| pubmed-article:9168818 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C2610925 | lld:lifeskim |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9168818 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9168818 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9168818 | pubmed:dateCreated | 1997-6-23 | lld:pubmed |
| pubmed-article:9168818 | pubmed:abstractText | Mouse thymocytes are known to undergo apoptosis by ligating some unique anti-Thy-1 monoclonal antibodies (mAbs), G7 and KT16. However, the precise mechanisms of Thy-1-mediated apoptosis are as yet unclear. We investigated Thy-1-mediated apoptosis using our previously generated anti-Thy-1 mAb, MCS-34, which was similar to G7 because both antibodies recognized both Thy-1.1 and Thy-1.2 and bound Thy-1A epitope. Unlike G7, MCS-34 alone could not induce apoptosis in thymocytes; however, it could induce apoptosis when it was cross-linked with second antibodies. Thus, MCS-34 could not aggregate by itself, but G7 could. In the course of investigating the apoptosis-related molecules that were involved in the thymocyte apoptosis induced by cross-linking of MCS-34 or by G7 ligation, we found that CPP 32-like proteases were activated during the apoptosis. Furthermore, the expression of bcl-2 and bcl-XL proteins was decreased in these apoptosis processes. Whereas the ligation of MCS-34 alone could not generate apoptosis signals that led to the activation of CPP32-like proteases and the decrease in bcl-2 and bcl-XL expression, the aggregation of Thy-1 glycoprotein might be crucial to signal thymocyte apoptosis. These results indicate that MCS-34 is a useful anti-Thy-1 mAb for analyzing the Thy-1-mediated signals since MCS-34 can control the level of apoptosis by using second antibodies. | lld:pubmed |
| pubmed-article:9168818 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9168818 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9168818 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9168818 | pubmed:month | May | lld:pubmed |
| pubmed-article:9168818 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:9168818 | pubmed:author | pubmed-author:KatoYY | lld:pubmed |
| pubmed-article:9168818 | pubmed:author | pubmed-author:LeeS HSH | lld:pubmed |
| pubmed-article:9168818 | pubmed:author | pubmed-author:TsuruoTT | lld:pubmed |
| pubmed-article:9168818 | pubmed:author | pubmed-author:KodamaNN | lld:pubmed |
| pubmed-article:9168818 | pubmed:author | pubmed-author:FujitaNN | lld:pubmed |
| pubmed-article:9168818 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9168818 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9168818 | pubmed:volume | 232 | lld:pubmed |
| pubmed-article:9168818 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9168818 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9168818 | pubmed:pagination | 400-6 | lld:pubmed |
| pubmed-article:9168818 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9168818 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9168818 | pubmed:articleTitle | Aggregation of Thy-1 glycoprotein induces thymocyte apoptosis through activation of CPP32-like proteases. | lld:pubmed |
| pubmed-article:9168818 | pubmed:affiliation | Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan. | lld:pubmed |
| pubmed-article:9168818 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9168818 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9168818 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:24832 | entrezgene:pubmed | pubmed-article:9168818 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9168818 | lld:pubmed |
