N40, a Novel Nonacidic Matrix Protein from Pearl Oyster Nacre, Facilitates Nucleation of Aragonite in Vitro

Yan, Zhenguang; Gu, Jie; Gong, Na; Li, Changzhong; Zhou, Yujuan; Xie, Liping; Zhang, Rongqing

doi:10.1021/bm0701494

Cited by 57 publications

(50 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After day 5, the number of CaCO 3 aragonites around the nucleus increased until the aragonites formed a smooth surface. During the middle stages (days [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20], the carbon content decreased, as did the organic matrix and the baseline Raman spectrum. In previous studies, the CaCO 3 first deposited on the nucleus was the aragonitic [29] or calcitic [30] prismatic layer found in the cross section of the pearl, and the nacreous layer then formed on the prismatic layer.…”

Section: Discussion (A) the Pearl Formation Processmentioning

confidence: 99%

The role of matrix proteins in the control of nacreous layer deposition during pearl formation

Liu

Xiang

et al. 2011

Proc. R. Soc. B.

Self Cite

View full text Add to dashboard Cite

To study the function of pearl oyster matrix proteins in nacreous layer biomineralization in vivo, we examined the deposition on pearl nuclei and the expression of matrix protein genes in the pearl sac during the early stage of pearl formation. We found that the process of pearl formation involves two consecutive stages: (i) irregular calcium carbonate (CaCO 3 ) deposition on the bare nucleus and (ii) CaCO 3 deposition that becomes more and more regular until the mature nacreous layer has formed on the nucleus. The low-expression level of matrix proteins in the pearl sac during periods of irregular CaCO 3 deposition suggests that deposition may not be controlled by the organic matrix during this stage of the process. However, significant expression of matrix proteins in the pearl sac was detected by day 30 -35 after implantation. On day 30, a thin layer of CaCO 3 , which we believe was amorphous CaCO 3 , covered large aragonites. By day 35, the nacreous layer had formed. The whole process is similar to that observed in shells, and the temporal expression of matrix protein genes indicated that their bioactivities were crucial for pearl development. Matrix proteins controlled the crystal phase, shape, size, nucleation and aggregation of CaCO 3 crystals.

show abstract

Section: Discussion (A) the Pearl Formation Processmentioning

confidence: 99%

The role of matrix proteins in the control of nacreous layer deposition during pearl formation

Liu

Xiang

et al. 2011

Proc. R. Soc. B.

Self Cite

View full text Add to dashboard Cite

show abstract

“…5, Prisilkin-39 was only detected in the EISM but not in the ESM of the shell. According to previous reports on matrix proteins (47)(48)(49)(50), EISM proteins were conventionally believed to be responsible for the construction of the structural organic framework and the physical properties of the shell during calcification. Therefore, it is logical to assume that Prisilkin-39 exists as a framework component in the prismatic shell layer considering its presence pattern and amino acid composition (Gly/Tyr-rich).…”

Section: Characterization Of Deduced Amino Acid Sequence Ofmentioning

confidence: 99%

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

Kong

Yan

et al. 2009

Journal of Biological Chemistry

Self Cite

101

View full text Add to dashboard Cite

Molluscs form their shells out of CaCO 3 and a matrix of biomacromolecules. Understanding the role of matrices may shed some light on the mechanism of biomineralization. Here, a 1401-bp full-length cDNA sequence encoding a novel matrix protein was cloned from the mantle of the bivalve oyster, Pinctada fucata. The deduced protein (Prisilkin-39), which has a molecular mass of 39.3 kDa and an isoelectric point of 8.83, was fully characterized, and its role in biomineralization was demonstrated using both in vivo and in vitro crystal growth assays. Prisilkin-39 is a highly repetitive protein with an unusual composition of Gly, Tyr, and Ser residues. Expression of Prisilkin-39 was localized to columnar epithelial cells of the mantle edge, corresponding to the calcitic prismatic layer formation. Immunostaining in situ and immunodetection in vitro revealed the presence of a characteristic pattern of Prisilkin-39 in the organic sheet and in sheaths around the prisms. Prisilkin-39 binds tightly with chitin, an insoluble polysaccharide that forms the highly structured framework of the shell. Antibody injection in vivo resulted in dramatic morphological deformities in the inner shell surface structure, where large amounts of CaCO 3 were deposited in an uncontrolled manner. Moreover, Prisilkin-39 strictly prohibited the precipitation of aragonite in vitro. Taken together, Prisilkin-39 is the first protein shown to have dual function, involved both in the chitinous framework building and in crystal growth regulation during the prismatic layer mineralization. These observations may extend our view on the rare group of basic matrices and their functions during elaboration of the molluscan shell.

