EC, EC, EC, Matrix metalloproteinase-13, MMP-13, Collagenase 3, MMP13, Matrix Metallopeptidase 13, Matrix Metalloproteinase 13 (Collagenase 3), EC 3.4.24.-, MANDP1, CLG3, MDST, EC 3.4.24, EC, EC, EC:3.4.24.-, Matrix Metalloproteinase 13


MMP13 (Matrix metalloproteinase 13) plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

KO Status


Drug Information

Drug Name





Clinical Trials




Pfizer Pharmaceuticals Ltd (China)

Pain, Osteoarthritis




Pfizer Pharmaceuticals Ltd (China)




Pfizer Pharmaceuticals Ltd (China)



CTS-1027, RS-130830, RO-1130830


F. Hoffmann-La Roche Ltd

Hepatitis C, Arthritis, Hepatitis C, Chronic


PG-116800, PG-530742, PGE-7113313


Procter & Gamble

Heart Failure, Myocardial Infarction, Cardiomegaly, Osteoarthritis, Knee, Osteoarthritis





Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects

Johnson A.R., Pavlovsky A.G., Ortwine D.F., Prior F., Man C.F., Bornemeier D.A., Banotai C.A., Mueller W.T., McConnell P., Yan C., Baragi V., Lesch C., Roark W.H., Wilson M., Datta K., Guzman R., Han H.K., Dyer R.D.,

J. Biol. Chem. 282:27781-27791(2007)

Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2

Maskos K., Lang R., Tschesche H., Bode W.,

J. Mol. Biol. 366:1222-1231(2007)

Discovery of potent, selective, and orally active carboxylic acid based inhibitors of matrix metalloproteinase-13

Monovich L.G., Tommasi R.A., Fujimoto R.A., Blancuzzi V., Clark K., Cornell W.D., Doti R., Doughty J., Fang J., Farley D., Fitt J., Ganu V., Goldberg R., Goldstein R., Lavoie S., Kulathila R., Macchia W., Parker D.T., McQuire L.W.,

J. Med. Chem. 52:3523-3538(2009)

Discovery of (pyridin-4-yl)-2H-tetrazole as a novel scaffold to identify highly selective matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis

Schnute M.E., O'Brien P.M., Nahra J., Morris M., Howard Roark W., Hanau C.E., Ruminski P.G., Scholten J.A., Fletcher T.R., Hamper B.C., Carroll J.N., Patt W.C., Shieh H.S., Collins B., Pavlovsky A.G., Palmquist K.E., Aston K.W., Hitchcock J., Sunyer T.,

Bioorg. Med. Chem. Lett. 20:576-580(2010)

Orally active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease

Becker D.P., Barta T.E., Bedell L.J., Boehm T.L., Bond B.R., Carroll J., Carron C.P., Decrescenzo G.A., Easton A.M., Freskos J.N., Funckes-Shippy C.L., Heron M., Hockerman S., Howard C.P., Kiefer J.R., Li M.H., Mathis K.J., McDonald J.J., Yao J.,

J. Med. Chem. 53:6653-6680(2010)

Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins

Devel L., Beau F., Amoura M., Vera L., Cassar-Lajeunesse E., Garcia S., Czarny B., Stura E.A., Dive V.,

J. Biol. Chem. 287:26647-26656(2012)

Hydantoin based inhibitors of MMP13--discovery of AZD6605

De Savi C., Waterson D., Pape A., Lamont S., Hadley E., Mills M., Page K.M., Bowyer J., Maciewicz R.A.,

Bioorg. Med. Chem. Lett. 23:4705-4712(2013)

Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain

Stura E.A., Visse R., Cuniasse P., Dive V., Nagase H.,

FASEB J. 27:4395-4405(2013)

MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMD(MO)

Kennedy A.M., Inada M., Krane S.M., Christie P.T., Harding B., Lopez-Otin C., Sanchez L.M., Pannett A.A.J., Dearlove A., Hartley C., Byrne M.H., Reed A.A.C., Nesbit M.A., Whyte M.P., Thakker R.V.,

J. Clin. Invest. 115:2832-2842(2005)

Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas

Freije J.M.P., Diez-Itza I., Balbin M., Sanchez L.M., Blasco R., Tolivia J., Lopez-Otin C.,

J. Biol. Chem. 269:16766-16773(1994)