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Identification
- Generic Name
- Marimastat
- DrugBank Accession Number
- DB00786
- Background
Used in the treatment of cancer, Marmiastat is an angiogenesis and metastasis inhibitor. As an angiogenesis inhibitor it limits the growth and production of blood vessels. As an antimetatstatic agent it prevents malignant cells from breaching the basement membranes.
- Type
- Small Molecule
- Groups
- Investigational
- Structure
Structure for Marimastat (DB00786)
- Weight
- Average: 331.4079
Monoisotopic: 331.210721053 - Chemical Formula
- C15H29N3O5
- Synonyms
- Marimastat
- External IDs
- BB 2516
- BB-2516
- GI 5712
- GI-5712
- KB-R 8898
- TA 2516
- TA-2516
Pharmacology
- Indication
For the treatment of various cancers
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Used in the treatment of cancer, it is an angiogenesis and metastasis inhibitor. As an angiogenesis inhibitor it limits the growth and production of blood vessels. As an antimetatstatic agent it prevents malignant cells from breaching the basement membranes.
- Mechanism of action
Marimastat is a broad spectrum matrix metalloprotease inhibitor. It mimics the peptide structure of natural MMP substrates and binds to matrix metalloproteases, thereby preventing the degradation of the basement membrane by these proteases. This antiprotease action prevents the migration of endothelial cells needed to form new blood vessels. Inhibition of MMPs also prevents the entry and exit of tumor cells into existing blood cells, thereby preventing metastasis.
Target Actions Organism AInterstitial collagenase inhibitorHumans A72 kDa type IV collagenase inhibitorHumans AStromelysin-1 antagonistHumans AMatrilysin antagonistHumans ANeutrophil collagenase inhibitorHumans AMatrix metalloproteinase-9 inhibitorHumans AStromelysin-2 antagonistHumans AStromelysin-3 antagonistHumans AMacrophage metalloelastase inhibitorHumans ACollagenase 3 inhibitorHumans AMatrix metalloproteinase-14 inhibitorHumans AMatrix metalloproteinase-15 inhibitorHumans AMatrix metalloproteinase-16 inhibitorHumans AMatrix metalloproteinase-17 inhibitorHumans AMatrix metalloproteinase-19 inhibitorHumans AMatrix metalloproteinase-20 inhibitorHumans AMatrix metalloproteinase-21 inhibitorHumans AMatrix metalloproteinase-23 inhibitorHumans AMatrix metalloproteinase-24 inhibitorHumans AMatrix metalloproteinase-25 inhibitorHumans AMatrix metalloproteinase-26 inhibitorHumans AMatrix metalloproteinase-27 inhibitorHumans AMatrix metalloproteinase-28 inhibitorHumans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- Not Available
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as secondary alcohols. These are compounds containing a secondary alcohol functional group, with the general structure HOC(R)(R') (R,R'=alkyl, aryl).
