MMP14 Antibody
- Known as:
- MMP14 Antibody
- Catalog number:
- XW-7751
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- MMP14 Antibody
Related genes to: MMP14 Antibody
- Gene:
- MMP14 NIH gene
- Name:
- matrix metallopeptidase 14
- Previous symbol:
- -
- Synonyms:
- MT1-MMP
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-20
- Date modifiied:
- 2016-10-05
Related products to: MMP14 Antibody
Related articles to: MMP14 Antibody
- This study aimed to characterize large and small RNA transcriptomic changes in fibroid xenografts from mice treated with the TDO2 inhibitor 680C91 for two months and to validate selected findings using qRT-PCR, protein analyses, and in vitro fibroid explant models. Large RNA next-generation sequencing revealed that 680C91 induced broad transcriptomic alterations, with enrichment of pathways related to the extracellular space, RNA processing, PI3K/AKT signaling, and calcium signaling. Small RNA sequencing identified enrichment of pathways associated with PI3K/AKT signaling, proteoglycans in cancer, and interleukin signaling. Key differentially expressed genes were validated in xenografts and fibroid explants. Treatment with 680C91 significantly reduced the mRNA expression of VDR, MMP11, MMP14, COL11A1, CBX4, LINC02568, LINC01310, LINC02544, and LINC02182, while increasing miR-584-5p expression. These changes were consistently observed in fibroid explants treated with 680C91 for 48 hours. Corresponding decreases in protein levels of COL11A1, VDR, CBX4, MMP11, and MMP14 were also detected. Additionally, 680C91 inhibited AKT phosphorylation and reduced α-smooth muscle actin and vimentin expression. Importantly, all validated transcripts displayed expression patterns opposite to those observed in fibroid tissues compared with matched myometrium, with more pronounced effects in MED12-mutated tumors. These preclinical findings support TDO2 inhibition as a potential therapeutic strategy for uterine fibroids. - Source: PubMed
Publication date: 2026/05/11
Chuang Tsai-DerWiseman AbigailAlfaro GabrielaPejouhesh Jahromi SaynaPejouhesh Jahromi SepidehBaghdasarian DanielKhorram Omid - Diabetic kidney disease (DKD) is a leading microvascular complication of diabetes in which vascular smooth muscle cell (VSMC) senescence plays a pivotal pathogenic role. This study aimed to identify key genes regulating VSMC senescence in DKD through integrated bioinformatics and machine learning analysis, construct a diagnostic nomogram prediction model, screen candidate therapeutic compounds, and validate findings experimentally. - Source: PubMed
Publication date: 2026/05/01
Qu BoHe YuhuaWang BoWang ShanshanZhou LiMao Bing - Platelet-rich fibrin (PRF) is extensively utilized to enhance localized tissue healing, a process that critically depends on the transient polarization of macrophages toward a pro-inflammatory phenotype. Given that PRF, like other blood clot derivatives, may intrinsically modulate macrophage behavior, we conducted a comprehensive screening assay to characterize the global macrophage response to PRF exposure. To this end, we employed two widely used monocytic cell lines-U937 (histiocytic lymphoma) and THP-1 (acute monocytic leukemia)-as models to investigate macrophage responses. Cells were exposed to lysates derived from PRF, and transcriptomic alterations were profiled using bulk RNA sequencing. Differential gene expression analysis was performed, with significance determined by an adjusted p-value threshold of <0.05. In U937-derived macrophages, gene expression profiling revealed a transcriptional signature consistent with inflammatory activation. Clustering of upregulated genes highlighted pathways associated with chemokine activity (e.g., CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL20, CCL23, CCL26, CXCL5, CXCL6, CXCL8, CXCL16, and PPBP), RAGE receptor binding (FPR1, S100A8, S100A9, and S100A12), IgG binding (FCGR1A, FCGR2A, FCGR2B, and FCGR3A), prostaglandin biosynthesis (CBR1, CD74, EDN1, FABP5, IL1B, MIF, PTGES, and PTGS1), and collagen catabolism (CTSL, FAP, MMP3, MMP7, MMP9, MMP12, MMP14, MMP19, and MRC2). In contrast, PRF exposure in THP-1 cells primarily enriched genes involved in steroid biosynthesis, suggesting a more limited or distinct response. These findings underscore U937 cells as a more responsive and appropriate bioassay for modeling inflammatory macrophage polarization in response to PRF. Moreover, the identified gene signatures recapitulate key aspects of early wound healing, providing a relevant platform for studying macrophage reactivation in chronic wound environments. - Source: PubMed
