemistry Insecta - genetics Insecta - metabolism mechanical properties messenger RNA Molecular Sequence Data nucleotide sequences Sequence Alignment Silk Silk - chemistry Silk - genetics Silk - metabolism Silk glands silk proteins Tensile Strength Webspinner |
title | Characterization of silk spun by the embiopteran, Antipaluria urichi |
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