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Structural and Functional Aspects of Three Major Glycoproteins of the Human Milk Fat Globule Membrane

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 501))

Abstract

The MUC1 mucin, lactadherin, and butyrophilin are 3 major components of the human milk fat globule membrane. The mucin inhibits binding of S-fimbriatedEscherichia callto buccal epithelial cells, and lactadherin prevents symptomatic rotavirus infection in breast-fed infants. Butyrophilin has been suggested to be a structural component of the human milk fat globule (HMFG) membrane and to have receptor functions, but has no known anti-infective activity. These HMFG glycoproteins also are present in skimmed milk, possibly associated with phospholipid micelles, while mucin is also in a soluble form. Mucin and lactadherin resist digestion in the stomach of milk-fed infants, while butyrophilin is rapidly degraded. The MUC1 mucin is an extended rod-like structure forming part of the glycocalyx on the surface of many epithelial cells and membranes of milk, and may act as a decoy for binding of infective agents. The extracellular segment of butyrophilin has homology to Ig superfamily receptors and an intracellular domain with homology to developmentally regulated proteins. Lactadherin is a laterally mobile cell adhesion molecule that interacts with integrins and has a novel means of membrane-association involving specific binding to phosphatidylserine. The structural and functional aspects of these glyco-proteins are discussed with regard to their role in human milk for breast-fed infants.

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© 2001 Springer Science+Business Media New York

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Peterson, J.A., Scallan, C.D., Ceriani, R.L., Hamosh, M. (2001). Structural and Functional Aspects of Three Major Glycoproteins of the Human Milk Fat Globule Membrane. In: Newburg, D.S. (eds) Bioactive Components of Human Milk. Advances in Experimental Medicine and Biology, vol 501. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1371-1_23

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  • DOI: https://doi.org/10.1007/978-1-4615-1371-1_23

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5521-2

  • Online ISBN: 978-1-4615-1371-1

  • eBook Packages: Springer Book Archive

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