MMP8


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Related to MMP8: collagenase, MMP9, MMP2, TIMP-1, PubMed, MMP-1

MMP8

A gene on chromosome 11q22.3 that encodes matrix metalloproteinase 8, which degrades fibrillar type I, II and III collagens. It is involved in breaking down extracellular the matrix in physiological processes—e.g., embryonic development, reproduction, tissue remodelling and wound healing. It differs from most MMP family members in that it is stored in secondary granules within neutrophils and activated by autolytic cleavage.

Molecular pathology
Defects in MMP8 have been linked to arthritis and metastasis.
References in periodicals archive ?
Haptoglobin-MMP1 stimulates hyperkeratosis and acanthosis, promoting skin carcinogenesis, a process enhanced by MMP8 absence in defective inflammatory responses, and inhibited MMP9 absence (a mechanism involved in prolonged contact dermatitis) [23, 109, 110].
They found that around 25 per cent of these patients had a slightly different version of the gene for MMP8 and their arteries were more clogged than other patients.
These reports have shown a series of markedly overexpressed proteins in these pathological conditions, especially cytokines (i.e., IL-1b and RANK/RANKL/OPG) and MMPs (MMP8) [89].
Interestingly, in the six clusters, we also observed that various genes involved in angiogenesis and/or in vascular damage were targeted by selected miRNAs including THBS1, MMP8, VEGFA (CL1), FOSL2, THBD (CL2), HIPK1 and DDX6 (CL3), PGK1 (CL4), and ACTR2 (CL6).
Secretome components References CD26 [16] FGF1 [16] FLT-3 [62] G-CSF [62] GM-CSF [17] HGF [16] IGF-1 [17] IL-1ra [16] IL-6 [17] IL-16 [16] MMP8 [16] MMP9 [16] OPN [16] PF4 [16] SCF [62] SDF1 [16] VEGF [17]
Fernandez-Somoano et al., "Polymorphism +17 C/G in matrix metalloprotease MMP8 decreases lung cancer risk," BMC Cancer, vol.
Adeyemi, "Immunohistochemical expression of MMP-2 and MMP8 in oral squamous cell carcinoma," Journal of Clinical and Experimental Dentistry, vol.
Likewise, IL-10 also appears to have an important role in modulating the healing process, since in vitro studies have demonstrated its role in the induction of collagen synthesis and action of enzymes that degrade collagen, such as MMP1 and MMP8 [30].
Further, the proatherosclerotic effect of MMP8 deficiency indicated by higher neointima formation was shown to be dependent on an ADAM10-, N-cadherin, and [beta]-catenin-mediated pathway [131].
Lead MMP1 MMP2 MMP8 MMP9 MMP12 MMP14 Number 17 [136] NT NT >100 NT NT >100 Number 19 [136] NT >100 >100 >100 NT >100 KP-457 [135] >100 0.72 2.2 5.4 NT 2.14 INCB3619 [18] >0.5 0.045 NT 0.3 NT 0.8 Complex I [139] NT NT NT NT NT NT MEDI3622 [147] NT NT NT NT >10 NT D1(A12) [140] NT NT NT NT NT NT D8 [143] NT NT NT NT NT NT 4mut [19, 152] NT NT NT >1.0 NT >1.0 Lead ADAM33 ADAM9 ADAM10 ADAM17 Number 17 [136] NT NT >100 4.2 Number 19 [136] NT NT >100 4.3 KP-457 [135] NT NT 0.75 0.011 INCB3619 [18] 1.03 >5 0.022 0.014 Complex I [139] NT NT NT 11 MEDI3622 [147] NT NT >10 0.0031 D1(A12) [140] NT NT >1 0.0045 D8 [143] NT NT NT 0.0012 4mut [19, 152] NT NT NT 0.1 NT: not tested.
Korkiamaki et al., "Collagenase-2 (MMP8) and matrilysin-2 (MMP-26) expression in human wounds of different etiologies," Wound Repair and Regeneration, vol.