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Proteomes
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10.3390/proteomes1020128
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Article

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

by
Qiang Zhang
1,*,
Judy K. Cundiff
1,
Sarah D. Maria
1,
Robert J. McMahon
1,
Jessica G. Woo
2,
Barbara S. Davidson
2 and
Ardythe L. Morrow
2
1
Mead Johnson Nutrition, 2400 West Lloyd Expressway, Evansville, IN 47721, USA
2
Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45213, USA
*
Author to whom correspondence should be addressed.
Proteomes 2013, 1(2), 128-158; https://doi.org/10.3390/proteomes1020128
Received: 15 July 2013 / Revised: 15 August 2013 / Accepted: 26 August 2013 / Published: 3 September 2013
(This article belongs to the Special Issue Feature Paper 2013)
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Abstract

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. View Full-Text
Keywords: human milk; milk proteins; immunoglobulins; complement system; cellular processes human milk; milk proteins; immunoglobulins; complement system; cellular processes
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MDPI and ACS Style

Zhang, Q.; Cundiff, J.K.; Maria, S.D.; McMahon, R.J.; Woo, J.G.; Davidson, B.S.; Morrow, A.L. Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation. Proteomes 2013, 1, 128-158. https://doi.org/10.3390/proteomes1020128

AMA Style

Zhang Q, Cundiff JK, Maria SD, McMahon RJ, Woo JG, Davidson BS, Morrow AL. Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation. Proteomes. 2013; 1(2):128-158. https://doi.org/10.3390/proteomes1020128

Chicago/Turabian Style

Zhang, Qiang, Judy K. Cundiff, Sarah D. Maria, Robert J. McMahon, Jessica G. Woo, Barbara S. Davidson, and Ardythe L. Morrow. 2013. "Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation" Proteomes 1, no. 2: 128-158. https://doi.org/10.3390/proteomes1020128

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