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Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell.

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
As typical biofoulers, barnacles possess hard shells and cause serious biofouling problems. In this study, we analyzed the protein component of the barnacle Amphibalanus (= Balanus) amphitrite shell using gel-based proteomics. The results revealed 52 proteins in the A. Amphitrite shell. Among them, 40 proteins were categorized into 11 functional groups based on KOG database, and the remaining 12 proteins were unknown. Besides the known proteins in barnacle shell (SIPC, carbonic anhydrase and acidic acid matrix protein), we also identified chorion peroxidase, C-type lectin-like domains, serine proteases and proteinase inhibitor proteins in the A. Amphitrite shell. The sequences of these proteins were characterized and their potential functions were discussed. Histology and DAPI staining revealed living cells in the shell, which might secrete the shell proteins identified in this study.

No MeSH data available.


Hematoxylin-eosin (A) and DAPI staining (B) showing cells in histological sections of the Amphibalanus amphitrite shell.Arrows identify potential cell structures.
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pone.0133866.g007: Hematoxylin-eosin (A) and DAPI staining (B) showing cells in histological sections of the Amphibalanus amphitrite shell.Arrows identify potential cell structures.

Mentions: To evaluate the presence of living cells in the barnacle shell, decalcified shells were cut into thin sections and stained with HE or DAPI. At the lower part of the shell paries (just above the basal suture), HE staining revealed cell-shaped structures that were attached to the surfaces of the small inner channels around lacunaes (Fig 7A), and DAPI staining showed cell nucleuses (Fig 7B).


Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell.

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

Hematoxylin-eosin (A) and DAPI staining (B) showing cells in histological sections of the Amphibalanus amphitrite shell.Arrows identify potential cell structures.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4519255&req=5

pone.0133866.g007: Hematoxylin-eosin (A) and DAPI staining (B) showing cells in histological sections of the Amphibalanus amphitrite shell.Arrows identify potential cell structures.
Mentions: To evaluate the presence of living cells in the barnacle shell, decalcified shells were cut into thin sections and stained with HE or DAPI. At the lower part of the shell paries (just above the basal suture), HE staining revealed cell-shaped structures that were attached to the surfaces of the small inner channels around lacunaes (Fig 7A), and DAPI staining showed cell nucleuses (Fig 7B).

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
As typical biofoulers, barnacles possess hard shells and cause serious biofouling problems. In this study, we analyzed the protein component of the barnacle Amphibalanus (= Balanus) amphitrite shell using gel-based proteomics. The results revealed 52 proteins in the A. Amphitrite shell. Among them, 40 proteins were categorized into 11 functional groups based on KOG database, and the remaining 12 proteins were unknown. Besides the known proteins in barnacle shell (SIPC, carbonic anhydrase and acidic acid matrix protein), we also identified chorion peroxidase, C-type lectin-like domains, serine proteases and proteinase inhibitor proteins in the A. Amphitrite shell. The sequences of these proteins were characterized and their potential functions were discussed. Histology and DAPI staining revealed living cells in the shell, which might secrete the shell proteins identified in this study.

No MeSH data available.