| pubmed-article:16420484 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0769218 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C1415932 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0036734 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0532025 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C1149301 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:16420484 | lifeskim:mentions | umls-concept:C0893192 | lld:lifeskim |
| pubmed-article:16420484 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16420484 | pubmed:dateCreated | 2006-1-19 | lld:pubmed |
| pubmed-article:16420484 | pubmed:abstractText | Insulin-like growth factor (IGF) binding protein-related protein-1 (IGFBP-rP1) modulates cellular adhesion and growth in an IGF/insulin-dependent or independent manner. It also shows tumor-suppressive activity in vivo. We recently found that a single-chain IGFB-rP1 is proteolytically cleaved to a two-chain form by a trypsin-like, endogenous serine proteinase, changing its biological activities. In this study, we attempted to identify the IGFBP-rP1-processing enzyme. Of nine human cell lines tested, seven cell lines secreted IGFBP-rP1 at high levels, and two of them, ovarian clear cell adenocarcinoma (OVISE) and gastric carcinoma (MKN-45), highly produced the cleaved IGFBP-rP1. Serine proteinase inhibitors effectively blocked the IGFBP-rP1 cleavage in the OVISE cell culture. The conditioned medium of OVISE cells did not cleave purified IGFBP-rP1, but their membrane fraction had an IGFBP-rP1-cleaving activity. The membrane fraction contained an 80-kDa gelatinolytic enzyme, which was identified as the membrane-type serine proteinase matriptase (MT-SP1) by immunoblotting. When the membrane fraction was separated by SDS/PAGE, the IGFBP-rP1-cleaving activity comigrated with matriptase. A soluble form of matriptase purified in an inhibitor-free form efficiently cleaved IGFBP-rP1 at the same site as that found in a naturally cleaved IGFBP-rP1. Furthermore, small interfering RNAs for matriptase efficiently blocked both the matriptase expression and the cleavage of IGBP-rP1 in OVISE cells. These results demonstrate that IGFBP-rP1 is processed to the two-chain form by matriptase on the cell surface. | lld:pubmed |
| pubmed-article:16420484 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16420484 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16420484 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16420484 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16420484 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16420484 | pubmed:issn | 1742-464X | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:DicksonRobert... | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:LinChen-YongC... | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:MiyazakiKaoru... | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:SatoYuichiroY | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:YasudaChieC | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:HigashiShouic... | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:AhmedSanjidaS | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:JinXinlianX | lld:pubmed |
| pubmed-article:16420484 | pubmed:author | pubmed-author:YagiMotokiM | lld:pubmed |
| pubmed-article:16420484 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16420484 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:16420484 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16420484 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16420484 | pubmed:pagination | 615-27 | lld:pubmed |
| pubmed-article:16420484 | pubmed:dateRevised | 2007-4-20 | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:meshHeading | pubmed-meshheading:16420484... | lld:pubmed |
| pubmed-article:16420484 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16420484 | pubmed:articleTitle | Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25). | lld:pubmed |
| pubmed-article:16420484 | pubmed:affiliation | Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan. | lld:pubmed |
| pubmed-article:16420484 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16420484 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16420484 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16420484 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16420484 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16420484 | lld:pubmed |
