ArticleScientific reports2020
A shell matrix protein of Pinctada mazatlanica produces nacre platelets in vitro.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Quantitative Proteomic Profiling of Pinctada fucata Shell Nacre Defines a Solubility-Based Type Classification of Shell Matrix Proteins.Marine biotechnology (New York, N.Y.) · 2026Article
- Mollusk shells as marine bioactive materials: Composition, bioactivities, and prospects for food and health applications.iScience · 2026Review
- Nacre and Nacre-Inspired Materials: Historical Background, Definition, Fabrication Techniques and Gaps.Biomimetics (Basel, Switzerland) · 2026Review
- A c-type lectinFrontiers in immunology · 2024Article
- Microbially Induced Calcium Carbonate Precipitation byApplied and environmental microbiology · 2023Review
- Monitoring and modelling the glutamine metabolic pathway: a review and future perspectives.Metabolomics : Official journal of the Metabolomic Society · 2023Review
- Polyamines Promote Aragonite Nucleation and Generate Biomimetic Structures.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Proteomic and Transcriptomic Analyses in the Slipper SnailIntegrative organismal biology (Oxford, England) · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Nacre is the main component of the pearl oyster shells and it is synthesized by specialized soluble and insoluble shell matrix proteins. Insoluble proteins from the decalcification of the shell are the less studied proteins due to the technical problems to isolate them from the organic matrix. In this study, an insoluble shell matrix protein from Pinctada mazatlanica, pearlin (Pmaz-pearlin), was successfully cloned from the mantle tissue, and the native protein isolated from the shell was functionally characterized. The full coding sequence of Pmaz-pearlin mRNA consists of 423 base pairs, which encode to a 16.3 kDa pearlin. Analysis of the deduced amino acid sequence revealed that Pmaz-pearlin contained four acidic regions, an NG repeat domain, and Cys conserved residues, the latter potentially forms four disulfide bridges which might stabilize the protein structure. The isolated protein from the shell is a glycoprotein of ~ 16.74 kDa which can produce aragonite and calcite crystals in vitro. Our results show that Pmaz-pearlin is a well-conserved protein involved in nacre layer growth, which produces calcite crystals in the presence of CaCl
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