Department of Molecular Medicine, Sapienza University of Rome, Rome, Italy.
Department of Biology and Biotechnology, Sapienza University of Rome, Rome, Italy.
PLoS One. 2020 Jan 30;15(1):e0227279. doi: 10.1371/journal.pone.0227279. eCollection 2020.
Fibrous dysplasia (FD) of bone is a complex disease of the skeleton caused by dominant activating mutations of the GNAS locus encoding for the α subunit of the G protein-coupled receptor complex (Gsα). The mutation involves a substitution of arginine at position 201 by histidine or cysteine (GsαR201H or R201C), which leads to overproduction of cAMP. Several signaling pathways are implicated downstream of excess cAMP in the manifestation of disease. However, the pathogenesis of FD remains largely unknown. The overall FD phenotype can be attributed to alterations of skeletal stem/progenitor cells which normally develop into osteogenic or adipogenic cells (in cis), and are also known to provide support to angiogenesis, hematopoiesis, and osteoclastogenesis (in trans). In order to dissect the molecular pathways rooted in skeletal stem/progenitor cells by FD mutations, we engineered human skeletal stem/progenitor cells with the GsαR201C mutation and performed transcriptomic analysis. Our data suggest that this FD mutation profoundly alters the properties of skeletal stem/progenitor cells by pushing them towards formation of disorganized bone with a concomitant alteration of adipogenic differentiation. In addition, the mutation creates an altered in trans environment that induces neovascularization, cytokine/chemokine changes and osteoclastogenesis. In silico comparison of our data with the signature of FD craniofacial samples highlighted common traits, such as the upregulation of ADAM (A Disintegrin and Metalloprotease) proteins and other matrix-related factors, and of PDE7B (Phosphodiesterase 7B), which can be considered as a buffering process, activated to compensate for excess cAMP. We also observed high levels of CEBPs (CCAAT-Enhancer Binding Proteins) in both data sets, factors related to browning of white fat. This is the first analysis of the reaction of human skeletal stem/progenitor cells to the introduction of the FD mutation and we believe it provides a useful background for further studies on the molecular basis of the disease and for the identification of novel potential therapeutic targets.
骨纤维结构不良(FD)是一种复杂的骨骼疾病,由 GNAS 基因座编码的 G 蛋白偶联受体复合物(Gsα)的显性激活突变引起。该突变涉及精氨酸在 201 位被组氨酸或半胱氨酸取代(GsαR201H 或 R201C),导致 cAMP 的过度产生。在疾病表现中,下游有几个信号通路涉及过量的 cAMP。然而,FD 的发病机制在很大程度上仍然未知。总的 FD 表型可以归因于骨骼干细胞/祖细胞的改变,这些细胞通常发育成成骨细胞或脂肪细胞(顺式),并且已知也为血管生成、造血和破骨细胞生成提供支持(反式)。为了剖析 FD 突变所导致的骨骼干细胞/祖细胞中的分子途径,我们用 GsαR201C 突变工程化了人类骨骼干细胞/祖细胞,并进行了转录组分析。我们的数据表明,这种 FD 突变通过推动骨骼干细胞/祖细胞形成组织紊乱的骨骼,同时改变脂肪生成分化,从而深刻地改变了骨骼干细胞/祖细胞的特性。此外,突变创造了一个改变的反式环境,诱导新血管生成、细胞因子/趋化因子变化和破骨细胞生成。我们的数据与 FD 颅面样本的特征进行了计算机比较,突出了一些共同的特征,如 ADAM(解整合素和金属蛋白酶)蛋白和其他基质相关因子的上调,以及磷酸二酯酶 7B(PDE7B)的上调,这可以被认为是一种缓冲过程,被激活以补偿过量的 cAMP。我们还在两个数据集都观察到了 CEBPs(CCAAT 增强结合蛋白)的高水平,这些因子与白色脂肪的褐色化有关。这是首次分析人类骨骼干细胞/祖细胞对 FD 突变引入的反应,我们认为这为进一步研究疾病的分子基础和鉴定新的潜在治疗靶点提供了有用的背景。