{"refrec":{"BRefID":250547,"RR":"<b>Liu, C.; Li, S.; Huang, J.; Liu, Y.; Jia, G.; Xie, L.; Zhang, R.</b> (2015). Extensible byssus of <i>Pinctada fucata</i>: Ca<sup>2+</sup>-stabilized nanocavities and a thrombospondin-1 protein. <i>NPG Scientific Reports 5(15018)</i>: 13 pp. <a href=\"http://dx.doi.org/10.1038/srep15018\" target=\"_blank\">http://dx.doi.org/10.1038/srep15018</a>","BEntID":242241,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>NPG Scientific Reports 5(15018)</i>: 13 pp. <a href=\"http://dx.doi.org/10.1038/srep15018\" target=\"_blank\">http://dx.doi.org/10.1038/srep15018</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Liu, C.; Li, S.; Huang, J.; Liu, Y.; Jia, G.; Xie, L.; Zhang, R.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Liu, C. <i>et al.</i>","Englishabstract":"The extensible byssus is produced by the foot of bivalve animals, including the pearl oyster <i>Pinctada fucata,</i> and enables them to attach to hard underwater surfaces. However, the mechanism of their extensibility is not well understood. To understand this mechanism, we analyzed the ultrastructure, composition and mechanical properties of the <i>P. fucata</i> byssus using electron microscopy, elemental analysis, proteomics and mechanical testing. In contrast to the microstructures of <i>Mytilus sp.</i> byssus, the <i>P. fucata</i> byssus has an exterior cuticle without granules and an inner core with nanocavities. The removal of Ca<sup>2+</sup> by ethylenediaminetetraacetic acid (EDTA) treatment expands the nanocavities and reduces the extensibility of the byssus, which is accompanied by a decrease in the ß-sheet conformation of byssal proteins. Through proteomic methods, several proteins with antioxidant and anti-corrosive properties were identified as the main components of the distal byssus regions. Specifically, a protein containing thrombospondin-1 (TSP-1), which is highly expressed in the foot, is hypothesized to be responsible for byssus extensibility. Together, our findings demonstrate the importance of inorganic ions and multiple proteins for bivalve byssus extension, which could guide the future design of biomaterials for use in seawater.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Extensible byssus of <i>Pinctada fucata</i>: Ca<sup>2+</sup>-stabilized nanocavities and a thrombospondin-1 protein","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-15 01:32:45.284209","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2015,"MonPub":null,"DateUpdate":"2018-02-13","DateCreate":"2015-10-16","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000362418700002","VABBcode":null,"OpenAcc":1,"DOI":"10.1038/srep15018"},"refs":null,"anarec":{"AnaID":250547,"PubliDate":2015,"Pagination":"13 pp","XtraPublOfAnaID":null,"ISBN":null,"Volume":"5","Issue":"15018","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":208093,"SerRR":"Scientific Reports (Nature Publishing Group). 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