ArticleScientific reports2021
Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 21 citations in OpenAlex.
- Designing a Whole-Cell Biosensor for Detection of Toxic Metals Using Intein Splicing Inhibition ofACS omega · 2026Article
- Unravelling Mechanisms of Oxinflammation Induced by Heavy Metals.Metabolites · 2026Review
- myCRP, Cysteine-Rich Protein in the Yesso Scallop Mizuhopecten yessoensis, Is a Novel High-Molecular Weight Cd-Binding Protein.Marine biotechnology (New York, N.Y.) · 2025Article
- Exploring cadmium-binding proteins in Japanese scallops Mizuhopecten yessoensis: isolation and characterization.Environmental science and pollution research international · 2025Article
- The Spatial Distribution Patterns, Physicochemical Properties, and Structural Characterization of Proteins in Oysters (Foods (Basel, Switzerland) · 2022Article
- Deposition of Lead Phosphate by Lead-Tolerant Bacteria Isolated from Fresh Water near an Abandoned Mine.International journal of molecular sciences · 2022Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pacific oyster, Crassostrea gigas, is a traditional food worldwide. The soft body of the oyster can easily accumulate heavy metals such as cadmium (Cd). To clarify the molecular mechanism of Cd accumulation in the viscera of C. gigas, we identified Cd-binding proteins. 5,10,15,20-Tetraphenyl-21H,23H-porphinetetrasulfonic acid, disulfuric acid, tetrahydrate, and Cd-binding competition experiments using immobilized metal ion affinity chromatography revealed the binding of water-soluble high molecular weight proteins to Cd, including C. gigas protein disulfide isomerase (cgPDI). Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses revealed two CGHC motifs in cgPDI. The binding between Cd and rcgPDI was confirmed through a Cd-binding experiment using the TPPS method. Isothermal titration calorimetry (ITC) revealed the binding of two Cd ions to one molecule of rcgPDI. Circular dichroism (CD) spectrum and tryptophan fluorescence analyses demonstrated that the rcgPDI bound to Cd. The binding markedly changed the two-dimensional or three-dimensional structures. The activity of rcgPDI measured by a PDI Activity Assay Kit was more affected by the addition of Cd than by human PDI. Immunological analyses indicated that C. gigas contained cgPDI at a concentration of 1.0 nmol/g (viscera wet weight). The combination of ITC and quantification results revealed that Cd-binding to cgPDI accounted for 20% of the total bound Cd in the visceral mass. The findings provide new insights into the defense mechanisms of invertebrates against Cd.
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