Identification

Name
Marimastat
Accession Number
DB00786  (APRD00559)
Type
Small Molecule
Groups
Approved, Investigational
Description

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.

Structure
Thumb
Synonyms
  • Marimastat
External IDs
BB 2516 / BB-2516 / GI 5712 / GI-5712 / KB-R 8898 / TA 2516 / TA-2516
Categories
UNII
D5EQV23TDS
CAS number
154039-60-8
Weight
Average: 331.4079
Monoisotopic: 331.210721053
Chemical Formula
C15H29N3O5
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)[[email protected]@H](NC(=O)[[email protected]](CC(C)C)[[email protected]](O)C(=O)NO)C(C)(C)C

Pharmacology

Indication

For the treatment of various cancers

Structured Indications
Not Available
Pharmacodynamics

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.

TargetActionsOrganism
AInterstitial collagenase
inhibitor
Human
A72 kDa type IV collagenase
inhibitor
Human
AStromelysin-1
antagonist
Human
AMatrilysin
antagonist
Human
ANeutrophil collagenase
inhibitor
Human
AMatrix metalloproteinase-9
inhibitor
Human
AStromelysin-2
antagonist
Human
AStromelysin-3
antagonist
Human
AMacrophage metalloelastase
inhibitor
Human
ACollagenase 3
inhibitor
Human
AMatrix metalloproteinase-14
inhibitor
Human
AMatrix metalloproteinase-15
inhibitor
Human
AMatrix metalloproteinase-16
inhibitor
Human
AMatrix metalloproteinase-17
inhibitor
Human
AMatrix metalloproteinase-19
inhibitor
Human
AMatrix metalloproteinase-20
inhibitor
Human
AMatrix metalloproteinase-21
inhibitor
Human
AMatrix metalloproteinase-23
inhibitor
Human
AMatrix metalloproteinase-24
inhibitor
Human
AMatrix metalloproteinase-25
inhibitor
Human
AMatrix metalloproteinase-26
inhibitor
Human
AMatrix metalloproteinase-27
inhibitor
Human
AMatrix metalloproteinase-28
inhibitor
Human
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
Toxicity
Not Available
Affected organisms
  • Humans and other mammals
Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
Not Available
Food Interactions
Not Available

References

Synthesis Reference
Not Available
General References
Not Available
External Links
Human Metabolome Database
HMDB14924
PubChem Compound
119031
PubChem Substance
46505547
ChemSpider
106358
BindingDB
50063917
ChEBI
50662
ChEMBL
CHEMBL279785
Therapeutic Targets Database
DCL000005
PharmGKB
PA164748329
HET
097
Wikipedia
Marimastat
ATC Codes
Not Available
AHFS Codes
Not Available
PDB Entries
FDA label
Not Available
MSDS
Not Available

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
1CompletedTreatmentVascular Anomalies1
3CompletedTreatmentCancer, Breast1
3CompletedTreatmentLung Cancers2

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage forms
Not Available
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
PropertyValueSource
logP0.4Not Available
Predicted Properties
PropertyValueSource
Water Solubility3.38 mg/mLALOGPS
logP0.41ALOGPS
logP-0.059ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)8.61ChemAxon
pKa (Strongest Basic)-1ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count5ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area127.76 Å2ChemAxon
Rotatable Bond Count8ChemAxon
Refractivity84.2 m3·mol-1ChemAxon
Polarizability34.99 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET features
PropertyValueProbability
Human Intestinal Absorption+0.516
Blood Brain Barrier+0.5834
Caco-2 permeable-0.6426
P-glycoprotein substrateNon-substrate0.5779
P-glycoprotein inhibitor INon-inhibitor0.7079
P-glycoprotein inhibitor IINon-inhibitor0.8359
Renal organic cation transporterNon-inhibitor0.9815
CYP450 2C9 substrateNon-substrate0.8498
CYP450 2D6 substrateNon-substrate0.8202
CYP450 3A4 substrateNon-substrate0.5449
CYP450 1A2 substrateNon-inhibitor0.8587
CYP450 2C9 inhibitorNon-inhibitor0.8594
CYP450 2D6 inhibitorNon-inhibitor0.8881
CYP450 2C19 inhibitorNon-inhibitor0.8108
CYP450 3A4 inhibitorNon-inhibitor0.8754
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.9651
Ames testNon AMES toxic0.5559
CarcinogenicityNon-carcinogens0.6499
BiodegradationNot ready biodegradable0.9886
Rat acute toxicity2.5082 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9979
hERG inhibition (predictor II)Non-inhibitor0.9557
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Not Available
Spectra
SpectrumSpectrum TypeSplash Key
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSNot Available
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSNot Available

Taxonomy

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
Secondary alcohol / Organic 1,3-dipolar compound / Propargyl-type 1,3-dipolar organic compound / Carboximidic acid derivative / Carboximidic acid / Organic nitrogen compound / Organopnictogen compound / Hydrocarbon derivative / Organonitrogen compound / Aliphatic acyclic compound
Molecular Framework
Aliphatic acyclic compounds
External Descriptors
tricarboxylic acid triamide (CHEBI:50662)

