mmp14 Rabbit antibody Ab Aff - Purified
- Known as:
- mmp14 Rabbit (anti-) Antibody Aff - Purified
- Catalog number:
- GTX128198
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- ACR
- Gene target:
- mmp14 Rabbit antibody Aff - Purified
Related genes to: mmp14 Rabbit antibody Ab Aff - Purified
- 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 Rabbit antibody Ab Aff - Purified
Related articles to: mmp14 Rabbit antibody Ab Aff - Purified
- Osteosarcoma is a highly aggressive bone malignancy in which angiogenesis plays a crucial role in tumor progression. However, the molecular mechanisms underlying osteosarcoma-associated angiogenesis remain incompletely understood. In this study, we investigated the role of fibroblast growth factor-23 (FGF-23) in regulating angiogenesis in osteosarcoma. Bioinformatics analysis of the GSE218035 dataset revealed that matrix metalloproteinases (MMPs), particularly MMP-14, are significantly upregulated in osteosarcoma tissues. Functional assays demonstrated that FGF-23 induces MMP-14 expression in osteosarcoma cells and enhances endothelial tube formation, whereas silencing MMP-14 abolishes these effects. Mechanistic studies further showed that FGF-23 activates the p85/Akt/mTOR signaling pathway, leading to increased MMP-14 expression and angiogenic activity. Inhibition of pathway components by pharmacological inhibitors or siRNA significantly attenuated FGF-23-induced responses. In vivo, FGF-23 overexpression promoted tumor growth and vascularization, accompanied by elevated expression of MMP-14 and the endothelial marker CD31. Collectively, these findings demonstrate that FGF-23 promotes osteosarcoma angiogenesis through regulation of MMP-14 via the p85/Akt/mTOR signaling pathway and suggest that targeting this axis may provide a potential therapeutic strategy. - Source: PubMed
Publication date: 2026/07/19
Hou Chun-HanLin Chih-Yang - - Source: PubMed
Publication date: 2026/07/20
Liu YihengDou Feifei - Curcumin inhibits osteoclastogenesis and mitigates osteoporosis. Our data demonstrated that curcumin decreases membrane-bound RANKL (mRANKL) levels on osteoblasts. Notably, mRANKL exerts a more prominent role in osteoclastogenesis than its soluble counterpart (sRANKL). This study aimed to explore the role of RANKL membrane localization in curcumin-regulated osteoclastogenesis. We primarily investigated the effect of curcumin on mRANKL expression in osteoblasts in vitro and in vivo. Using fluorescence-activated cell sorting (FACS) for RANKL and co-culture experiments of osteoclast precursors (OCPs) with osteoblasts, we further analyzed the association between curcumin's indirect inhibition of osteoclast differentiation and mRANKL production. Finally, we explored the involvement of matrix metalloproteinase 14 (MMP14) in curcumin-mediated regulation of mRANKL levels. The results showed that curcumin significantly reduced mRANKL expression in osteoblasts. Curcumin also abrogated the upregulated RANKL levels in osteoblasts of Tg-hRANKL transgenic mice. Co-culture assays revealed that curcumin exerted the weakest inhibitory effect on osteoclast differentiation when OCPs were co-cultured with mRANKL-negative osteoblasts. Additionally, curcumin increased MMP14 expression in osteoblasts and enhanced the MMP14-RANKL interaction. Importantly, silencing MMP14 in osteoblasts reversed curcumin-inhibited mRANKL levels and osteoclast differentiation. Collectively, our findings indicated that curcumin inhibited mRANKL production in osteoblasts, which contributes to its therapeutic effect on osteoclastic osteoporosis. - Source: PubMed
Publication date: 2026/07/10
Gao TingweiKe TieXiao ZhanhaoGao Xi - Myocardial infarction (MI) is a leading cause of mortality worldwide. Identification of robust and translatable molecular markers remains challenging due to inter-dataset and inter-species variability. In this study, we performed a cross-species integrative analysis to identify conserved hub genes and potential therapeutic targets in MI. Analysis revealed five hub genes (IL6, SERPINE1, MMP14, PLAUR, and ENO1), which were consistently validated across human peripheral blood and multiple animal models. A multigene diagnostic model demonstrated strong predictive performance (AUC = 0.904). The model was developed to distinguish myocardial infarction (MI) samples from non-MI control samples in an independent peripheral blood dataset. Drug-gene interaction analysis identified candidate therapeutic compounds. These results are computational predictions from the DGIdb database and do not represent validated therapeutic effects in myocardial infarction. These findings highlight conserved molecular mechanisms of MI and provide potential biomarkers and therapeutic targets with translational relevance. - Source: PubMed
Publication date: 2026/07/06
Sheng ZhiyongLi QiangBao MingyuWang WenjingChen ZitongGuo Jiali - Cortical bone is a dense, lamellar structure containing osteoblast (OB)-lineage-derived osteocytes embedded within a mineralized matrix. How osteocytes differentiate and organize within lamellar bone remains incompletely understood. Here, we show that ATP6AP2 in the OB lineage is essential for osteocyte maturation and cortical bone development. Male mice with OB-lineage-specific deletion of Atp6ap2 (Atp6ap2) exhibit increased cortical bone mass composed largely of irregular woven bone, with impaired osteocyte maturation and survival, and abnormal osteocyte distribution. Mechanistic analyses identify matrix metalloproteinase-14 (MMP14) as a key downstream effector of ATP6AP2. ATP6AP2 interacts with MMP14 and promotes its surface localization largely in immature osteocytes, and expression of MMP14 in Atp6ap2-deficient OB-lineage cells diminishes cortical bone defects. These results reveal previously unrecognized roles for ATP6AP2 in regulating cortical osteocyte development and establish an ATP6AP2-MMP14 signaling axis that controls the woven-to-lamellar bone transition and osteocyte differentiation and distribution. - Source: PubMed
Publication date: 2026/07/11
Xiong LeiGuo Hao-HanPan Jin-XiuRen XiaoLee DaehoonMei LinXiong Wen-Cheng