pubmed-article:17597069 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C1412197 | lld:lifeskim |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C1154393 | lld:lifeskim |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:17597069 | lifeskim:mentions | umls-concept:C0249992 | lld:lifeskim |
pubmed-article:17597069 | pubmed:issue | 35 | lld:pubmed |
pubmed-article:17597069 | pubmed:dateCreated | 2007-8-27 | lld:pubmed |
pubmed-article:17597069 | pubmed:abstractText | ADAMs (a disintegrin and metalloproteinases) are a recently discovered gene family of multifunctional proteins with the disintegrin-like and metalloproteinase domains. To analyze the biological functions of ADAM28, we screened binding molecules to secreted-type ADAM28 (ADAM28s) by the yeast two-hybrid system and identified P-selectin glycoprotein ligand-1 (PSGL-1). Binding between the disintegrin-like domain of ADAM28s and the extracellular portion of PSGL-1 was determined by yeast two-hybrid assays, binding assays of the domain-specific recombinant ADAM28s species using PSGL-1 stable transfectants and leukocyte cell lines expressing native PSGL-1 (HL-60 cells and Jurkat cells), and co-immunolocalization and co-immunoprecipitation of the molecules in these cells. Incubation of HL-60 cells with recombinant ADAM28s enhanced the binding to P-selectin-coated wells and P-selectin-expressing endothelial cells. In addition, intravenous injection of ADAM28s-treated HL-60 cells increased their accumulation in the pulmonary microcirculation and alveolar spaces in a mouse model of endotoxin-induced inflammation. These data suggest a novel function that ADAM28s promotes PSGL-1/P-selectin-mediated leukocyte rolling adhesion to endothelial cells and subsequent infiltration into tissue spaces through interaction with PSGL-1 on leukocytes under inflammatory conditions. | lld:pubmed |
pubmed-article:17597069 | pubmed:language | eng | lld:pubmed |
pubmed-article:17597069 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17597069 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17597069 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17597069 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17597069 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:HashimotoGaku... | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:IkedaEijiE | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:OkadaYasunori... | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:IshidaSusumuS | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:MochizukiSats... | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:ShimodaMasayu... | lld:pubmed |
pubmed-article:17597069 | pubmed:author | pubmed-author:NagaiNorihiro... | lld:pubmed |
pubmed-article:17597069 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17597069 | pubmed:day | 31 | lld:pubmed |
pubmed-article:17597069 | pubmed:volume | 282 | lld:pubmed |
pubmed-article:17597069 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17597069 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17597069 | pubmed:pagination | 25864-74 | lld:pubmed |
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pubmed-article:17597069 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17597069 | pubmed:articleTitle | Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells. | lld:pubmed |
pubmed-article:17597069 | pubmed:affiliation | Department of Pathology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo, 160-0016, Japan. | lld:pubmed |
pubmed-article:17597069 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17597069 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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