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Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes
BACKGROUND: Eggshell mineralization in commercially important species such as chicken, turkey or quail is of interest as a general model of calcium carbonate biomineralization. Knowledge of proteins and molecular mechanisms in eggshell assembly may also pave the way to manipulation of thickness of t...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4550075/ https://www.ncbi.nlm.nih.gov/pubmed/26312056 http://dx.doi.org/10.1186/s12953-015-0078-1 |
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author | Mann, Karlheinz Mann, Matthias |
author_facet | Mann, Karlheinz Mann, Matthias |
author_sort | Mann, Karlheinz |
collection | PubMed |
description | BACKGROUND: Eggshell mineralization in commercially important species such as chicken, turkey or quail is of interest as a general model of calcium carbonate biomineralization. Knowledge of proteins and molecular mechanisms in eggshell assembly may also pave the way to manipulation of thickness of the calcified layer or other features. Comparison of eggshell matrix proteomes of different species may contribute to a better understanding of the mineralization process. The recent publication of the quail genome sequence now enables the proteomic analysis of the quail shell matrix and this comparison with those of chicken and turkey. RESULTS: The quail eggshell proteome comprised 622 identified proteins, 311 of which were shared with chicken and turkey eggshell proteomes. Forty-eight major proteins (iBAQ-derived abundance higher than 0.1 % of total identified proteome) together covered 94 % of total proteome mass. Fifteen of these are also among the most abundant proteins in chicken and turkey eggshell matrix. Only three proteins with a percentage higher than 1.0 % of the total had not previously been identified as eggshell matrix proteins. These were an uncharacterized member of the latexin family, an uncharacterized protease inhibitor containing a Kunitz domain, and gastric intrinsic factor. The most abundant proteins were ovocleidin-116, ovalbumin and ovocalyxin-36 representing approximately 31, 13 and 8 % of the total identified proteome, respectively. The major phosphoproteins were ovocleidin-116 and osteopontin. While osteopontin phosphorylation sites were predominantly conserved between chicken and quail sequences, conservation was less in ovocleidin-116. CONCLUSIONS: Ovocleidin-116 and ovocalyxin-36 are among the most abundant eggshell matrix proteins in all three species of the family Phasianidae analyzed so far, indicating that their presently unknown function is essential for eggshell mineralization. Evidence for other chicken eggshell-specific proteins in quail was inconclusive. Therefore measurement of additional eggshell proteomes, especially from species of different families and preferentially from outside the order Galliformes, will be necessary. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12953-015-0078-1) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4550075 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-45500752015-08-27 Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes Mann, Karlheinz Mann, Matthias Proteome Sci Research Article BACKGROUND: Eggshell mineralization in commercially important species such as chicken, turkey or quail is of interest as a general model of calcium carbonate biomineralization. Knowledge of proteins and molecular mechanisms in eggshell assembly may also pave the way to manipulation of thickness of the calcified layer or other features. Comparison of eggshell matrix proteomes of different species may contribute to a better understanding of the mineralization process. The recent publication of the quail genome sequence now enables the proteomic analysis of the quail shell matrix and this comparison with those of chicken and turkey. RESULTS: The quail eggshell proteome comprised 622 identified proteins, 311 of which were shared with chicken and turkey eggshell proteomes. Forty-eight major proteins (iBAQ-derived abundance higher than 0.1 % of total identified proteome) together covered 94 % of total proteome mass. Fifteen of these are also among the most abundant proteins in chicken and turkey eggshell matrix. Only three proteins with a percentage higher than 1.0 % of the total had not previously been identified as eggshell matrix proteins. These were an uncharacterized member of the latexin family, an uncharacterized protease inhibitor containing a Kunitz domain, and gastric intrinsic factor. The most abundant proteins were ovocleidin-116, ovalbumin and ovocalyxin-36 representing approximately 31, 13 and 8 % of the total identified proteome, respectively. The major phosphoproteins were ovocleidin-116 and osteopontin. While osteopontin phosphorylation sites were predominantly conserved between chicken and quail sequences, conservation was less in ovocleidin-116. CONCLUSIONS: Ovocleidin-116 and ovocalyxin-36 are among the most abundant eggshell matrix proteins in all three species of the family Phasianidae analyzed so far, indicating that their presently unknown function is essential for eggshell mineralization. Evidence for other chicken eggshell-specific proteins in quail was inconclusive. Therefore measurement of additional eggshell proteomes, especially from species of different families and preferentially from outside the order Galliformes, will be necessary. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12953-015-0078-1) contains supplementary material, which is available to authorized users. BioMed Central 2015-08-27 /pmc/articles/PMC4550075/ /pubmed/26312056 http://dx.doi.org/10.1186/s12953-015-0078-1 Text en © Mann and Mann. 2015 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Mann, Karlheinz Mann, Matthias Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title | Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title_full | Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title_fullStr | Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title_full_unstemmed | Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title_short | Proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
title_sort | proteomic analysis of quail calcified eggshell matrix: a comparison to chicken and turkey eggshell proteomes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4550075/ https://www.ncbi.nlm.nih.gov/pubmed/26312056 http://dx.doi.org/10.1186/s12953-015-0078-1 |
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