Identification of nacre matrix protein genes hic14 and hic19 and their roles in crystal growth and pearl formation in the mussel Hyriopsis cumingii

2019 ◽  
Vol 66 (4) ◽  
pp. 545-554
Author(s):  
Can Jin ◽  
Hong‐Yu Ren ◽  
Jing‐Wen Pu ◽  
Xiao‐Jun Liu ◽  
Jia‐Le Li
Keyword(s):  
Crystal Growth ◽  
Matrix Protein ◽  
Hyriopsis Cumingii ◽  
Pearl Formation

A novel nacre matrix protein hic24 in Hyriopsis cumingii is essential for calcium carbonate nucleation and involved in pearl formation

2018 ◽  
Vol 66 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Xiaojun Liu ◽  
Zhenming Liu ◽  
Can Jin ◽  
Haoran Li ◽  
Jia-Le Li
Keyword(s):  
Calcium Carbonate ◽  
Matrix Protein ◽  
Hyriopsis Cumingii ◽  
Pearl Formation

scholarly journals Hic74, a novel alanine and glycine rich matrix protein related to nacreous layer formation in the mollusc Hyriopsis cumingii

2017 ◽  
Vol 2 (3) ◽  
pp. 119-123 ◽  
Author(s):  
Xiaojun Liu ◽  
Can Jin ◽  
Leiming Wu ◽  
Shaojian Dong ◽  
Shimei Zeng ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Nacreous Layer ◽  
Layer Formation ◽  
Hyriopsis Cumingii

Proteins From Oyster Shell: Biomineralization Regulators and Commercial Polymer Analogs

1999 ◽  
Vol 599 ◽  
Author(s):  
A. P. Wheeler ◽  
C. S. Sikes
Keyword(s):  
Crystal Growth ◽  
Aspartic Acid ◽  
Large Scale ◽  
Matrix Protein ◽  
Gene Families ◽  
Eastern Oyster ◽  
Matrix Proteins ◽  
The Matrix

AbstractMolluscan shell is a composite made up of μm-sized CaCO3 crystals and an organic phase (matrix). This report outlines our studies on the structure and activities of matrix proteins isolated from the inner calcite layer of shell of the Eastern oyster, including their cellular origin and structure and their relationship to the crystalline mineral phase. In addition, we present results of the synthesis and commercialization of polypeptide polymers which are based on the structure and activities of the oyster proteins. Extracted shell proteins are polyanionic and range in size from relatively small soluble forms to those which are crosslinked and insoluble. The soluble forms are capable of adsorbing to calcite in vitro and in the process changing its growth habit and acting as threshold growth inhibitors. Their function in vivo is not understood, but they may serve to control shell crystal morphology. The insoluble protein forms gels readily and may serve to provide resiliency to the shell and, from in vitro and in situ observations, appears to serve as a site for nucleation of crystals. However, from studies in vitro, these gels do not lower the energy of activation for nucleation, as previously expected. Matrix protein aggregates are identifiable by AFM on the surface of crystals, but as such do not serve as nucleation sites for new crystal growth. If the aggregates are removed, then ectopic crystal growth proceeds readily revealing orientation of the underlying crystals. All the matrix proteins contain domains rich in aspartic acid, are heavily phosphorylated, crossreact in antibody studies and may belong to a limited number of gene families with individuals modified post-synthesis. The proteins are made by a specialized group of cells located primarily some distance from the growing edge of the shell and appear to be assembled into sheets soon after secretion. Soluble anti-scalants and crosslinked insoluble water absorbents have been developed based on the structure and activity of the matrix proteins. These are primarily poly(aspartates) which can be made in large scale via thermal polycondensation of aspartic acid. The soluble forms are commercially used as biodegradable water treatment chemicals among other applications.

Sign in / Sign up

Export Citation Format

Share Document