Source:http://linkedlifedata.com/resource/pubmed/id/11787681
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-1-11
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pubmed:abstractText |
The MUC1 mucin, lactadherin, and butyrophilin are 3 major components of the human milk fat globule membrane. The mucin inhibits binding of S-fimbriated Escherichia coli to 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 glycoproteins are discussed with regard to their role in human milk for breast-fed infants.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/MFGE8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mucin-1,
http://linkedlifedata.com/resource/pubmed/chemical/butyrophilin,
http://linkedlifedata.com/resource/pubmed/chemical/milk fat globule
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pubmed:status |
MEDLINE
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pubmed:issn |
0065-2598
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
501
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
179-87
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11787681-Anti-Infective Agents,
pubmed-meshheading:11787681-Antigens, Surface,
pubmed-meshheading:11787681-Glycolipids,
pubmed-meshheading:11787681-Glycoproteins,
pubmed-meshheading:11787681-Humans,
pubmed-meshheading:11787681-Membrane Glycoproteins,
pubmed-meshheading:11787681-Milk, Human,
pubmed-meshheading:11787681-Milk Proteins,
pubmed-meshheading:11787681-Mucin-1
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pubmed:year |
2001
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pubmed:articleTitle |
Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane.
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pubmed:affiliation |
Cancer Research Institute of Contra Costa, San Francisco, CA 94107, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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