A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation

Abstract Biomineralization, including shell formation, is dedicatedly regulated by matrix proteins. PfY2, a matrix protein detected in the ethylene diamine tetraacetic acid (EDTA)-soluble fraction from both prismatic layer and nacreous layer, was discovered by our group using microarray. It may play...

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Autores principales:	Yi Yan, Dong Yang, Xue Yang, Chuang Liu, Jun Xie, Guilan Zheng, Liping Xie, Rongqing Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eace077ec4274dbb8355cbc3553deca9
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spelling	oai:doaj.org-article:eace077ec4274dbb8355cbc3553deca92021-12-02T12:32:37ZA Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation10.1038/s41598-017-06375-w2045-2322https://doaj.org/article/eace077ec4274dbb8355cbc3553deca92017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06375-whttps://doaj.org/toc/2045-2322Abstract Biomineralization, including shell formation, is dedicatedly regulated by matrix proteins. PfY2, a matrix protein detected in the ethylene diamine tetraacetic acid (EDTA)-soluble fraction from both prismatic layer and nacreous layer, was discovered by our group using microarray. It may play dual roles during biomineralization. However, the molecular mechanism is still unclear. In this research, we studied the function of PfY2 on crystallization in vivo and in vitro, revealing that it might be a negative regulator during shell formation. Notching experiment indicated that PfY2 was involved in shell repairing and regenerating process. Repression of PfY2 gene affected the structure of prismatic and nacreous layer simultaneously, confirming its dual roles in shell formation. Recombinant protein rPfY2 significantly suppressed CaCO3 precipitation rate, participated in the crystal nucleation process, changed the morphology of crystals and inhibited the transformation of amorphous calcium carbonate (ACC) to stable calcite or aragonite in vitro. Our results may provide new evidence on the biomineralization inhibition process.Yi YanDong YangXue YangChuang LiuJun XieGuilan ZhengLiping XieRongqing ZhangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yi Yan Dong Yang Xue Yang Chuang Liu Jun Xie Guilan Zheng Liping Xie Rongqing Zhang A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
description	Abstract Biomineralization, including shell formation, is dedicatedly regulated by matrix proteins. PfY2, a matrix protein detected in the ethylene diamine tetraacetic acid (EDTA)-soluble fraction from both prismatic layer and nacreous layer, was discovered by our group using microarray. It may play dual roles during biomineralization. However, the molecular mechanism is still unclear. In this research, we studied the function of PfY2 on crystallization in vivo and in vitro, revealing that it might be a negative regulator during shell formation. Notching experiment indicated that PfY2 was involved in shell repairing and regenerating process. Repression of PfY2 gene affected the structure of prismatic and nacreous layer simultaneously, confirming its dual roles in shell formation. Recombinant protein rPfY2 significantly suppressed CaCO3 precipitation rate, participated in the crystal nucleation process, changed the morphology of crystals and inhibited the transformation of amorphous calcium carbonate (ACC) to stable calcite or aragonite in vitro. Our results may provide new evidence on the biomineralization inhibition process.
format	article
author	Yi Yan Dong Yang Xue Yang Chuang Liu Jun Xie Guilan Zheng Liping Xie Rongqing Zhang
author_facet	Yi Yan Dong Yang Xue Yang Chuang Liu Jun Xie Guilan Zheng Liping Xie Rongqing Zhang
author_sort	Yi Yan
title	A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
title_short	A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
title_full	A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
title_fullStr	A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
title_full_unstemmed	A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation
title_sort	novel matrix protein, pfy2, functions as a crucial macromolecule during shell formation
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/eace077ec4274dbb8355cbc3553deca9
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A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation

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