MMP8

Case Study 1: K Juurikka, 2021

Researchers mapped the substrates of MMP8 to elucidate its previously shown tumour-protective role in oral tongue squamous cell carcinoma (OTSCC). MMP8 overexpressing (+) HSC-3 cells, previously demonstrated to have reduced migration and invasion, showed enhanced cell-cell adhesion. By analysing the secretomes of MMP8 + and control cells with terminal amine isotopic labelling of substrates (TAILS) coupled with liquid chromatography and tandem mass spectrometry (LC-MS/MS), researchers identified 36 potential substrates of MMP8, including FXYD domain-containing ion transport regulator 5 (FXYD5). Cleavage of FXYD5 by MMP8 was confirmed using recombinant proteins. Furthermore, they detected a loss of FXYD5 levels on cell membrane of MMP8 + cells, which was rescued by inhibition of the proteolytic activity of MMP8. Silencing (si) FXYD5 increased the cell-cell adhesion of control but not that of MMP8 + cells. FXYD5 is a novel substrate of MMP8 and reducing FXYD5 levels either with siRNA or cleavage by MMP8 increases cell adhesion leading to reduced motility.

Fig1. The spheroid area of control and MMP8 + cells embedded in Myogel–Fibrin matrix at day 0.

Fig2. Cleavage assay of recombinant FXYD5 with and without APMA-activated recombinant MMP8 using silver staining.

Case Study 2: An Fang, 2022

In this study, the effect of the matrix metallopeptidase (MMP) family on the permeability of the BBB during RABV infection was evaluated. The expression level of MMP8 was upregulated in mice infected with lab-attenuated RABV but not with wt RABV. Lab-attenuated RABV rather than wt RABV activates inflammatory signaling pathways mediated by the nuclear factor κB (NF-κB) and mitogen-activated protein kinase (MAPK) pathways. Activated NF-κB (p65) and AP-1 (c-Fos) bind to the MMP8 promoter, resulting in upregulation of its transcription. Analysis of mouse brains infected with the recombinant RABV expressing MMP8 indicated that MMP8 enhanced BBB permeability, leading to infiltration of inflammatory cells into the central nervous system (CNS). In brain-derived endothelial cells, treatment with MMP8 recombinant protein caused the degradation of tight junction (TJ) proteins, and the application of an MMP8 inhibitor inhibited the degradation of TJ proteins after RABV infection.

Fig3. MMP8 protein levels were assessed using Western blotting.

Fig4. The occludin, claudin-5, and ZO-1 expression levels in bEnd.3 cells were determined by Western blotting after treatment with MMP8 recombinant protein.

MMP8 involved in several pathways and played different roles in them. We selected most pathways MMP8 participated on our site, such as Activation of Matrix Metalloproteinases, Collagen degradation, Degradation of the extracellular matrix, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP8 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

MMP8 has several biochemical functions, for example, calcium ion binding, metalloendopeptidase activity, serine-type endopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP8 itself. We selected most functions MMP8 had, and list some proteins which have the same functions with MMP8. You can find most of the proteins on our site.

MMP8 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MMP8 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP8.

Gene Family

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