Evidence map›Paper›PMID 22416139›Full record

ArticleThe Journal of biological chemistry2012

Novel basic protein, PfN23, functions as key macromolecule during nacre formation.

Dong Fang, Cong Pan, Huijuan Lin, Ya Lin, Guiyou Zhang, Hongzhong Wang, Maoxian He, Liping Xie, Rongqing Zhang

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

Who cites it

28 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

9 authors.

Dong FangInstitute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Cong Pan
Huijuan Lin
Ya Lin
Guiyou Zhang
Hongzhong Wang
Maoxian He
Liping Xie
Rongqing Zhang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fine microstructure of nacre (mother of pearl) illustrates the beauty of nature. Proteins found in nacre were believed to be "natural hands" that control nacre formation. In the classical view of nacre formation, nucleation of the main minerals, calcium carbonate, is induced on and by the acidic proteins in nacre. However, the basic proteins were not expected to be components of nacre. Here, we reported that a novel basic protein, PfN23, was a key accelerator in the control over crystal growth in nacre. The expression profile, in situ immunostaining, and in vitro immunodetection assays showed that PfN23 was localized within calcium carbonate crystals in the nacre. Knocking down the expression of PfN23 in adults via double-stranded RNA injection led to a disordered nacre surface in adults. Blocking the translation of PfN23 in embryos using morpholino oligomers led to the arrest of larval development. The in vitro crystallization assay showed that PfN23 increases the rate of calcium carbonate deposition and induced the formation of aragonite crystals with characteristics close to nacre. In addition, we constructed the peptides and truncations of different regions of this protein and found that the positively charged C-terminal region was a key region for the function of PfN23 Taken together, the basic protein PfN23 may be a key accelerator in the control of crystal growth in nacre. This provides a valuable balance to the classic view that acidic proteins control calcium carbonate deposition in nacre.

Indexed as

Amino Acid SequenceAnimalsAnimal ShellsBlotting, WesternCalcium CarbonateCrystallizationGene ExpressionMacromolecular SubstancesMicroscopy, Electron, ScanningMolecular Sequence DataNacreOligodeoxyribonucleotides, AntisensePinctadaProteinsReverse Transcriptase Polymerase Chain ReactionRNA InterferenceCalcium CarbonateMacromolecular SubstancesNacreOligodeoxyribonucleotides, AntisenseProteinsSerine

Identifiers

PMID22416139
PMCPMC3346131

What OpenQuestion holds

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Registered trials

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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.