| Autor: |
Eustace BK; Department of Physiology, Tufts University School of Medicine, Boston, MA 02111, USA., Sakurai T, Stewart JK, Yimlamai D, Unger C, Zehetmeier C, Lain B, Torella C, Henning SW, Beste G, Scroggins BT, Neckers L, Ilag LL, Jay DG |
| Jazyk: |
angličtina |
| Zdroj: |
Nature cell biology [Nat Cell Biol] 2004 Jun; Vol. 6 (6), pp. 507-14. Date of Electronic Publication: 2004 May 16. |
| DOI: |
10.1038/ncb1131 |
| Abstrakt: |
Tumour cell invasiveness is crucial for cancer metastasis and is not yet understood. Here we describe two functional screens for proteins required for the invasion of fibrosarcoma cells that identified the molecular chaperone heat shock protein 90 (hsp90). The hsp90 alpha isoform, but not hsp90 beta, is expressed extracellularly where it interacts with the matrix metalloproteinase 2 (MMP2). Inhibition of extracellular hsp90 alpha decreases both MMP2 activity and invasiveness. This role for extracellular hsp90 alpha in MMP2 activation indicates that cell-impermeant anti-hsp90 drugs might decrease invasiveness without the concerns inherent in inhibiting intracellular hsp90. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
