ArticleThe Journal of biological chemistry2009
Cloning and characterization of Prisilkin-39, a novel matrix protein serving a dual role in the prismatic layer formation from the oyster Pinctada fucata.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- The Hydractinia cell atlas reveals cellular and molecular principles of cnidarian coloniality.Nature communications · 2025Article
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- A Blueprint of Microstructures and Stage-Specific Transcriptome Dynamics of Cuticle Formation inInternational journal of molecular sciences · 2022Article
- Transcriptome analysis of the bivalve Placuna placenta mantle reveals potential biomineralization-related genes.Scientific reports · 2022Article
- A species-specific miRNA participates in biomineralization by targeting CDS regions of Prisilkin-39 and ACCBP in Pinctada fucata.Scientific reports · 2020Article
- Gene expression profiles at different stages for formation of pearl sac and pearl in the pearl oyster Pinctada fucata.BMC genomics · 2019Article
- PfmPif97-like regulated by Pfm-miR-9b-5p participates in shell formation in Pinctada fucata martensii.PloS one · 2019Article
- Zinc incorporation in marine bivalve shells grown in mine-polluted seabed sediments: a case study in the Malfidano mining area (SW Sardinia, Italy).Environmental science and pollution research international · 2018Article
- Transcriptional regulation of the matrix protein Shematrin-2 during shell formation in pearl oyster.The Journal of biological chemistry · 2018Article
- Cloning, characterization and functional analysis of an Alveoline-like protein in the shell of Pinctada fucata.Scientific reports · 2018Article
- The receptor genes PfBMPR1B and PfBAMBI are involved in regulating shell biomineralization in the pearl oyster Pinctada fucata.Scientific reports · 2017Article
- A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation.Scientific reports · 2017Article
- Identification and Differential Expression of Biomineralization Genes in the Mantle of Pearl Oyster Pinctada fucata.Marine biotechnology (New York, N.Y.) · 2017Article
- Transcriptome analysis of the freshwater pearl mussel (Cristaria plicata) mantle unravels genes involved in the formation of shell and pearl.Molecular genetics and genomics : MGG · 2017Article
- cDNA Microarray Analysis Revealing Candidate Biomineralization Genes of the Pearl Oyster, Pinctada fucata martensii.Marine biotechnology (New York, N.Y.) · 2016Article
- In-depth proteomic analysis of shell matrix proteins of Pinctada fucata.Scientific reports · 2015Article
- Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein.Scientific reports · 2015Article
- The AP-1 transcription factor homolog Pf-AP-1 activates transcription of multiple biomineral proteins and potentially participates in Pinctada fucata biomineralization.Scientific reports · 2015Article
- Microarray: a global analysis of biomineralization-related gene expression profiles during larval development in the pearl oyster, Pinctada fucata.BMC genomics · 2015Article
- Insulin treatment prevents the increase in D-serine in hippocampal CA1 area of diabetic rats.American journal of Alzheimer's disease and other dementias · 2015Article
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12 authors.
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Abstract
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.
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