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An interactomics overview of the human and bovine milk proteome over lactation

BACKGROUND: Milk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differenc...

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Autores principales: Zhang, Lina, van Dijk, Aalt D. J., Hettinga, Kasper
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267443/
https://www.ncbi.nlm.nih.gov/pubmed/28149201
http://dx.doi.org/10.1186/s12953-016-0110-0
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author Zhang, Lina
van Dijk, Aalt D. J.
Hettinga, Kasper
author_facet Zhang, Lina
van Dijk, Aalt D. J.
Hettinga, Kasper
author_sort Zhang, Lina
collection PubMed
description BACKGROUND: Milk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differences between human and bovine milk, the qualitative and quantitative differences in the milk proteome as well as their changes over lactation were compared using both label-free and labelled proteomics techniques. These datasets were analysed and compared, to better understand the role of milk proteins in development of the newborn. METHODS: Human and bovine milk samples were prepared by using filter-aided sample preparation (FASP) combined with dimethyl labelling and analysed by nano LC LTQ-Orbitrap XL mass spectrometry. RESULTS: The human and bovine milk proteome show similarities with regard to the distribution over biological functions, especially the dominant presence of enzymes, transport and immune-related proteins. At a quantitative level, the human and bovine milk proteome differed not only between species but also over lactation within species. Dominant enzymes that differed between species were those assisting in nutrient digestion, with bile salt-activated lipase being abundant in human milk and pancreatic ribonuclease being abundant in bovine milk. As lactation advances, immune-related proteins decreased slower in human milk compared to bovine milk. Notwithstanding these quantitative differences, analysis of human and bovine co-expression networks and protein-protein interaction networks indicated that a subset of milk proteins displayed highly similar interactions in each of the different networks, which may be related to the general importance of milk in nutrition and healthy development of the newborn. CONCLUSIONS: Our findings promote a better understanding of the differences and similarities in dynamics of human and bovine milk proteins, thereby also providing guidance for further improvement of infant formula. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12953-016-0110-0) contains supplementary material, which is available to authorized users.
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spelling pubmed-52674432017-02-01 An interactomics overview of the human and bovine milk proteome over lactation Zhang, Lina van Dijk, Aalt D. J. Hettinga, Kasper Proteome Sci Research BACKGROUND: Milk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differences between human and bovine milk, the qualitative and quantitative differences in the milk proteome as well as their changes over lactation were compared using both label-free and labelled proteomics techniques. These datasets were analysed and compared, to better understand the role of milk proteins in development of the newborn. METHODS: Human and bovine milk samples were prepared by using filter-aided sample preparation (FASP) combined with dimethyl labelling and analysed by nano LC LTQ-Orbitrap XL mass spectrometry. RESULTS: The human and bovine milk proteome show similarities with regard to the distribution over biological functions, especially the dominant presence of enzymes, transport and immune-related proteins. At a quantitative level, the human and bovine milk proteome differed not only between species but also over lactation within species. Dominant enzymes that differed between species were those assisting in nutrient digestion, with bile salt-activated lipase being abundant in human milk and pancreatic ribonuclease being abundant in bovine milk. As lactation advances, immune-related proteins decreased slower in human milk compared to bovine milk. Notwithstanding these quantitative differences, analysis of human and bovine co-expression networks and protein-protein interaction networks indicated that a subset of milk proteins displayed highly similar interactions in each of the different networks, which may be related to the general importance of milk in nutrition and healthy development of the newborn. CONCLUSIONS: Our findings promote a better understanding of the differences and similarities in dynamics of human and bovine milk proteins, thereby also providing guidance for further improvement of infant formula. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12953-016-0110-0) contains supplementary material, which is available to authorized users. BioMed Central 2017-01-05 /pmc/articles/PMC5267443/ /pubmed/28149201 http://dx.doi.org/10.1186/s12953-016-0110-0 Text en © The Author(s). 2017 Open AccessThis 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
Zhang, Lina
van Dijk, Aalt D. J.
Hettinga, Kasper
An interactomics overview of the human and bovine milk proteome over lactation
title An interactomics overview of the human and bovine milk proteome over lactation
title_full An interactomics overview of the human and bovine milk proteome over lactation
title_fullStr An interactomics overview of the human and bovine milk proteome over lactation
title_full_unstemmed An interactomics overview of the human and bovine milk proteome over lactation
title_short An interactomics overview of the human and bovine milk proteome over lactation
title_sort interactomics overview of the human and bovine milk proteome over lactation
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267443/
https://www.ncbi.nlm.nih.gov/pubmed/28149201
http://dx.doi.org/10.1186/s12953-016-0110-0
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