- Kingdom
- Organic compounds
- Super Class
- Organic oxygen compounds
- Class
- Organooxygen compounds
- Sub Class
- Alcohols and polyols
- Direct Parent
- Secondary alcohols
- Alternative Parents
- Propargyl-type 1,3-dipolar organic compounds / Carboximidic acids / Organopnictogen compounds / Organonitrogen compounds / Hydrocarbon derivatives
- Substituents
- Aliphatic acyclic compound / Carboximidic acid / Carboximidic acid derivative / Hydrocarbon derivative / Organic 1,3-dipolar compound / Organic nitrogen compound / Organonitrogen compound / Organopnictogen compound / Propargyl-type 1,3-dipolar organic compound / Secondary alcohol
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- tricarboxylic acid triamide (CHEBI:50662)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- D5EQV23TDS
- CAS number
- 154039-60-8
- InChI Key
- OCSMOTCMPXTDND-OUAUKWLOSA-N
- InChI
- InChI=1S/C15H29N3O5/c1-8(2)7-9(10(19)13(21)18-23)12(20)17-11(14(22)16-6)15(3,4)5/h8-11,19,23H,7H2,1-6H3,(H,16,22)(H,17,20)(H,18,21)/t9-,10+,11-/m1/s1
- IUPAC Name
- (2S,3R)-N'-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N,2-dihydroxy-3-(2-methylpropyl)butanediamide
- SMILES
- CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)[C@H](O)C(=O)NO)C(C)(C)C
References
- General References
- Not Available
- External Links
- Human Metabolome Database
- HMDB0014924
- PubChem Compound
- 119031
- PubChem Substance
- 46505547
- ChemSpider
- 106358
- BindingDB
- 50063917
- ChEBI
- 50662
- ChEMBL
- CHEMBL279785
- ZINC
- ZINC000001544157
- Therapeutic Targets Database
- DCL000005
- PharmGKB
- PA164748329
- PDBe Ligand
- 097
- Wikipedia
- Marimastat
- PDB Entries
- 1r55 / 2jih / 3hy7
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample data3 Completed Treatment Breast Cancer 1 somestatus stop reason just information to hide 3 Completed Treatment Lung Cancer 2 somestatus stop reason just information to hide 1 Completed Treatment Vascular Anomalies 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source logP 0.4 Not Available - Predicted Properties
Property Value Source Water Solubility 3.38 mg/mL ALOGPS logP 0.41 ALOGPS logP -0.059 Chemaxon logS -2 ALOGPS pKa (Strongest Acidic) 8.61 Chemaxon pKa (Strongest Basic) -1 Chemaxon Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 5 Chemaxon Hydrogen Donor Count 5 Chemaxon Polar Surface Area 127.76 Å2 Chemaxon Rotatable Bond Count 8 Chemaxon Refractivity 84.2 m3·mol-1 Chemaxon Polarizability 35.04 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter Yes Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.516 Blood Brain Barrier + 0.5834 Caco-2 permeable - 0.6426 P-glycoprotein substrate Non-substrate 0.5779 P-glycoprotein inhibitor I Non-inhibitor 0.7079 P-glycoprotein inhibitor II Non-inhibitor 0.8359 Renal organic cation transporter Non-inhibitor 0.9815 CYP450 2C9 substrate Non-substrate 0.8498 CYP450 2D6 substrate Non-substrate 0.8202 CYP450 3A4 substrate Non-substrate 0.5449 CYP450 1A2 substrate Non-inhibitor 0.8587 CYP450 2C9 inhibitor Non-inhibitor 0.8594 CYP450 2D6 inhibitor Non-inhibitor 0.8881 CYP450 2C19 inhibitor Non-inhibitor 0.8108 CYP450 3A4 inhibitor Non-inhibitor 0.8754 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9651 Ames test Non AMES toxic 0.5559 Carcinogenicity Non-carcinogens 0.6499 Biodegradation Not ready biodegradable 0.9886 Rat acute toxicity 2.5082 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9979 hERG inhibition (predictor II) Non-inhibitor 0.9557
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
Spectrum Spectrum Type Splash Key Predicted GC-MS Spectrum - GC-MS Predicted GC-MS splash10-0bt9-9461000000-742ee3dab4b7fe4f11c2 Predicted MS/MS Spectrum - 10V, Positive (Annotated) Predicted LC-MS/MS splash10-001i-2269000000-570e7adab98691542b49 Predicted MS/MS Spectrum - 10V, Negative (Annotated) Predicted LC-MS/MS splash10-03l3-1393000000-d01d82a88548804d9365 Predicted MS/MS Spectrum - 20V, Negative (Annotated) Predicted LC-MS/MS splash10-0006-9710000000-4e320e9c924301ad3671 Predicted MS/MS Spectrum - 20V, Positive (Annotated) Predicted LC-MS/MS splash10-03di-2490000000-d4f9f14d1f7362ee4289 Predicted MS/MS Spectrum - 40V, Negative (Annotated) Predicted LC-MS/MS splash10-0ce9-9531000000-616faf0bc26d238a2fc9 