Evidence map›Paper›PMID 41454042›Full record

ArticleMarine biotechnology (New York, N.Y.)2025

myCRP, Cysteine-Rich Protein in the Yesso Scallop Mizuhopecten yessoensis, Is a Novel High-Molecular Weight Cd-Binding Protein.

Zehua Zheng, Yuto Namikawa, Masahiko Awaji, Yugo Kato, Kurin Iimura, Makoto Nakakido, Kouhei Tsumoto, Lumi Negishi, Hitoshi Kurumizaka, Shino Homma-Takeda and 1 more

Abstract read
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In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

11 authors.

Zehua Zheng *Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Yuto Namikawa *Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Masahiko AwajiDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Yugo KatoDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Kurin IimuraDepartment of Food and Nutrition, Faculty of Human Life, Jumonji University, 2-1-28 Sugasawa, Niiza, Saitama, Japan.
Makoto NakakidoDepartment of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
Kouhei TsumotoDepartment of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
Lumi NegishiInstitute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo, 113-8657, Japan.
Hitoshi KurumizakaInstitute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo, 113-8657, Japan.
Shino Homma-TakedaInstitute for Radiological Science, National Institutes for Quantum Science and Technology, 4-9-1 Anagawa, Inage-ku, Chiba, 263-8555, Japan.
Michio SuzukiDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. amichio@g.ecc.u-tokyo.ac.jp.

Funding

Japan Society for the Promotion of Science JP19H05771
6 · The paper itself

Abstract

Heavy metal bioaccumulation in marine organisms is a critical concern for the oceanic environment and food safety. Scallops, as filter-feeding bivalves, accumulate cadmium (Cd) in their midgut gland to toxic concentrations that may pose risks to human health. Despite extensive research on Cd bioaccumulation in the Yesso scallop Mizuhopecten yessoensis, a major Cd-binding protein has not yet been functionally characterized. In this study, we used high-performance liquid chromatography coupled with inductively coupled plasma mass spectrometry (HPLC-ICP-MS) to isolate Cd-binding proteins, and identified myCRP, a novel high-molecular-weight Cd-binding protein. myCRP contains a cysteine-rich sequence, resembling metallothionein Cd-binding motifs, and is expressed exclusively in the midgut gland. Cd-binding assays demonstrated that myCRP binds Cd in a dose-dependent manner. Immunostaining revealed the presence of a small cluster of myCRP-containing cells in the connective tissue surrounding digestive tubules in the midgut gland. Synchrotron radiation X-ray fluorescence (SR-XRF) analyses showed the distribution of Cd throughout the entire midgut gland tissue. We conclude that myCRP is partly responsible for Cd binding in the midgut gland. Our findings clarify a new mechanism of Cd-binding in marine organisms from both biological and molecular perspectives.

Indexed as

CadmiumPectinidaeProteinsAmino Acid SequenceAnimalsMetallothioneinCadmiumcadmium-binding proteinMetallothioneinProteinsBioaccumulationCadmiumCysteine-rich proteinDetoxificationMidgut glandMizuhopecten yessoensis

Identifiers

PMID41454042

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.