Activation of proMMP9 by proteases

Stable Identifier
Reaction [transition]
Homo sapiens
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proMMP9 can be activated by trypsin and chymotrypsin (Sopata & Dancewicz 1974), tissue kallikrein (Tschesche et al. 1989, Desrivieres et al. 1993), cathepsin G (Murphy et al. 1980), and trypsin-2 (Sorsa et al. 1997). This appears to be a one-step activation; the single peptide bond cleaved by trypsin-2 in proMMP-9 is Arg106-Phe107. Modes of activation by other proteases are unclear. Activation is inhibited by endostatin (Nyberg et al. 2003).

Literature References
PubMed ID Title Journal Year
2557753 Tissue kallikrein effectively activates latent matrix degrading metalloenzymes

Oberhoff, R, Tschesche, H, Michaelis, J, Fedrowitz, J, Kohnert, U

Adv Exp Med Biol 1989
9261109 Activation of type IV procollagenases by human tumor-associated trypsin-2

Sorsa, T, Tuuttila, A, Bergmann, U, Salo, T, Teronen, O, Koivunen, E, Leinonen, J, Tschesche, H, Tyynelä, J, Konttinen, YT, Heikkilä, P, Stenman, UH, Niemi, E, Osman, S

J Biol Chem 1997
4216367 Presence of a gelatin-specific proteinase and its latent form in human leucocytes

Sopata, I, Dancewicz, AM

Biochim Biophys Acta 1974
6263256 The latent collagenase and gelatinase of human polymorphonuclear neutrophil leucocytes

Baggiolini, M, Bretz, U, Reynolds, JJ, Murphy, G

Biochem J 1980
Catalyst Activity

serine-type endopeptidase activity of proMMP9 activating proteases [extracellular region]

This event is regulated