Abstract:
:Unstimulated human fibrosarcoma cells (HT1080) constitutively secrete matrix metalloproteinase 2 (MMP 2) as a proenzyme requiring proteolytic cleavage by membrane type-1 MMP (MT1 MMP) for activation. Physiological and pharmacological stimuli induce clustering of MT1 MMP/tissue inhibitor of MMP 2 "receptors", promoting binding and activation of MMP 2. We now report that cholesterol depleted HT1080 cells accumulated MT1 MMP on the cell surface and activated MMP 2. A specific inhibitor of mitogen activated protein kinase kinase 1/2 inhibited both MMP 2 activation and extracellular signal-related kinase phosphorylation induced by cholesterol depletion. Our data indicate that the cholesterol content of unstimulated cells is critical for secretion of MMP 2 as an inactive zymogen and control of pericellular proteolysis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Atkinson SJ,English JL,Holway N,Murphy Gdoi
10.1016/j.febslet.2004.04.040keywords:
subject
Has Abstractpub_date
2004-05-21 00:00:00pages
65-70issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304004430journal_volume
566pub_type
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