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原纤维蛋白组装体:组织形成和纤维化的细胞外决定因素

Fibrillin assemblies: extracellular determinants of tissue formation and fibrosis.

作者信息

Olivieri Jacopo, Smaldone Silvia, Ramirez Francesco

机构信息

Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, USA.

出版信息

Fibrogenesis Tissue Repair. 2010 Dec 2;3:24. doi: 10.1186/1755-1536-3-24.

Abstract

The extracellular matrix (ECM) plays a key role in tissue formation, homeostasis and repair, mutations in ECM components have catastrophic consequences for organ function and therefore, for the fitness and survival of the organism. Collagen, fibrillin and elastin polymers represent the architectural scaffolds that impart specific mechanic properties to tissues and organs. Fibrillin assemblies (microfibrils) have the additional function of distributing, concentrating and modulating local transforming growth factor (TGF)-β and bone morphogenetic protein (BMP) signals that regulate a plethora of cellular activities, including ECM formation and remodeling. Fibrillins also contain binding sites for integrin receptors, which induce adaptive responses to changes in the extracellular microenvironment by reorganizing the cytoskeleton, controlling gene expression, and releasing and activating matrix-bound latent TGF-β complexes. Genetic evidence has indicated that fibrillin-1 and fibrillin-2 contribute differently to the organization and structural properties of non-collagenous architectural scaffolds, which in turn translate into discrete regulatory outcomes of locally released TGF-β and BMP signals. Additionally, the study of congenital dysfunctions of fibrillin-1 has yielded insights into the pathogenesis of acquired connective tissue disorders of the connective tissue, such as scleroderma. On the one hand, mutations that affect the structure or expression of fibrillin-1 perturb microfibril biogenesis, stimulate improper latent TGF-β activation, and give rise to the pleiotropic manifestations in Marfan syndrome (MFS). On the other hand, mutations located around the integrin-binding site of fibrillin-1 perturb cell matrix interactions, architectural matrix assembly and extracellular distribution of latent TGF-β complexes, and lead to the highly restricted fibrotic phenotype of Stiff Skin syndrome. Understanding the molecular similarities and differences between congenital and acquired forms of skin fibrosis may therefore provide new therapeutic tools to mitigate or even prevent disease progression in scleroderma and perhaps other fibrotic conditions.

摘要

细胞外基质(ECM)在组织形成、内环境稳定和修复中起关键作用,ECM成分的突变会对器官功能产生灾难性后果,进而影响生物体的健康和生存。胶原蛋白、原纤维蛋白和弹性蛋白聚合物构成了赋予组织和器官特定力学特性的结构支架。原纤维蛋白组装体(微原纤维)还具有分布、浓缩和调节局部转化生长因子(TGF)-β和骨形态发生蛋白(BMP)信号的额外功能,这些信号调节大量细胞活动,包括ECM的形成和重塑。原纤维蛋白还含有整合素受体的结合位点,整合素受体通过重组细胞骨架、控制基因表达以及释放和激活与基质结合的潜伏TGF-β复合物,诱导对细胞外微环境变化的适应性反应。遗传学证据表明,原纤维蛋白-1和原纤维蛋白-2对非胶原结构支架的组织和结构特性的贡献不同,这反过来又转化为局部释放的TGF-β和BMP信号的不同调节结果。此外,对原纤维蛋白-1先天性功能障碍的研究为诸如硬皮病等获得性结缔组织疾病的发病机制提供了见解。一方面,影响原纤维蛋白-1结构或表达的突变会扰乱微原纤维的生物合成,刺激潜伏TGF-β的不适当激活,并导致马凡综合征(MFS)的多效性表现。另一方面,位于原纤维蛋白-1整合素结合位点周围的突变会扰乱细胞-基质相互作用、结构基质组装以及潜伏TGF-β复合物的细胞外分布,并导致硬皮综合征的高度局限性纤维化表型。因此,了解先天性和获得性皮肤纤维化形式之间的分子异同,可能会提供新的治疗手段来减轻甚至预防硬皮病以及其他可能的纤维化疾病的疾病进展。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f17/3012016/281ad98088fb/1755-1536-3-24-1.jpg

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