Cargando…
Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein
The extensible byssus is produced by the foot of bivalve animals, including the pearl oyster Pinctada fucata, 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, co...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4597212/ https://www.ncbi.nlm.nih.gov/pubmed/26446436 http://dx.doi.org/10.1038/srep15018 |
_version_ | 1782393885677322240 |
---|---|
author | Liu, Chuang Li, Shiguo Huang, Jingliang Liu, Yangjia Jia, Ganchu Xie, Liping Zhang, Rongqing |
author_facet | Liu, Chuang Li, Shiguo Huang, Jingliang Liu, Yangjia Jia, Ganchu Xie, Liping Zhang, Rongqing |
author_sort | Liu, Chuang |
collection | PubMed |
description | The extensible byssus is produced by the foot of bivalve animals, including the pearl oyster Pinctada fucata, 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 P. fucata byssus using electron microscopy, elemental analysis, proteomics and mechanical testing. In contrast to the microstructures of Mytilus sp. byssus, the P. fucata byssus has an exterior cuticle without granules and an inner core with nanocavities. The removal of Ca(2+) by ethylenediaminetetraacetic acid (EDTA) treatment expands the nanocavities and reduces the extensibility of the byssus, which is accompanied by a decrease in the β-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. |
format | Online Article Text |
id | pubmed-4597212 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-45972122015-10-13 Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein Liu, Chuang Li, Shiguo Huang, Jingliang Liu, Yangjia Jia, Ganchu Xie, Liping Zhang, Rongqing Sci Rep Article The extensible byssus is produced by the foot of bivalve animals, including the pearl oyster Pinctada fucata, 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 P. fucata byssus using electron microscopy, elemental analysis, proteomics and mechanical testing. In contrast to the microstructures of Mytilus sp. byssus, the P. fucata byssus has an exterior cuticle without granules and an inner core with nanocavities. The removal of Ca(2+) by ethylenediaminetetraacetic acid (EDTA) treatment expands the nanocavities and reduces the extensibility of the byssus, which is accompanied by a decrease in the β-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. Nature Publishing Group 2015-10-08 /pmc/articles/PMC4597212/ /pubmed/26446436 http://dx.doi.org/10.1038/srep15018 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Liu, Chuang Li, Shiguo Huang, Jingliang Liu, Yangjia Jia, Ganchu Xie, Liping Zhang, Rongqing Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title | Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title_full | Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title_fullStr | Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title_full_unstemmed | Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title_short | Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
title_sort | extensible byssus of pinctada fucata: ca(2+)-stabilized nanocavities and a thrombospondin-1 protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4597212/ https://www.ncbi.nlm.nih.gov/pubmed/26446436 http://dx.doi.org/10.1038/srep15018 |
work_keys_str_mv | AT liuchuang extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT lishiguo extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT huangjingliang extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT liuyangjia extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT jiaganchu extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT xieliping extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein AT zhangrongqing extensiblebyssusofpinctadafucataca2stabilizednanocavitiesandathrombospondin1protein |