Source:http://linkedlifedata.com/resource/pubmed/id/11089884
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
|
pubmed:dateCreated |
2000-12-11
|
pubmed:abstractText |
This study aimed at clarifying the role of Aminopeptidase N (APN), a Zn2+-dependent ectopeptidase localized on the cell surface of human osteosarcoma cell lines treated with proinflammatory cytokines. We investigated the proinflammatory cytokines interleukin-1 beta (IL-1beta), IL-6 and tumor necrosis factor alpha (TNF-alpha) as well as the anti-inflammatory cytokine transforming growth factor beta (TGF-beta) for their influence on APN regulation. Soluble IL-6 receptor (sIL-6R) was always used together with IL-6 to achieve a stable effect. In addition, the invasive potential of the osteosarcoma cell lines MG63 and HOS was examined. Competitive RT-PCR and Ala-pNA activity assays revealed that IL-6 and sIL-6R significantly increased the mRNA expression and activity of APN in both osteosarcoma cell lines. Although IL-1beta significantly stimulated APN mRNA expression in both cell lines, it influenced the enzyme activity only in MG63. TNF-alpha and TGF-beta, however, had an effect neither on mRNA expression nor on the enzyme activity of APN in both cell lines. In the Matrigel invasion assay, IL-6 and sIL-6R significantly up-regulated the transmigration of these cell lines, whereas other cytokines did not. The up-regulated invasion was inhibited by bestatin, a specific inhibitor of APN. Cellular migration correlated highly with APN activity (r = 0.79, P < 0.002). These findings suggest that APN contributes to the invasive potential of human osteosarcomas enhanced by IL-6 and SIL-6R.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD13,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/interleukin 6-interleukin 6...
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0262-0898
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
17
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
857-63
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11089884-Antigens, CD13,
pubmed-meshheading:11089884-Bone Neoplasms,
pubmed-meshheading:11089884-Humans,
pubmed-meshheading:11089884-Interleukin-1,
pubmed-meshheading:11089884-Interleukin-6,
pubmed-meshheading:11089884-Neoplasm Invasiveness,
pubmed-meshheading:11089884-Osteosarcoma,
pubmed-meshheading:11089884-Receptors, Interleukin,
pubmed-meshheading:11089884-Receptors, Interleukin-6,
pubmed-meshheading:11089884-Recombinant Fusion Proteins,
pubmed-meshheading:11089884-Transforming Growth Factor beta,
pubmed-meshheading:11089884-Tumor Cells, Cultured,
pubmed-meshheading:11089884-Tumor Necrosis Factor-alpha
|
pubmed:year |
1999
|
pubmed:articleTitle |
Possible contribution of aminopeptidase N (APN/CD13) to invasive potential enhanced by interleukin-6 and soluble interleukin-6 receptor in human osteosarcoma cell lines.
|
pubmed:affiliation |
Department of Pathology, Otto-von-Guericke University Magdeburg, Germany. akirakid@naramed-u.ac.jp
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|