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Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation

In-depth understanding of the changing functions of human milk (HM) proteins and the corresponding physiological adaptions of the lactating mammary gland has been inhibited by incomplete knowledge of the HM proteome. We analyzed the HM whey proteome (n = 10 women with samples at 1 week and 1, 3, 6,...

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Detalles Bibliográficos
Autores principales: Zhang, Qiang, Cundiff, Judy K., Maria, Sarah D., McMahon, Robert J., Woo, Jessica G., Davidson, Barbara S., Morrow, Ardythe L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302745/
https://www.ncbi.nlm.nih.gov/pubmed/28250401
http://dx.doi.org/10.3390/proteomes1020128
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author Zhang, Qiang
Cundiff, Judy K.
Maria, Sarah D.
McMahon, Robert J.
Woo, Jessica G.
Davidson, Barbara S.
Morrow, Ardythe L.
author_facet Zhang, Qiang
Cundiff, Judy K.
Maria, Sarah D.
McMahon, Robert J.
Woo, Jessica G.
Davidson, Barbara S.
Morrow, Ardythe L.
author_sort Zhang, Qiang
collection PubMed
description In-depth understanding of the changing functions of human milk (HM) proteins and the corresponding physiological adaptions of the lactating mammary gland has been inhibited by incomplete knowledge of the HM proteome. We analyzed the HM whey proteome (n = 10 women with samples at 1 week and 1, 3, 6, 9 and 12 months) using a quantitative proteomic approach. One thousand three hundred and thirty three proteins were identified with 615 being quantified. Principal component analysis revealed a transition in the HM whey proteome-throughout the first year of lactation. Abundance changes in IgG, sIgA and sIgM display distinct features during the first year. Complement components and other acute-phase proteins are generally at higher levels in early lactation. Proteomic analysis further suggests that the sources of milk fatty acids (FA) shift from more direct blood influx to more de novo mammary synthesis over lactation. The abundances of the majority of glycoproteins decline over lactation, which is consistent with increased enzyme expression in glycoprotein degradation and decreased enzyme expression in glycoprotein synthesis. Cellular detoxification machinery may be transformed as well, thereby accommodating increased metabolic activities in late lactation. The multiple developing functions of HM proteins and the corresponding mammary adaption become more apparent from this study.
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spelling pubmed-53027452017-02-27 Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation Zhang, Qiang Cundiff, Judy K. Maria, Sarah D. McMahon, Robert J. Woo, Jessica G. Davidson, Barbara S. Morrow, Ardythe L. Proteomes Article In-depth understanding of the changing functions of human milk (HM) proteins and the corresponding physiological adaptions of the lactating mammary gland has been inhibited by incomplete knowledge of the HM proteome. We analyzed the HM whey proteome (n = 10 women with samples at 1 week and 1, 3, 6, 9 and 12 months) using a quantitative proteomic approach. One thousand three hundred and thirty three proteins were identified with 615 being quantified. Principal component analysis revealed a transition in the HM whey proteome-throughout the first year of lactation. Abundance changes in IgG, sIgA and sIgM display distinct features during the first year. Complement components and other acute-phase proteins are generally at higher levels in early lactation. Proteomic analysis further suggests that the sources of milk fatty acids (FA) shift from more direct blood influx to more de novo mammary synthesis over lactation. The abundances of the majority of glycoproteins decline over lactation, which is consistent with increased enzyme expression in glycoprotein degradation and decreased enzyme expression in glycoprotein synthesis. Cellular detoxification machinery may be transformed as well, thereby accommodating increased metabolic activities in late lactation. The multiple developing functions of HM proteins and the corresponding mammary adaption become more apparent from this study. MDPI 2013-09-03 /pmc/articles/PMC5302745/ /pubmed/28250401 http://dx.doi.org/10.3390/proteomes1020128 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Zhang, Qiang
Cundiff, Judy K.
Maria, Sarah D.
McMahon, Robert J.
Woo, Jessica G.
Davidson, Barbara S.
Morrow, Ardythe L.
Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title_full Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title_fullStr Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title_full_unstemmed Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title_short Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation
title_sort quantitative analysis of the human milk whey proteome reveals developing milk and mammary-gland functions across the first year of lactation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302745/
https://www.ncbi.nlm.nih.gov/pubmed/28250401
http://dx.doi.org/10.3390/proteomes1020128
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