Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene. [5][6]

Mar 30, 2025 · Complete information for MMP10 gene (Protein Coding), Matrix Metallopeptidase 10, including: function, proteins, disorders, pathways, orthologs, and expression.

MMP-10, which is overexpressed in aortic valve from patients with calcific aortic stenosis, seems to play a central role in calcification in AS through Akt phosphorylation. Our results suggest that MMP-10 facilitates H. pylori persistence and promotes gastritis.

Matrix metalloproteinases (Mmps) stimulate tumor invasion and metastasis by degrading the extracellular matrix. Here we reveal an unexpected role for Mmp10 (stromelysin 2) in the maintenance and tumorigenicity of mouse lung cancer stem-like cells ...

Aug 1, 2016 · Stromelysin-2 (MMP10) is expressed by macrophages in numerous tissues after injury; however, little is known of its function. In this study, we report that MMP10 is expressed by macrophages in human lungs from patients with cystic fibrosis and induced in mouse macrophages in response to Pseudomonas aeruginosa infection both in vivo and by ...

MMP10 contributes to HCC development, participating in tumor angiogenesis, growth, and dissemination. We identified a new reciprocal crosstalk between MMP10 and the CXCR4/SDF1 axis contributing to HCC progression and metastasis.

Jan 12, 2021 · Matrix metalloproteinase-10 (MMP-10) is a zinc-dependent endopeptidase involved in regulating a wide range of biologic processes, such as apoptosis, cell proliferation, and tissue remodeling....

In this study, we identified matrix metalloproteinase-10 (MMP10) is expressed in CSCs/CICs of EOC. An immunohistochemical study revealed that a high expression level of MMP10 is a marker for poor prognosis and platinum resistance in multivariate analysis.

Mar 5, 2024 · Gene target information for MMP10 - matrix metallopeptidase 10 (human). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.

We report the generation of a highly selective and tightly binding MMP10 inhibitor (Ki < 2 n m). Using bio-layer interferometry–based binding assays, we found that this antibody interacts with the MMP10 active site. Activity assays demonstrated that the antibody selectively inhibits MMP10 over its closest relative, MMP3.