Publication date: 2026/04/22
Panahipour LaylaHuang XiaoyuZampino FrancescaMiron Richard JGruber Reinhard - Metastasis is the primary driver of cancer mortality, yet the anti-metastatic mechanisms of the natural compound Ginsenoside Rh2 (G-Rh2) remain incompletely defined. Here, we integrate computational and experimental approaches to elucidate how G-Rh2 suppresses tumor cell invasion and migration. Molecular docking and dynamics simulations, using an AlphaFold2-predicted model of FAK, predicted that G-Rh2 binds potentially to the kinase domain at the critical Tyr-577 phosphorylation site, thereby sterically hindering FAK activation. Experimentally, non-cytotoxic doses of G-Rh2 inhibited HeLa cell migration and Matrigel invasion. Mechanistically, G-Rh2 disrupted focal adhesion dynamics by downregulating vinculin and impairing actin cytoskeleton remodeling. Concurrently, it suppressed invadopodia formation, cortactin localization, and MMP14 expression, reducing extracellular matrix degradation. Crucially, cellular and biochemical assays-including Western blotting with site-specific phospho-antibodies-validated the computational prediction, showing that G-Rh2 selectively inhibits FAK phosphorylation at Tyr-577 (but not Tyr-397) without affecting total FAK levels. These findings were corroborated in a mouse xenograft model, where G-Rh2 treatment reduced tumor invasiveness and decreased levels of both phospho-FAK (Tyr-577) and vinculin in vivo. This work reveals a dual mechanism, positioning G-Rh2 as a promising FAK-targeted therapeutic agent to prevent tumor invasion and migration. - Source: PubMed
Publication date: 2026/05/04
Zhang XinXiao YunjieWang ShenHan YifanWang ShijiangFan JiehouCheng LiliZhao Xinbin - Increased matrix metalloproteinase (MMP) expression has long been recognized as a common feature of colorectal cancers (CRCs), yet less is known about how these enzymes interact to impact cancer progression. Taking advantage of single-cell and spatial transcriptomic data, we analyzed the cell-type-specific and spatial expression of MMPs in CRCs. Distinct colon cancer-associated fibroblast (CAF) subtypes were found to express different MMP combinations, including MMP1/3-expressing and MMP11-expressing CAFs. Conversely, myeloid cells (monocytes, macrophages, and dendritic cells) expressed varying levels of the "myeloid MMPs" 9, 12, and 14, which correlated closely with secretory gene expression. Finally, a small population of cancer cells expressed high levels of MMP7. The MMP7-expressing cancer cells frequently co-expressed MMP1, MMP14, and several Wnt-related genes, consistent with a cancer cell type at high risk of malignancy and metastasis. Spatial transcriptomic data showed MMP expression in discernible clusters driven in part by cell-type localization, including fibroblast-heavy stromal regions and inflammatory cell hubs. Epithelial-rich areas showed subregions of MMP7-expressing cancer cells, including areas where cancer cell and myeloid MMP expression overlap. Tumors showed a wide variation in MMP1-expressing CAFs, a variation reflected in primary CAF cell lines. In vitro, MMP1 expression was a stable phenotype that persisted through multiple rounds of division. MMP1-expressing CAFs were frequently positioned at the stromal interface, suggesting a role in facilitating cell movement across the tumor boundary. Our analysis indicates that cell-type and positional MMP expression varies between tumors and may play a role in determining lesion progression and cancer spread. - Source: PubMed
Publication date: 2026/04/22
Danese Nicholas AKurkcu ShanBleiler MarinaNito KleaKuo AlanRosenberg Daniel WNakanishi MasakoGiardina Charles