matrix metalloproteinase 2

matrix metalloproteinase 2

A 62-kD tissue enzyme encoded on chromosome 16q13-q21 that degrades collagens and other matrix proteins, and which may be linked to cancer.

Cytokine inducers
Activin, CD40L, EGF, endothelin-1, FGF-b, FGF-3, G-CSF, GM-CSF, HGF, IFN-α, IFN-γ, IGF-1, IL-1α, IL-1β, IL-3, IL-6, sIL-6 Rα, IL-8, IL-18, LIF, M-CSF, MIF, oncostatin M, PDGF, SCF, TGF-α, TGF-β1, TNF-α, VEGF.
 
Substrates
3 α-chains of native Collagens I, IV, V, VII, X, XI, and XIV; gelatin, elastin, fibronectin, laminin-1, laminin-5, galectin, aggrecan, decorin, hyaluronidase-treated versican, proteoglycan link protein, osteonectin, MBP, GST-TNF/TNF peptide, IL-1β, serum amyloid A, APP695, α1-AT, prolysyl oxidase fusion protein, IGF-BP5, IGF-BP5, FGF R1, MMP-1, MMP-9, MMP-13.
References in periodicals archive ?
Excretion of matrix metalloproteinase 2 and 9 are associated with a high stage and grade of bladder carcinoma.
Prognostic significance of matrix metalloproteinase 2 and tissue inhibitor of metalloproteinase 2 expression in prostate cancer.
37-39) The final step of the invadopodia maturation process involves the secretion of proteases, such as matrix metalloproteinase 2 (MMP-2) and matrix metalloproteinase 9 (MMP-9), and presentation of membrane type 1 metalloproteinase (MT1-MMP) at the protruding invadopodia.
Increased activity of matrix metalloproteinase 2 and 9 after hepatic radiofrequency ablation.
Matrix metalloproteinase 2, matrix metalloproteinase 9, connective tissue growth factor in the equine tear fluid: possible implications in corneal wound healing [tese].
The expression of matrix metalloproteinases 1, 2, and 9 was not significantly changed, but an increased level of tissue inhibitor of matrix metalloproteinase 1 mRNA was observed without modification of tissue inhibitor of matrix metalloproteinase 2 mRNA.
Kind of sample as preanalytical determinant of matrix metalloproteinase 2 and 9 and tissue inhibitor of metalloproteinase 2 in blood.
Increased matrix metalloproteinase 2 concentration and transcript expression in advanced colorectal carcinomas.
The mRNA expression levels of matrix metalloproteinase 2 (MMP-2) and tissue inhibitor of metalloproteinase 1, 2 (TIMP1, 2) were measured using quantitative real-time reverse transcription-polymerase chain reaction.
Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ("gelatinase") by human neutrophil elastase and cathepsin G.
Zymography technique with gelatin as a substrate indicated that both the serum and the synovial fluid of all investigated patients contain matrix metalloproteinase 2 and 9 (Fig.

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