MMP1 inhibitors(Matrix metalloproteinase-1 inhibitors), MMP13 inhibitors(Matrix metalloproteinase 13 inhibitors), MMP8 inhibitors(Matrix metalloproteinase 8 inhibitors)

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Therapeutic Areas

Immune System DiseasesSkin and Musculoskeletal Diseases

Active Indication-

Inactive Indication

Rheumatoid Arthritis

Originator Organization

F. Hoffmann-La Roche Ltd.

Active Organization-

Inactive Organization

Roche Products Ltd.

Drug Highest PhaseDiscontinuedClinical

First Approval Date-

Regulation-

Structure/Sequence

Molecular FormulaC22H36N4O5

InChIKeyGFUITADOEPNRML-SJORKVTESA-N

CAS Registry190648-49-8

100 Clinical Results associated with Cipemastat

100 Translational Medicine associated with Cipemastat

100 Patents (Medical) associated with Cipemastat

Literatures (Medical) associated with Cipemastat

01 Feb 2022·Chemical Biology & Drug DesignQ4 · MEDICINE

Bioinformatics screening of ETV4 transcription factor oncogenes and identifying small‐molecular anticancer drugs

Q4 · MEDICINE

Article

Author: Nair, Achuthsankar S. ; I.V, Ambily Nath

AbstractThis bioinformatics study aimed to identify ETV4 transcription factor oncogenes and outline anticancer drugs for these genes. First, we collected known 61 ETV4 cancer targets that were framed as two classes of queries to screen against the multiomics resources in GeneMANIA. This method accessed and added functionally similar 20 genes to each set. These data were interpreted by hub genes, network clustering, gene ontology, and pathway analyses, and the results confirmed that all resultant genes were cancer promoters. The ETS‐binding motifs were identified from the promoter regions of these genes. Thus, 23 ETV4 targets were figured and those involved in oncogenesis were filtered as the following 16 putative nodes: MMP8, MMP14, KDR, BRIP1, CXCR1, GRB14, SHC2, SHC4, SH2B1, SH2B2, INPPL1, PTPN3, GNG12, SEMA4D, RHOA, and SPSB2. The transcriptional regulation of these oncogenes was coordinated by an extensive miRNA network that found to deregulate many cancer pathways. Using DgIb database, the high quality 6 oncogene‐drug combinations (MMP8‐CHEMBL1231240, MMP8‐Aminomethylamide, CXCR1‐Reparixin, SEMA4D‐Pepinemab, RHOA‐Clausine E, and SPSB2‐CHEMBL175296) were proposed. These findings may advance our understanding of novel neoplastic gene nexus of ETV4 and design treatment strategies for its modulation.

24 Sep 2019·BiochemistryQ3 · BIOLOGY

Development and Application of the Metalloprotease Activity Multiplexed Bead-Based Immunoassay (MAMBI)

Q3 · BIOLOGY

Article

Author: Ravindra, Kodihalli C. ; Isaacson, Keith B. ; Ramseier, Julie Y. ; Miller, Miles A. ; Chiswick, Evan L. ; Griffith, Linda G. ; Ahrens, Caroline C. ; Lauffenburger, Douglas A.

Metalloproteinases (MMPs) are zinc-dependent endopeptidases that cleave various proteins to regulate normal and diseased cellular functions, and as such, they play significant roles in human tissue development, homeostasis, and the pathogenesis of many diseases, including cancers, endometriosis, arthritis, etc. Most MMPs are produced as zymogenic latent enzymes that must be cleaved to activate their catalytic regions, and localized endogenous protein inhibitors further regulate activity. Accordingly, they operate within recursive networks to degrade extracellular matrix proteins and regulate cell signaling by cleaving growth factors and receptors at the cell surface and in the local pericellular environment. Thus, high-resolution information about the concentrations of specific active MMPs, revealing their intricate regulatory networks, may improve disease diagnosis and treatment. Here, we introduce a new and readily mastered method for measuring MMP activities in a multiplex fashion. We integrate aspects of activity-based enzyme labeling with commercial high-throughput, multiplexed protein quantification to yield the metalloproteinase activity multiplexed bead-based immunoassay (MAMBI). Assays of recombinant active MMP-1, -2, -3, -7, -8, -9, -12, and -13 establish the sensitivity and selectivity of MAMBI detection. Levels of active native MMPs are similarly characterized in conditioned cell culture medium, menstrual effluent, and uterine tissue. In a single MAMBI (5 μL), we achieve sensitivities equal to those from leading single-plex MMP activity detection strategies (e.g., 10-15 M for MMP-1). We also demonstrate high-throughput inhibitor screening via the MAMBI approach in complex, patient-derived samples.

29 Jan 2019·The Journal of Infectious DiseasesQ2 · MEDICINE

Matrix Metalloproteinase Inhibition in a Murine Model of Cavitary Tuberculosis Paradoxically Worsens Pathology

Q2 · MEDICINE

Article

Author: Ordonez, Alvaro A ; Pokkali, Supriya ; Bishai, William R ; Kübler, André ; Elkington, Paul T ; Urbanowski, Michael E ; Sanchez-Bautista, Julian ; Klunk, Mariah H ; Jain, Sanjay K

AbstractMatrix metalloproteinases (MMPs) degrade extracellular matrix and are implicated in tuberculosis pathogenesis and cavitation. In particular, MMP-7 is induced by hypoxia and highly expressed around pulmonary cavities of Mycobacterium tuberculosis–infected C3HeB/FeJ mice. In this study, we evaluated whether administration of cipemastat, an orally available potent inhibitor of MMP-7, could reduce pulmonary cavitation in M. tuberculosis–infected C3HeB/FeJ mice. We demonstrate that, compared with untreated controls, cipemastat treatment paradoxically increases the frequency of cavitation (32% vs 7%; P = .029), immunopathology, and mortality. Further studies are needed to understand the role of MMP inhibitors as adjunctive treatments for pulmonary tuberculosis.

100 Deals associated with Cipemastat

External Link

KEGG	Wiki	ATC	Drug Bank
D03517	Cipemastat	-	-

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