Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane.
Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane.
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DOI:
10.1007/978-1-4615-1371-1_23
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发表时间:
2001
影响因子:
--
通讯作者:
Jerry A. Peterson;C. Scallan;Roberto L. Ceriani;M. Hamosh
中科院分区:
文献类型:
--
作者:
Jerry A. Peterson;C. Scallan;Roberto L. Ceriani;M. Hamosh
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.