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Recombinant matrix metalloproteinase-14 catalytic domain induces apoptosis in human osteoblastic SaOS-2 cells.

Abstract：

:Our study previously showed that estrogen and progesterone stimulated the production of matrix metalloproteinase-14 [MMP-14, or also named membrane type matrix metalloproteinses-1 (MT1-MMP)] in osteoblastic cells. MMP-14 was implied to regulate the function of osteoblasts by degrading bone matrix or growth factors, but the mechanism is unclear. Since MMP-14 plays a role primarily through the catalytic domain, and truncated MMP-14 containing the catalytic domain and lacking transmembrane domain can be secreted into medium by cultured cells, our present study was performed to observe the direct effects of recombinant MMP-14 catalytic domain on cultured human osteoblastic osteogenic sarcoma (SaOS)-2 cells. Our data showed that recombinant MMP-14 catalytic domain activated proMMP-2 secreted into media by SaOS-2 cells, and this process was blocked by ethylenediamine tetraacetic acid (EDTA) treatment. Recombinant MMP-14 catalytic domain inhibited the adhesion of SaOS-2 cells to immobilized type I collagen or fibronectin in a dose-dependent manner, and these effects on SaOS-2 cells were abolished by EDTA. Recombinant MMP-14 catalytic domain induced SaOS-2 cells apoptosis in a dose-dependent manner, and apoptosis-inducing activity of MMP-14 catalytic domain was blocked if it was treated with EDTA. In conclusion, we revealed that recombinant MMP-14 catalytic domain induced SaOS-2 cells apoptosis. We also indirectly showed the activity of MMP-14 catalytic domain to degrade extracellular matrix (ECM) in cultures of SaOS-2 cells through Gelatin Zymograms and adhesion assay. This suggests that since adhesion of cells to ECM serves as a survival mechanism in osteoblasts, the catalytic activity of recombinant MMP-14 catalytic domain on matrix proteins contributes to its apoptosis-inducing activity.

journal_name

J Endocrinol Invest

journal_title

Journal of endocrinological investigation

authors

Luo XH,Liao EY,Liao HJ,Jin Y,Zhou HD,Huang G

doi

10.1007/BF03345259

keywords:

subject

Has Abstract

pub_date

2003-11-01 00:00:00

pages

1111-6

issue

11

eissn

0391-4097

issn

1720-8386

pii

5498

journal_volume

26

pub_type

杂志文章

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