Department of Pathology, College of Veterinary Medicine, The University of Georgia, Athens, GA, USA.
Department of Pathology, College of Veterinary Medicine, and Department of Basic Sciences, AU/UGA Medical Partnership, The University of Georgia, Athens, GA, USA.
Adv Exp Med Biol. 2021;1348:127-138. doi: 10.1007/978-3-030-80614-9_5.
Proteoglycans consist of protein cores to which at least one glycosaminoglycan chain is attached. They play important roles in the physiology and biomechanical function of tendons, ligaments, cardiovascular system, and other systems through their involvement in regulation of assembly and maintenance of extracellular matrix, and through their participation in cell proliferation together with growth factors. They can be divided into two main groups, small and large proteoglycans. The small proteoglycans are also known as small leucine-rich proteoglycans (SLRPs) which are encoded by 18 genes and are further subclassified into Classes I-V. Several members of Class I and II, such as decorin and biglycan from Class I, and Class II fibromodulin and lumican, are known to regulate collagen fibrillogenesis. Decorin limits the diameter of collagen fibrils during fibrillogenesis. The function of biglycan in fibrillogenesis is similar to that of decorin. Though biomechanical function of tendon is compromised in decorin-deficient mice, decorin can substitute for lack of biglycan in biglycan-deficient mice. New data also indicate an important role for biglycan in disorders of the cardiovascular system, including aortic valve stenosis and aortic dissection. Two members of the Class II of SLRPs, fibromodulin and lumican bind to the same site within the collagen molecule and can substitute for each other in fibromodulin- or lumican-deficient mice.Aggrecan and versican are the major representatives of the large proteoglycans. Though they are mainly found in the cartilage where they provide resilience and toughness, they are present also in tensile portions of tendons and, in slightly different biochemical form in fibrocartilage. Degradation by aggrecanase is responsible for the appearance of different forms of aggrecan and versican in different parts of the tendon where these cleaved forms play different roles. In addition, they are important components of the ventricularis of cardiac valves. Mutations in the gene for versican or in the gene for elastin (which binds to versican ) lead to severe disruptions of normal developmental of the heart at least in mice.
蛋白聚糖由至少一个糖胺聚糖链连接到其蛋白质核心组成。它们通过参与调节细胞外基质的组装和维持,以及通过与生长因子一起参与细胞增殖,在肌腱、韧带、心血管系统和其他系统的生理学和生物力学功能中发挥重要作用。它们可以分为两大类,即小蛋白聚糖和大蛋白聚糖。小蛋白聚糖也称为小富含亮氨酸的蛋白聚糖 (SLRPs),由 18 个基因编码,并进一步细分为 I-V 类。I 类和 II 类的几个成员,如 I 类的 decorin 和 biglycan,以及 II 类的 fibromodulin 和 lumican,已知可调节胶原原纤维的形成。decorin 在原纤维形成过程中限制胶原纤维的直径。biglycan 在原纤维形成中的功能类似于 decorin。尽管在 decorin 缺陷型小鼠中肌腱的生物力学功能受损,但 decorin 可以替代 biglycan 缺陷型小鼠中 biglycan 的缺乏。新数据还表明 biglycan 在心血管系统疾病中起着重要作用,包括主动脉瓣狭窄和主动脉夹层。SLRPs II 类的两个成员,fibromodulin 和 lumican,结合到胶原分子的相同位点,并且可以在 fibromodulin 或 lumican 缺陷型小鼠中相互替代。aggrecan 和 versican 是大蛋白聚糖的主要代表。尽管它们主要存在于软骨中,为其提供弹性和韧性,但它们也存在于肌腱的拉伸部分,并以略有不同的生化形式存在于纤维软骨中。aggrecanase 的降解导致不同形式的 aggrecan 和 versican 在肌腱不同部位的出现,这些裂解形式在不同部位发挥不同的作用。此外,它们是心脏瓣膜心室的重要组成部分。versican 或弹性蛋白(与 versican 结合)基因的突变至少在小鼠中导致心脏正常发育的严重破坏。