show abstract

“…For aragonite, what we must draw from are studies conducted with mollusk shell nacre-associated protein sequences [34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][50][51]. For in vitro-based studies, several different carbonate-based assays have been used to achieve supersaturation conditions necessary for calcium carbonate crystal growth, with no control over pH, and the duration of these nucleation experiments were variable (i.e., from several hours up to 7 days) [36,38,39,[41][42][43][44][46][47][48][49][50][51].…”

Section: Protein-polymorph Formation and Stabilization-what Do We Curmentioning

confidence: 99%

“…For in vitro-based studies, several different carbonate-based assays have been used to achieve supersaturation conditions necessary for calcium carbonate crystal growth, with no control over pH, and the duration of these nucleation experiments were variable (i.e., from several hours up to 7 days) [36,38,39,[41][42][43][44][46][47][48][49][50][51]. Further, some studies utilized Mg(II) ions in the assay mixture to mimic seawater conditions and promote and stabilize aragonite [36,44].…”

Section: Protein-polymorph Formation and Stabilization-what Do We Curmentioning

confidence: 99%

“…Second, and perhaps most importantly, genomic and proteomic studies of biomineralization proteins have uncovered a vast repertory of proteins [6][7][8]13,14,[26][27][28] that could potentially manage many aspects of proposed nucleation processes, including polymorphism. However, although many protein studies have confirmed that polymorphs do form when proteins are present [34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][50][51][52][53], these studies have not provided information that is needed for detailing the mechanisms of polymorph formation, or, have utilized a variety of testing methods that prevent cross-comparisons of datasets necessary for mechanism building [34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][50][51]…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Polymorphs, Proteins, and Nucleation Theory: A Critical Analysis

Evans

2017

Minerals

View full text Add to dashboard Cite

Over the last eight years new theories regarding nucleation, crystal growth, and polymorphism have emerged. Many of these theories were developed in response to observations in nature, where classical nucleation theory failed to account for amorphous mineral precursors, phases, and particle assembly processes that are responsible for the formation of invertebrate mineralized skeletal elements, such as the mollusk shell nacre layer (aragonite polymorph) and the sea urchin spicule (calcite polymorph). Here, we summarize these existing nucleation theories and place them within the context of what we know about biomineralization proteins, which are likely participants in the management of mineral precursor formation, stabilization, and assembly into polymorphs. With few exceptions, much of the protein literature confirms that polymorph-specific proteins, such as those from mollusk shell nacre aragonite, can promote polymorph formation. However, past studies fail to provide important mechanistic insights into this process, owing to variations in techniques, methodologies, and the lack of standardization in mineral assay experimentation. We propose that the way forward past this roadblock is for the protein community to adopt standardized nucleation assays and approaches that are compatible with current and emerging nucleation precursor studies. This will allow cross-comparisons, kinetic observations, and hopefully provide the information that will explain how proteins manage polymorph formation and stabilization.

show abstract

N40, a Novel Nonacidic Matrix Protein from Pearl Oyster Nacre, Facilitates Nucleation of Aragonite in Vitro

Cited by 57 publications

References 37 publications

The role of matrix proteins in the control of nacreous layer deposition during pearl formation

The role of matrix proteins in the control of nacreous layer deposition during pearl formation

Cloning and Characterization of Prisilkin-39, a Novel Matrix Protein Serving a Dual Role in the Prismatic Layer Formation from the Oyster Pinctada fucata

Polymorphs, Proteins, and Nucleation Theory: A Critical Analysis

Contact Info

Product

Resources

About