| pubmed-article:1406635 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1406635 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
| pubmed-article:1406635 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:1406635 | lifeskim:mentions | umls-concept:C0051926 | lld:lifeskim |
| pubmed-article:1406635 | lifeskim:mentions | umls-concept:C1415205 | lld:lifeskim |
| pubmed-article:1406635 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:1406635 | pubmed:dateCreated | 1992-10-26 | lld:pubmed |
| pubmed-article:1406635 | pubmed:abstractText | We used complementary biochemical and immunological techniques to establish that an endothelial cell transmembrane glycoprotein, GP116, is a CD44-like molecule and binds directly both to extracellular matrix components (e.g., hyaluronic acid) and to ankyrin. The specific characteristics of GP116 are as follows: (i) GP116 can be surface labeled with Na 125I and contains a wheat germ agglutinin-binding site(s), indicating that it has an extracellular domain; (ii) GP116 displays immunological cross-reactivity with a panel of CD44 antibodies, shares some peptide similarity with CD44, and has a similar 52-kDa precursor molecule, indicating that it is a CD44-like molecule; (iii) GP116 displays specific hyaluronic acid-binding properties, indicating that it is a hyaluronic acid receptor; (iv) GP116 can be phosphorylated by endogenous protein kinase C activated by 12-O-tetradecanoylphorbol-13-acetate and by exogenously added protein kinase C; and (v) GP116 and a 20-kDa tryptic polypeptide fragment of GP116 from the intracellular domain are capable of binding the membrane-cytoskeleton linker molecule, ankyrin. Furthermore, phosphorylation of GP116 by protein kinase C significantly enhances GP116 binding to ankyrin. Together, these findings strongly suggest that phosphorylation of the transmembrane glycoprotein GP116 (a CD44-like molecule) by protein kinase C is required for effective GP116-ankyrin interaction during endothelial cell adhesion events. | lld:pubmed |
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| pubmed-article:1406635 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1406635 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1406635 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1406635 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1406635 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1406635 | pubmed:author | pubmed-author:BourguignonL... | lld:pubmed |
| pubmed-article:1406635 | pubmed:author | pubmed-author:ChewAA | lld:pubmed |
| pubmed-article:1406635 | pubmed:author | pubmed-author:BourguignonG... | lld:pubmed |
| pubmed-article:1406635 | pubmed:author | pubmed-author:FOXJ NJN | lld:pubmed |
| pubmed-article:1406635 | pubmed:author | pubmed-author:LokeshwarV... | lld:pubmed |
| pubmed-article:1406635 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1406635 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:1406635 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1406635 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1406635 | pubmed:pagination | 4464-71 | lld:pubmed |
| pubmed-article:1406635 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1406635 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1406635 | pubmed:articleTitle | A CD44-like endothelial cell transmembrane glycoprotein (GP116) interacts with extracellular matrix and ankyrin. | lld:pubmed |
| pubmed-article:1406635 | pubmed:affiliation | Department of Cell Biology, School of Medicine, University of Miami, Florida 33101. | lld:pubmed |
| pubmed-article:1406635 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1406635 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1406635 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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