MMP14

(redirected from MT1MMP)

MMP14

A gene on chromosome 14q11-q12 that encodes matrix metalloproteinase 14, which specifically activates progelatinase A. It may be involved in actin cytoskeleton reorganisation by cleaving PTK7. Unlike other matrix metalloproteinases, which are secreted as inactive proproteins and activated when cleaved by extracellular proteinases, MMP14 is a transmembrane protein that is activated from its precursor by furin endopeptidase cleavage.

Molecular pathology
MMP14 may trigger invasion by tumour cells by activating progelatinase A on the surface of tumour cells.
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Variables Values [a.sub.0] 2.0 x [10.sup.6] [M] [b.sub.0] 1.0 x [10.sup.6] [M] [c.sub.0] 1.0 x [10.sup.6] [M] [k.sub.1] 2.1 x [10.sup.7] [M.sup.-1][s.sup.-1] [l.sub.1] 0 [M.sup.-1][s.sup.-1] [k.sub.2] 2.74 x [10.sup.6] [M.sup.-1][s.sup.-1] [l.sub.2] 2.0 x [10.sup.-4] [M.sup.-1][s.sup.-1] [k.sub.3] 2.0 x [10.sup.6] [M.sup.-1][s.sup.-1] [l.sub.3] 1.0 x [10.sup.-2] [M.sup.-1][s.sup.-1] FIGURE 2: Binding sites of a (MMP2), b (TIMP2), and c (MT1MMP).
Rapti et al., "The activity of a designer tissue inhibitor of metalloproteinases (TIMP)-1 against native membrane type 1 matrix metalloproteinase (MT1MMP) in a cell-based environment," Cancer Letters, vol.
The variable ability of tumor cell lines to bind progelatinase A with or without enzyme activation suggests the presence of a progelatinase A receptor distinct from MT1MMP receptor, such as integrin [alpha]v[beta]3 of the surface of cultured melanoma cells [101].
Estrogen deficiency induced by ovariectomy gives rise to a reduction of active MMP-2 in the initial phase and a concurrent elevation of MMP-2 and MT1MMP expression in latter period [54].
Bone marrow-derived stem cells (BMSCs) induce an angiogenic effect and elicit vessel morphogenesis both in vitro and in vivo depending on proteolytic ability of MT1MMP [68].