Predicted MS/MS Spectrum - 40V, Positive (Annotated) Predicted LC-MS/MS splash10-0bu0-9520000000-f8beed596431f4db036a Predicted 1H NMR Spectrum 1D NMR Not Applicable Predicted 13C NMR Spectrum 1D NMR Not Applicable - Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 189.1020327 predictedDarkChem Lite v0.1.0 [M-H]- 188.3190327 predictedDarkChem Lite v0.1.0 [M-H]- 188.3617 predictedDeepCCS 1.0 (2019) [M+H]+ 190.0791327 predictedDarkChem Lite v0.1.0 [M+H]+ 189.4027327 predictedDarkChem Lite v0.1.0 [M+H]+ 190.7197 predictedDeepCCS 1.0 (2019) [M+Na]+ 189.2378327 predictedDarkChem Lite v0.1.0 [M+Na]+ 188.5905327 predictedDarkChem Lite v0.1.0 [M+Na]+ 197.39293 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369)
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP1
- Uniprot ID
- P03956
- Uniprot Name
- Interstitial collagenase
- Molecular Weight
- 54006.61 Da
References
- Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [Article]
- Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP2
- Uniprot ID
- P08253
- Uniprot Name
- 72 kDa type IV collagenase
- Molecular Weight
- 73881.695 Da
References
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Treharne GD, Boyle JR, Goodall S, Loftus IM, Bell PR, Thompson MM: Marimastat inhibits elastin degradation and matrix metalloproteinase 2 activity in a model of aneurysm disease. Br J Surg. 1999 Aug;86(8):1053-8. [Article]
- Fanchon S, Bourd K, Septier D, Everts V, Beertsen W, Menashi S, Goldberg M: Involvement of matrix metalloproteinases in the onset of dentin mineralization. Eur J Oral Sci. 2004 Apr;112(2):171-6. [Article]
- Bernardo MM, Brown S, Li ZH, Fridman R, Mobashery S: Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. J Biol Chem. 2002 Mar 29;277(13):11201-7. Epub 2002 Jan 14. [Article]
- Shinoda K, Shibuya M, Hibino S, Ono Y, Matsuda K, Takemura A, Zou D, Kokubo Y, Takechi A, Kudoh S: A novel matrix metalloproteinase inhibitor, FYK-1388 suppresses tumor growth, metastasis and angiogenesis by human fibrosarcoma cell line. Int J Oncol. 2003 Feb;22(2):281-8. [Article]
- Bourd-Boittin K, Fridman R, Fanchon S, Septier D, Goldberg M, Menashi S: Matrix metalloproteinase inhibition impairs the processing, formation and mineralization of dental tissues during mouse molar development. Exp Cell Res. 2005 Apr 1;304(2):493-505. Epub 2005 Jan 11. [Article]
- Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Antagonist
- General Function
- Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed:11029580, PubMed:1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed:2383557). Acts also intracellularly (PubMed:22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311)
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP3
- Uniprot ID
- P08254
- Uniprot Name
- Stromelysin-1
- Molecular Weight
- 53976.84 Da
References
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Antagonist
- General Function
- Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP7
- Uniprot ID
- P09237
- Uniprot Name
- Matrilysin
- Molecular Weight
- 29676.62 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Can degrade fibrillar type I, II, and III collagens
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP8
- Uniprot ID
- P22894
- Uniprot Name
- Neutrophil collagenase
- Molecular Weight
- 53411.72 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide
- Specific Function
- Collagen binding
- Gene Name
- MMP9
- Uniprot ID
- P14780
- Uniprot Name
- Matrix metalloproteinase-9
- Molecular Weight
- 78457.51 Da
References
- Underwood CK, Min D, Lyons JG, Hambley TW: The interaction of metal ions and Marimastat with matrix metalloproteinase 9. J Inorg Biochem. 2003 Jun 1;95(2-3):165-70. [Article]
- Nenan S, Lagente V, Planquois JM, Hitier S, Berna P, Bertrand CP, Boichot E: Metalloelastase (MMP-12) induced inflammatory response in mice airways: effects of dexamethasone, rolipram and marimastat. Eur J Pharmacol. 2007 Mar 15;559(1):75-81. Epub 2006 Dec 12. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Antagonist
- General Function
- Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP10
- Uniprot ID
- P09238
- Uniprot Name
- Stromelysin-2
- Molecular Weight
- 54150.745 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Antagonist
