Abstract
The enhanced expression of matrix metalloproteinases (MMP), especially gelatinases MMP-2 and MMP-9, has been associated with the invasive behavior of tumor cells. Previously we reported that primary acute myelogenous leukemia blasts and human leukemic cultured KG-1 cells but not HEL cells penetrate a reconstituted basement membrane (Matrigel) in an invasion assay. In this study, we investigated the role of MMP-2 and MMP-9 in in vitro invasion by leukemic cells. We found that both recombinant human tissue inhibitor of metalloproteinase-2 (rhTIMP-2) and anti-MMP-2 antibody inhibit the invasiveness of KG-1 cells in the Matrigel assay (by 76% and 51% respectively), while anti-MMP-9 antibody does not, indicating that MMP-2 but not MMP-9 in involved in the invasive process. KG-1 cells were found to secrete constitutively the latent (but not the activated) forms of both MMP-2 and MMP-9 and, after stimulation with the phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA), higher levels of these pro-MMP. TPA stimulation, however, did not increase the in vitro invasiveness of these cells. Analysis by Western blot and flow cytometry revealed the presence of the activated form of MMP-2 (64 kDa) on the surface of KG-1 cells and primary A...Continue Reading
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