193807-58-8

Usage

Uses

Used in Research Applications:
GELATINASE A is used as a standard in zymography for measuring the gelatinolytic activity of MMP2. This application is essential for understanding the enzyme's role in various biological processes and its potential involvement in diseases.
Used in Biomedical Applications:
GELATINASE A is used as an enzymatic method for the dissociation of brain tissue into single cells. This technique is vital for studying cellular interactions and functions within the brain, as well as for developing potential therapeutic strategies for neurological disorders.
Used in Pharmaceutical Industry:
GELATINASE A is used as a target for drug development in the pharmaceutical industry. Inhibitors of GELATINASE A have the potential to treat various diseases, such as cancer, where MMP2 is involved in tumor growth, invasion, and metastasis.
Used in Diagnostics:
GELATINASE A can be used as a biomarker in diagnostics to assess the risk of certain diseases or to monitor the progression of a disease. Elevated levels of MMP2 have been associated with various pathological conditions, making it a valuable indicator for diagnostic purposes.

Biological Activity

mmp-2/mmp-9 inhibitor i is a potent inhibitor of matrix metalloproteinase-2 (mmp-2) and mmp-9.matrix metalloproteinase (mmp), a typical metalloproteinase, requires zinc ion at its active sites. as many as 18 kinds of mmp have been identified and cloned and are collectively called the mmp family.

Biochem/physiol Actions

Matrix Metalloproteinase-2 (MMP-2) cleaves gelatin, type IV, V, VII, X, and XI collagens, fibronectin, elastin, laminin, proteoglycans and a range of non extracellular matrix (ECM ) components. MMP-2 cleaves native type I collagen to N-terminal ? and C-terminal ? fragments identical to those generated by interstitial collagenases. MMP2 and MMP9 play an essential role in matrix degradation and they are implicated in the maintenance of neovascularization. In mice, deletion or inhibition of MMP2 protects against myocardial rupture.

in vitro

mmp-2/mmp-9 inhibitor i was identified as a potent inhibitor of matrix metalloproteinase-2 (mmp-2) and mmp-9 with ic50 values of 310 and 240 nm, respectively. mmp-2/mmp-9 inhibitor i acted by binding zinc at the active site of these mmps. mmp-2/mmp-9 inhibitor i was found to be able to block mmp-2/mmp-9-dependent invasion in cell culture model [1].

in vivo

both hydroxamic acid and carboxylic acid analogs of mmp-2/mmp-9 inhibitor i were evaluated for their inhibitory activities in animal cancer models. results showed that lung colonization of lewis lung carcinoma cells was suppressed by these inhibitors significantly. in addition, antitumor activity was also observed in the human lung cancer model. ma44 cells growed as a solid tumor on the peritoneum after being implanted ip, and mice bearing ma44 eventually died within 3 to 4 weeks. daily oral administration of compound 5l led to prolonged survival of ma44-bearing mice [1].

IC 50

310 and 240 nm for mmp-2 and mmp-9, respectively

references

[1] tamura, y. ,watamane, f.,nakatani, t., et al. highly selective and orally active inhibitors of type iv collagenase (mmp-9 and mmp-2): n-sulfonylamino acid derivatives. j. med. chem. 41(4), 640-649 (1998).

Upstream product

• 13033-84-6 D-phenylalanine methyl ester hydrochloride 
• 1623-93-4 4-diphenylsulfonyl chloride 
• 1469273-31-1 C₂₅H₂₇NO₄S 
• 3081-28-5 D-phenylalanine tert-butyl ester 
• 193810-34-3 (R)-2-(Biphenyl-4-sulfonylamino)-3-phenyl-propionic acid benzyl ester 

Downstream Products

• 193807-60-2 (2R)-[(4-biphenylylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide 
• 193810-35-4 (R)-N-Benzyloxy-2-(biphenyl-4-sulfonylamino)-3-phenyl-propionamide 

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Various N-sulfonylamino acid derivatives were synthesized and evaluated for their in vitro and in vivo activities to inhibit type IV collagenase (MMP-9 and MMP-2). When the amino acid residue and the sulfonamide moiety were modified, their inhibitory activities were greatly affected by the structure of the sulfonamide moiety. A series of aryl sulfonamide derivatives containing biaryl, tetrazole, amide, and triple bond were found to be potent and highly selective inhibitors of MMP-9 and MMP-2. In addition, these compounds were orally active in animal models of tumor growth and metastasis. These results revealed the potential of the N-sulfonylamino acid derivatives as a new type of candidate drug for the treatment of cancer.