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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).
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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
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MMP8
C
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MMP21 Show summary » |
MMP23 Show summary » |
MMP27 Show summary » |
MMP28 Show summary » |
Database page citation:
M10: Matrix metallopeptidase. Accessed on 14/02/2025. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=738.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.
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)