- General Function
- May play an important role in the progression of epithelial malignancies
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP11
- Uniprot ID
- P24347
- Uniprot Name
- Stromelysin-3
- Molecular Weight
- 54589.395 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3
- Specific Function
- Calcium ion binding
- Gene Name
- MMP12
- Uniprot ID
- P39900
- Uniprot Name
- Macrophage metalloelastase
- Molecular Weight
- 54001.175 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- 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
- Specific Function
- Calcium ion binding
- Gene Name
- MMP13
- Uniprot ID
- P45452
- Uniprot Name
- Collagenase 3
- Molecular Weight
- 53819.32 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Endopeptidase that degrades various components of the extracellular matrix such as collagen (PubMed:8015608). Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). Activates progelatinase A/MMP2, thereby acting as a positive regulator of cell growth and migration (PubMed:22065321, PubMed:8015608). Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657, PubMed:22065321). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a regulator of Notch signaling by mediating cleavage and inhibition of DLL1 (PubMed:21572390). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140). Acts as a negative regulator of the GDF15-GFRAL aversive response by mediating cleavage and inactivation of GFRAL (PubMed:35177851)
- Specific Function
- Endopeptidase activity
- Gene Name
- MMP14
- Uniprot ID
- P50281
- Uniprot Name
- Matrix metalloproteinase-14
- Molecular Weight
- 65893.445 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A
- Specific Function
- Enzyme activator activity
- Gene Name
- MMP15
- Uniprot ID
- P51511
- Uniprot Name
- Matrix metalloproteinase-15
- Molecular Weight
- 75806.45 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells
- Specific Function
- Enzyme activator activity
- Gene Name
- MMP16
- Uniprot ID
- P51512
- Uniprot Name
- Matrix metalloproteinase-16
- Molecular Weight
- 69521.03 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin
- Specific Function
- Enzyme activator activity
- Gene Name
- MMP17
- Uniprot ID
- Q9ULZ9
- Uniprot Name
- Matrix metalloproteinase-17
- Molecular Weight
- 66652.23 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP19
- Uniprot ID
- Q99542
- Uniprot Name
- Matrix metalloproteinase-19
- Molecular Weight
- 57356.565 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP20
- Uniprot ID
- O60882
- Uniprot Name
- Matrix metalloproteinase-20
- Molecular Weight
- 54386.5 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway (PubMed:26429889, PubMed:26437028). Cleaves alpha-1-antitrypsin (PubMed:12617721)
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP21
- Uniprot ID
- Q8N119
- Uniprot Name
- Matrix metalloproteinase-21
- Molecular Weight
- 65042.83 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity)
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP23B
- Uniprot ID
- O75900
- Uniprot Name
- Matrix metalloproteinase-23
- Molecular Weight
- 43934.385 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity)
- Specific Function
- Cadherin binding
- Gene Name
- MMP24
- Uniprot ID
- Q9Y5R2
- Uniprot Name
- Matrix metalloproteinase-24
- Molecular Weight
- 73230.93 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- May activate progelatinase A
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP25
- Uniprot ID
- Q9NPA2
- Uniprot Name
- Matrix metalloproteinase-25
- Molecular Weight
- 62553.445 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP26
- Uniprot ID
- Q9NRE1
- Uniprot Name
- Matrix metalloproteinase-26
- Molecular Weight
- 29708.27 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP27
- Uniprot ID
- Q9H306
- Uniprot Name
- Matrix metalloproteinase-27
- Molecular Weight
- 59025.39 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Can degrade casein. Could play a role in tissues homeostasis and repair
- Specific Function
- Metalloendopeptidase activity
- Gene Name
- MMP28
- Uniprot ID
- Q9H239
- Uniprot Name
- Matrix metalloproteinase-28
- Molecular Weight
- 58938.525 Da
References
Drug created at June 13, 2005 13:24 / Updated at May 03, 2024 10:05