Targets

Details
1. Interstitial collagenase
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protei...
Gene Name
MMP1
Uniprot ID
P03956
Uniprot Name
Interstitial collagenase
Molecular Weight
54006.61 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
  3. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rup...
Gene Name
MMP2
Uniprot ID
P08253
Uniprot Name
72 kDa type IV collagenase
Molecular Weight
73881.695 Da
References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
  2. 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. [PubMed:10460642]
  3. 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. [PubMed:15056115]
  4. 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. [PubMed:11790786]
  5. 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. [PubMed:12527923]
  6. 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. [PubMed:15748894]
Details
3. Stromelysin-1
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Antagonist
General Function
Zinc ion binding
Specific Function
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Gene Name
MMP3
Uniprot ID
P08254
Uniprot Name
Stromelysin-1
Molecular Weight
53976.84 Da
References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
Details
4. Matrilysin
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Antagonist
General Function
Zinc ion binding
Specific Function
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
Gene Name
MMP7
Uniprot ID
P09237
Uniprot Name
Matrilysin
Molecular Weight
29676.62 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Details
5. Neutrophil collagenase
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Can degrade fibrillar type I, II, and III collagens.
Gene Name
MMP8
Uniprot ID
P22894
Uniprot Name
Neutrophil collagenase
Molecular Weight
53411.72 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves...
Gene Name
MMP9
Uniprot ID
P14780
Uniprot Name
Matrix metalloproteinase-9
Molecular Weight
78457.51 Da
References
  1. 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. [PubMed:12763661]
  2. 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. [PubMed:17234180]
  3. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Antagonist
General Function
Zinc ion binding
Specific Function
Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Gene Name
MMP10
Uniprot ID
P09238
Uniprot Name
Stromelysin-2
Molecular Weight
54150.745 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Antagonist
General Function
Zinc ion binding
Specific Function
May play an important role in the progression of epithelial malignancies.
Gene Name
MMP11
Uniprot ID
P24347
Uniprot Name
Stromelysin-3
Molecular Weight
54589.395 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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 hydropho...
Gene Name
MMP12
Uniprot ID
P39900
Uniprot Name
Macrophage metalloelastase
Molecular Weight
54001.175 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Details
10. Collagenase 3
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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 co...
Gene Name
MMP13
Uniprot ID
P45452
Uniprot Name
Collagenase 3
Molecular Weight
53819.32 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganizatio...
Gene Name
MMP14
Uniprot ID
P50281
Uniprot Name
Matrix metalloproteinase-14
Molecular Weight
65893.445 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
Gene Name
MMP15
Uniprot ID
P51511
Uniprot Name
Matrix metalloproteinase-15
Molecular Weight
75806.45 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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....
Gene Name
MMP16
Uniprot ID
P51512
Uniprot Name
Matrix metalloproteinase-16
Molecular Weight
69521.03 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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 mediator...
Gene Name
MMP17
Uniprot ID
Q9ULZ9
Uniprot Name
Matrix metalloproteinase-17
Molecular Weight
66652.23 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditi...
Gene Name
MMP19
Uniprot ID
Q99542
Uniprot Name
Matrix metalloproteinase-19
Molecular Weight
57356.565 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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 p...
Gene Name
MMP20
Uniprot ID
O60882
Uniprot Name
Matrix metalloproteinase-20
Molecular Weight
54386.5 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin.
Gene Name
MMP21
Uniprot ID
Q8N119
Uniprot Name
Matrix metalloproteinase-21
Molecular Weight
65042.83 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity).
Gene Name
MMP23A
Uniprot ID
O75900
Uniprot Name
Matrix metalloproteinase-23
Molecular Weight
43934.385 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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 nocicept...
Gene Name
MMP24
Uniprot ID
Q9Y5R2
Uniprot Name
Matrix metalloproteinase-24
Molecular Weight
73230.93 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
May activate progelatinase A.
Gene Name
MMP25
Uniprot ID
Q9NPA2
Uniprot Name
Matrix metalloproteinase-25
Molecular Weight
62553.445 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific 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.
Gene Name
MMP26
Uniprot ID
Q9NRE1
Uniprot Name
Matrix metalloproteinase-26
Molecular Weight
29708.27 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.
Gene Name
MMP27
Uniprot ID
Q9H306
Uniprot Name
Matrix metalloproteinase-27
Molecular Weight
59025.39 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]
Kind
Protein
Organism
Human
Pharmacological action
Yes
Actions
Inhibitor
General Function
Zinc ion binding
Specific Function
Can degrade casein. Could play a role in tissues homeostasis and repair.
Gene Name
MMP28
Uniprot ID
Q9H239
Uniprot Name
Matrix metalloproteinase-28
Molecular Weight
58938.525 Da
References
  1. Heath EI, Grochow LB: Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs. 2000 May;59(5):1043-55. [PubMed:10852638]
  2. Belotti D, Paganoni P, Giavazzi R: MMP inhibitors: experimental and clinical studies. Int J Biol Markers. 1999 Oct-Dec;14(4):232-8. [PubMed:10669951]

Drug created on June 13, 2005 07:24 / Updated on October 02, 2017 04:45