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Calcium-enriched casein phosphopeptide stimulates release of IL-6 cytokine in human epithelial intestinal cell line

Published online by Cambridge University Press:  22 September 2005

David D Kitts  and
Soichiro Nakamura
David D Kitts
Affiliation:
Food, Nutrition and Health, Faculty of Agricultural Sciences, University of British Columbia, Vancouver, B.C., Canada. V6T-1Z4
Soichiro Nakamura
Affiliation:
Department of Life and Environmental Science and Department of Life Science and Biotechnology, Shimane University, Shimane, Japan. 690-8504
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Abstract

Phosphopeptides derived from digests of milk casein possess bioactive properties with gastrointestinal, immunological, vasoregulatory and nutritional activities (Clare & Swaisgood, 2000; Kitts & Weiler, 2003). Products of tryptic digestion of casein, yielding caseinphosphopeptides (CPP), bind to divalent minerals such as iron and calcium by ionic interactions that involve phosphoseryl residues (Kitts & Yuan, 1992; Aìt-Oukhartar, 2000). Distribution of phosphoserine moieties varies with the individual native caseinates, and the extent of phosphorylation directly influences CPP mineral binding affinity (e.g. αs2>, αs1>β-caseins). The anionic pentapeptide (SerP-SerP-SerP-Glu-Glu) is the distinctive feature for the major fractions of casein phosphopeptides (CPP) characterized both in vitro and in vivo. Common CPP derived from tryptic digests of whole bovine casein in vitro include, β-casein-4P (1–25), αs1-casein-5P (59–79), αs2-casein-4P (1–21) and αs2-casein-4P (46–70) (Kitts & Kwong, 2004).

Keywords

Intestinal epithelial cellscytokine IL-6caseinphosphopeptide III
Type
Research Article
Information
Journal of Dairy Research , Volume 73 , Issue 1 , February 2006 , pp. 44 - 48
Copyright
Proprietors of Journal of Dairy Research 2006

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