Regulation of Matrix Metalloproteinase Activity^a

Selective transduction of protease-rich tumors by matrix-metalloproteinase-targeted retroviral vectors

“…19 It was therefore important to determine whether the MMP-activatable vectors would be activated by MMP-rich cells in an in vivo setting. HT1080 and A431 tumor xenografts were therefore established in nude mice and concentrated stocks of the EGF-displaying and wild-type vectors were administered by direct intratumoral inoculation.…”

Expression of stromelysin-3 in the human placenta and placental bed

“…Indeed, cell-bound u-PA is a key enzyme in the initiation of the plasminogen activation cascade, a major pathway of extracellular proteolysis. Also, u-PA can convert the widely occurring zymogen plasminogen into enzymatically active plasmin (Dano et al, 1985;Liotta, Steeg and Stetler-Stevenson, 1991;P611~inen, Stephens and Vaheri, 1991), which can directly degrade various ECM glycoproteins (Montgomery et al, 1993) and activate other matrix-degrading enzymes, such as prointerstitial collagenase (He et al, 1989;Murphy et al, 1994), pro-gelatinase B and pro-stromelysin-1 which mediate this matrix degradation. As ST3 is able to cleave and inactivate the proteinase inhibitors cited above, the concomitant production of ST3 and plasmin (via u-PA activity) by trophoblastic cells could be seen as a prerequisite for initiating a potent proteolytic cascade that enables the degradation of most ECM components.…”

Cartilage tissue engineering for degenerative joint disease☆

“…Recently, IL-17 was found to activate not only collagenases MMP 3, and MMP13 but also aggrecanase 1 and thus has been proposed as a target for reducing cartilage degradation [71]. Control of MMP activity is achieved through tissue inhibitors of metalloproteinases (TIMPs) [72]. Imbalance between MMP activity and TIMP inhibition is a characteristic of OA cartilage leading to collagen type II degradation [73].…”