MMP13

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MMP13

A gene on chromosome 11q22.3 that encodes matrix metalloproteinase 13, which cleaves collagens I in the extracellular matrix. MMP13 may play a role in turnover of articular cartilage.

Molecular pathology
Defects in MMP13 cause spondyloepimetaphyseal dysplasia Missouri type and metaphyseal anadysplasia type 1. MMP13 may play a role in the pathogenesis of osteoarthritis.
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References in periodicals archive ?
Grupo Colagenases MMP Nome enzimatico MMP-1 Colagenase intersticial MMP-8 Neutrofilo colagenase MMP-13 Colagenase-3 Gelatinases MMP-2 Gelatinase A MMP-9 Gelatinase B Estromalisinas MMP-3 Estromalisina-1 MMP-10 Estromalisina-2 MMP-11 Estromalisina-3 MMPs tipo MMP-14 MT1-MMP membrana MMP-16 MT3-MMP MMP-17 MT4-MMP MMP-24 MT5-MMP MMP-25 MT6-MMP Outras MMP-7 Matrilisina MMP-26 Matrilisina-2 MMP-12 Macrofago metaloelastase
Hyaluronic acid fights arthritis via multiple mechanisms, most notably by inhibiting the enzyme MMP-13, which is a key element in the joint destruction seen in osteoarthritis.
MMP-13 levels were similar in all five study groups.
(3), (4), (7), (9), (19), (20) MMP-13, sometimes referred to as collagenase-3, exhibits the broadest specificity of the collagenases, with the highest activity against type II collagen, the primary collagen found in cartilage, and has been expressed in pathologies associated with excessive ECM degradation.
MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP12, and MMP-13 were simultaneously measured using the Fluorokine MultiAnalyte Profiling assays (R&D Systems) on a Luminex 100 Bioanalyzer (Luminex.).
(1,2,8) Collagenase-3 (MMP-13) was demonstrated to play a major role in cartilage degeneration.
(2-4) Secreted-type MMPs can be classified into 6 subgroups according to their substrate specificity and structural differences (2): (1) collagenases, including tissue collagenase (MMP1), neutrophil collagenase (MMP8), and collagenase 3 (MMP13); (2) gelatinases, such as gelatinase A (MMP2) and gelatinase B (MMP9); (3) stromelysins, including stromelysin 1 (MMP3) and stromelysin 2 (MMP-10); (4) matrilysins, such as matrilysin 1 (MMP7) and matrilysin 2 (MMP26); (5) furin-activated MMPs, including stromelysin 3 (MMP-13) and epilysin (MMP 28); and (6) other MMPs such as metalloelastase (MMP12), MMP19, enamelysin (MMP-20), MMP21, and MMP-27.
The co-induction of NF-[kappa]B, MMP-13, and c-myc indicated in our microarray results is consistent with previous work by Tak and Firestein (2001).
This is consistent with our tests of the c-src inhibitor, PP2, which blocked Fn-f mediated upregulation of MMP-13. Our data suggest that Fn-f disrupt Fn receptor and enhance diffusion of cortical actin, the latter of which is associated with movement of c-src away from the plasma membrane where it can be inactivated.