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J Biol Chem, Vol. 274, Issue 36, 25371-25378, September 3, 1999
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From the Departments of Along with degradation of type IV collagen in
basement membrane, destruction of the stromal collagens, types I and
III, is an essential step in the invasive/metastatic behavior of tumor cells, and it is mediated, at least in part, by interstitial
collagenase 1 (matrix metalloproteinase 1 (MMP-1)). Because A2058
melanoma cells produce substantial quantities of MMP-1, we used these
cells as models for studying invasion of type I collagen. With a
sensitive and quantitative in vitro invasion assay, we
monitored the ability of these cells to invade a matrix of type I
collagen and the ability of a serine proteinase inhibitor and
all-trans-retinoic acid to block invasion. Although these
cells produce copious amounts of MMP-1, they do not invade collagen
unless they are co-cultured with fibroblasts or with conditioned medium
derived from fibroblasts. Our studies indicate that a proteolytic
cascade that depends on stromal/tumor cell interactions facilitates the
ability of A2058 melanoma cells to invade a matrix of type I collagen.
This cascade activates latent MMP-1 and involves both serine
proteinases and MMPs, particularly stromelysin 1 (MMP-3).
All-trans-retinoic acid (10 Medicine,
¶ Pharmacology/Toxicology, and ** Biochemistry, Dartmouth Medical
School, Hanover, New Hampshire 03755 and the Department of
Biochemistry, §§ University of Kansas Medical Center,
Kansas City, Kansas 66160
6 M)
suppresses the invasion of tumor cells by several mechanisms that
include suppression of MMP synthesis and an increase in levels of
tissue inhibitor of metalloproteinases 1 and 2. We conclude that
invasion of stromal collagen by A2058 melanoma cells is mediated by a
novel host/tumor cell interaction in which a proteolytic cascade
culminates in the activation of pro-MMP-1 and tumor cell invasion.
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