Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase= gelatinase B) in osteoclasts: implications for bone resorption.
Y Okada, K Naka, K Kawamura… - … ; a journal of technical …, 1995 - europepmc.org
Y Okada, K Naka, K Kawamura, T Matsumoto, I Nakanishi, N Fujimoto, H Sato, M Seiki
Laboratory investigation; a journal of technical methods and pathology, 1995•europepmc.orgBackground Matrix metalloproteinase 9 (MMP-9, 92-kD gelatinase/type IV collagenase=
gelatinase B) is a member of the MMP gene family and implicated in tissue destruction in the
various pathophysiologic conditions. Our previous study showed that MMP-9 purified from
human fibrosarcoma cells can cleave the cross-link-containing NH (2)-terminal telopeptides
of the alpha 2 chain of type I collagen and collagen types III, IV, and V as well as gelatins.
gelatinase B) is a member of the MMP gene family and implicated in tissue destruction in the
various pathophysiologic conditions. Our previous study showed that MMP-9 purified from
human fibrosarcoma cells can cleave the cross-link-containing NH (2)-terminal telopeptides
of the alpha 2 chain of type I collagen and collagen types III, IV, and V as well as gelatins.
Background
Matrix metalloproteinase 9 (MMP-9, 92-kD gelatinase/type IV collagenase= gelatinase B) is a member of the MMP gene family and implicated in tissue destruction in the various pathophysiologic conditions. Our previous study showed that MMP-9 purified from human fibrosarcoma cells can cleave the cross-link-containing NH (2)-terminal telopeptides of the alpha 2 chain of type I collagen and collagen types III, IV, and V as well as gelatins.
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