title: Proteolytic Systems in Milk: Perspectives on the Evolutionary Function within the Mammary Gland and the Infant.
abstract: Milk contains elements of numerous proteolytic systems (zymogens, active proteases, protease inhibitors and protease activators) produced in part from blood, in part by mammary epithelial cells and in part by immune cell secretion. Researchers have examined milk proteases for decades, as they can cause major defects in milk quality and cheese production. Most previous research has examined these proteases with the aim to eliminate or control their actions. However, our recent peptidomics research demonstrates that these milk proteases produce specific peptides in healthy milk and continue to function within the infant's gastrointestinal tract. These findings suggest that milk proteases have an evolutionary function in aiding the infant's digestion or releasing functional peptides. In other words, the mother provides the infant with not only dietary proteins but also the means to digest them. However, proteolysis in the milk is controlled by a balance of protease inhibitors and protease activators so that only a small portion of milk proteins are digested within the mammary gland. This regulation presents a question: If proteolysis is beneficial to the infant, what benefits are gained by preventing complete proteolysis through the presence of protease inhibitors? In addition to summarizing what is known about milk proteolytic systems, we explore possible evolutionary explanations for this proteolytic balance.
authors.affiliation: Department of Food Science and Technology, University of California, Davis, One Shields Avenue, Davis, CA, 95616, USA. dcdallas@ucdavis.edu.|Foods for Health Institute, University of California, Davis, One Shields Avenue, Davis, CA, 95616, USA. dcdallas@ucdavis.edu.
authors.forename: David C
authors.initials: DC
authors.lastname: Dallas
authors.affiliation: Institute of Food and Health, School of Agriculture and Food Science, University College Dublin, Belfield, Dublin, Ireland.
authors.forename: Niamh M
authors.initials: NM
authors.lastname: Murray
authors.affiliation: Department of Food Science and Technology, University of California, Davis, One Shields Avenue, Davis, CA, 95616, USA.|Foods for Health Institute, University of California, Davis, One Shields Avenue, Davis, CA, 95616, USA.
authors.forename: Junai
authors.initials: J
authors.lastname: Gan
mesh_terms: D000818:Animals; D004063:Digestion; D004798:Enzymes / Q000097:blood; D004847:Epithelial Cells / Q000378:metabolism / Q000502:physiology*; D019143:Evolution, Molecular; D005260:Female; D041981:Gastrointestinal Tract / Q000378:metabolism*; D006801:Humans; D007223:Infant; D007234:Infant, Premature / Q000378:metabolism; D007774:Lactation / Q000378:metabolism; D042361:Mammary Glands, Human / Q000378:metabolism*; D020782:Matrix Metalloproteinases / Q000378:metabolism; D008895:Milk, Human / Q000201:enzymology* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism; D057900:Transcytosis
chemical_list: D004798:Enzymes; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D020782:Matrix Metalloproteinases
keywords: Digestion; Mammary gland; Milk; Protease; Protease activator; Protease inhibitor