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Literature summary for 3.4.24.7 extracted from

  • Rand, L.; Green, J.A.; Saraiva, L.; Friedland, J.S.; Elkington, P.T.
    Matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade (2009), J. Immunol., 182, 5865-5872.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
TIMP-1 specific MMP-1 inhibitor. Inhibition of p38 signaling by SB203580 increases TIMP-1 secretion, as well as infection with Mycobacterium tuberculosis, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular MMP-1 is secreted Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
macrophage primary, monocyte-derived Homo sapiens
-

Synonyms

Synonyms Comment Organism
matrix metalloproteinase-1
-
 Homo sapiens
MMP-1
-
 Homo sapiens

Expression

Organism Comment Expression
Homo sapiens SB203580 and PD98059 suppress MMP-1 secretion down
Homo sapiens MMP-1 expression and secretion is induced by infection with Mycobacterium tuberculosis by 57.8%, the specific inhibitor TIMP-1 expression is also induced by 243.7%. The MMP-1 induction is specifically inhibited by 4-aminosalicyclic acid via inhibiting a p38 MAPK-prostaglandin signaling cascade, overview up

General Information

General Information Comment Organism
metabolism matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1, overview Homo sapiens
physiological function matrix metalloproteinase-1 degrades the extracellular matrix and is implicated in tuberculosis-driven tissue destruction, signaling pathways regulating macrophage MMP-1 in human pulmonary tuberculosis, overview Homo sapiens