Dataset Information

Proteomic analysis of larval and adult shell matrix proteins in Crassostrea nippona by LC-MS/MS

ABSTRACT: This project contains proteomic profiles of shell matrix proteins (SMPs) from the Iwagaki oyster Crassostrea nippona, covering both life stage-specific shells (D-stage larval and adult shell) and shell microstructure-specific layers (prismatic, foliated, and chalky layers of the adult shell). These datasets were generated to investigate the molecular composition and regulatory mechanisms underlying biomineralized shell formation across developmental stages and shell architectures. The identified proteins provide insights into shell mineralization from both structural and evolutionary perspectives.

INSTRUMENT(S):

ORGANISM(S): Crassostrea Nippona

TISSUE(S): Exoskeleton

SUBMITTER: Yitian Bai

LAB HEAD: Yitian Bai

PROVIDER: PXD064366 | Pride | 2026-02-09

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Adult_shell-whole.proteinGroups.txt	Txt
	Adult_shell-whole.raw	Raw
	Chalky_layer_of_adult_shell.proteinGroups.txt	Txt
	Chalky_layer_of_adult_shell.raw	Raw
	Foliated_layer_of_adult_shell.proteinGroups.txt	Txt

Items per page:

1 - 5 of 11

Publications

Evolutionary innovation within conserved gene regulatory networks underlying biomineralized skeletons in Bilateria.

Bai Yitian Y Min Yue Y Liu Shikai S Hu Yiming Y Jin Shulei S Yu Hong H Kong Lingfeng L Macqueen Daniel J DJ Du Shaojun S Li Qi Q

Molecular biology and evolution 20260201 2

Biomineralized skeletons have evolved convergently across animals and exhibit remarkable diversity in structure and development. However, the evolutionary origins of gene regulatory networks underlying biomineralized skeletons remain elusive. Here, we report comprehensive developmental profiling of transcriptomic and chromatin dynamics in a bivalve mollusc, Crassostrea nippona. We provide evidence for a biphasic regulatory program orchestrating larval and adult shell formation, involving the coo ...[more]

PMID: 41556888

Similar Datasets

Project description:Background: The shells of various Haliotis species have served as models of invertebrate biomineralization and physical shell properties for more than 20 years. A focus of this research has been the nacreous inner layer of the shell with its conspicuous arrangement of aragonite platelets, resembling in cross-section a brick-and-mortar wall. In comparison, the outer, less stable, calcitic prismatic layer has received much less attention. One of the first molluscan shell proteins to be characterized at the molecular level was Lustrin A, a component of the nacreous organic matrix of Haliotis rufescens. This was soon followed by the C-type lectin perlucin and the growth factor-binding perlustrin, both isolated from H. laevigata nacre, and the crystal growth-modulating AP7 and AP24, isolated from H. rufescens nacre. Mass spectrometry-based proteomics was subsequently applied to to Haliotis biomineralization research with the analysis of the H. asinina shell matrix and yielded 14 different shell-associated proteins. That study was the most comprehensive for a Haliotis species to date. Methods: The shell proteomes of nacre and prismatic layer of the marine gastropod Haliotis laevigata were analyzed combining mass spectrometry-based proteomics and next generation sequencing. Results: We identified 297 proteins from the nacreous shell layer and 350 proteins from the prismatic shell layer from the green lip abalone H. laevigata. Considering the overlap between the two sets we identified a total of 448 proteins. Fifty-one nacre proteins and 43 prismatic layer proteins were defined as major proteins based on their abundance at more than 0.2% of the total. The remaining proteins occurred at low abundance and may not play any significant role in shell fabrication. The overlap of major proteins between the two shell layers was 17, amounting to a total of 77 major proteins. Conclusions: The H. laevigata shell proteome shares moderate sequence similarity at the protein level with other gastropod, bivalve and more distantly related invertebrate biomineralising proteomes. Features conserved in H. laevigata and other molluscan shell proteomes include short repetitive sequences of low complexity predicted to lack intrinsic three-dimensional structure, and domains such as tyrosinase, chitin-binding, and carbonic anhydrase. This catalogue of H. laevigata shell proteins represents the most comprehensive for a haliotid and should support future efforts to elucidate the molecular mechanisms of shell assembly.