| pubmed-article:11787681 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0026140 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C1879746 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C1547011 | lld:lifeskim |
| pubmed-article:11787681 | lifeskim:mentions | umls-concept:C0670751 | lld:lifeskim |
| pubmed-article:11787681 | pubmed:dateCreated | 2002-1-11 | lld:pubmed |
| pubmed-article:11787681 | 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. | lld:pubmed |
| pubmed-article:11787681 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11787681 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11787681 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11787681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11787681 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11787681 | pubmed:issn | 0065-2598 | lld:pubmed |
| pubmed-article:11787681 | pubmed:author | pubmed-author:PetersonJ AJA | lld:pubmed |
| pubmed-article:11787681 | pubmed:author | pubmed-author:HamoshMM | lld:pubmed |
| pubmed-article:11787681 | pubmed:author | pubmed-author:CerianiR LRL | lld:pubmed |
| pubmed-article:11787681 | pubmed:author | pubmed-author:ScallanC DCD | lld:pubmed |
| pubmed-article:11787681 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11787681 | pubmed:volume | 501 | lld:pubmed |
| pubmed-article:11787681 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11787681 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11787681 | pubmed:pagination | 179-87 | lld:pubmed |
| pubmed-article:11787681 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:meshHeading | pubmed-meshheading:11787681... | lld:pubmed |
| pubmed-article:11787681 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11787681 | pubmed:articleTitle | Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane. | lld:pubmed |
| pubmed-article:11787681 | pubmed:affiliation | Cancer Research Institute of Contra Costa, San Francisco, CA 94107, USA. | lld:pubmed |
| pubmed-article:11787681 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11787681 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11787681 | pubmed:publicationType | Review | lld:pubmed |
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