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MMP-14 (MT1-MMP)
MMP-15 (MT2-MMP)
MMP-16 (MT3-MMP)
MMP-1 (Collagenase-1)
MMP-13 (Collagenase-3)
MMP-2 (Gelatinase A)
Cathepsin K
Hinge
Hemopexin-like
Pro-domain
Furin activation site
Transmembrane
Fibronectin repeat
Metalloproteinase
Cytoplasmic tail
Cysteine protease
Fig. 3.1 Mammalian collagenases. The figure depicts the domain structure of the seven
mammalian proteases with validated roles in physiological turnover of native collagen. The
specific domain types are indicated. The six MMP collagenases all cleave fibrillar collagens at a
single conserved Gly-Ile or Gly-Leu bond that is located three quarters of the distance from the
N-terminus toward the C-terminus of the collagen triple helix. Cathepsin K cleaves the collagen
at multiple sites within the triple helix and also degrades the nonhelical N- and C-telopeptide
regions. Proteases capable of cleaving collagens in their nonhelical globular regions, after
denaturation of collagen caused by initial collagenase cleavage, or proteases engaged in bulk
collagen turnover within the lysosome are not depicted [modified from Parks et al. ( 2004 )]
in humans and mice has different consequences (Itoh et al. 1997 ; Martignetti et al.
2001 ), and no true ortholog of human MMP-1 has been found in the mouse (Puente
et al. 2003 ). Nevertheless, a coherent and somewhat unexpected picture has
emerged, in which the membrane-bound MMP collagenases (MMP-14, MMP-15,
and MMP-16) appear to be the enzymes that are most important for collagen
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