Top ▲
Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
« Hide
More detailed introduction
Matrix metalloproteinases (MMP) are calcium- and zinc-dependent proteinases regulating the extracellular matrix and are often divided (e.g. [13]) on functional and structural bases into gelatinases, collagenases, stromyelinases and matrilysins, as well as membrane type-MMP (MT-MMP).
MMP2
C
Show summary »
More detailed page |
MMP8
C
Show summary »
More detailed page |
MMP21 Show summary » |
MMP23 Show summary » |
MMP27 Show summary » |
MMP28 Show summary » |
Database page citation:
M10: Matrix metallopeptidase. Accessed on 10/12/2023. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=738.
Concise Guide to PHARMACOLOGY citation:
Alexander SP, Fabbro D, Kelly E, Mathie A, Peters JA, Veale EL et al. (2021) THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Enzymes. Br J Pharmacol. 178 Suppl 1:S313-S411.
A number of small molecule ‘broad spectrum’ inhibitors of MMP have been described, including marimastat and batimastat.
Tissue inhibitors of metalloproteinase (TIMP) proteins are endogenous inhibitors acting to chelate MMP proteins: TIMP1 (TIMP1, P01033), TIMP2 (TIMP2, P16035), TIMP3 (TIMP3, P35625), TIMP4 (TIMP4, Q99727)