拉力力促进骨质分化通过ephrinB2-EphB4信号通路在正牙运动中的牙分化
Hang Yu1,2,3, Xiaoxi Wei1,2,3, Huan Jiang1,2,3
1Department of Orthodontics, Stomatology School of Jilin University, No. 1500 Qinghua Road, ChaoYang Area, Changchun City, Jilin Province, P.R. China.
BMC oral health
|January 23, 2025
概括
张力 (TF) 通过以B2-EphB4信号通路促进骨质细胞分化. 在这个过程中,ERK1/2通道部分参与其中,这对于正统牙牙移动期间的骨形成至关重要.
科学领域:
- 生物医学工程 生物医学工程
- 细胞生物学 细胞生物学
- 矯正牙科 矯正牙科是一種矯正牙科.
背景情况:
- 骨质分化对骨健康和再生至关重要.
- 已知张力 (TF) 影响细胞行为,包括骨质母细胞功能.
- 通过TF促进骨质生分化的特定分子机制需要进一步阐明.
研究的目的:
- 调查以弗林B2-EphB4信号通路是否介导TF诱导的骨质母细胞的骨质生分化.
- 探索TF在正统牙运动 (OTM) 期间骨形成中的作用.
- 为了确定参与TF诱导的骨质生成差异化的下游信号通路.
主要方法:
- MC3T3-E1细胞接受了TF,并评估了细胞增殖.
- 使用ALP和ARS染色,qPCR和西部斑点分析了骨质分化标志物.
- 使用NVP-BHG712阻止了EphB4受体.
- 建立了一种大鼠OTM模型,治疗包括以B2-Fc和NVP-BHG712.
- 使用微型CT和H&E染色评估了膜骨变化.
- 分析了MAPK通路,以确定它们的参与.
主要成果:
- TF显著促进了MC3T3-E1细胞的骨质分化,这种效应通过阻断EphB4受体而被抑制.
- 在体内,TF增强了膜骨的形成,通过以弗林B2-EphB4信号通路进行介导.
- TF增加了MAPK通路激活,在EphB4受体阻塞时,p-ERK1/2促进显著下降.
结论:
- 通过ephrinB2-EphB4信号通路,TF促进骨质分化.
- 该ERK1/2通路作用于以弗林B2-EphB4信号的下游,部分调解TF诱导的骨质分化.
- 这个信号轴是增强OTM期间骨形成的潜在目标.
相关概念视频
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal
2.2K
Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
2.2K
Tension Response at Adherens Junctions
2.6K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
2.6K
Cell-matrix's Response to Mechanical Forces
2.5K
In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue.
Anchoring junctions mechanically attach a cell to the...
Anchoring junctions mechanically attach a cell to the...
2.5K
TGF - β Signaling Pathway
7.2K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.2K
Bone Remodeling
38.1K
Bone remodeling is a continuous and balanced process of bone resorption by osteoclasts and bone formation by osteoblasts. In adults, it helps maintain bone mass and calcium homeostasis. While mechanical stress can stimulate turnover as part of the normal maintenance and reparative process, several hormones also regulate bone remodeling.
38.1K
Regulation of Angiogenesis and Blood Supply
2.5K
Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits. Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl...
2.5K


