Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Japan.
Am J Physiol Cell Physiol. 2022 May 1;322(5):C967-C976. doi: 10.1152/ajpcell.00081.2022. Epub 2022 Apr 6.
Aggrecan (Acan) and versican (Vcan) are large chondroitin sulfate proteoglycans of the extracellular matrix. They share the same structural domains at both N- and C-termini. The N-terminal G1 domain binds hyaluronan (HA), forms an HA-rich matrix, and regulates HA-mediated signaling. The C-terminal G3 domain binds other extracellular matrix molecules and forms a supramolecular structure that stores transforming growth factor β (TGFβ) and bone morphogenetic proteins (BMPs) and regulates their signaling. EGF-like motifs in the G3 domain may directly act like an EGF ligand. Both Acan and Vcan are present in cartilage, intervertebral disc, brain, heart, and aorta. Their localizations are essentially reciprocal. This review describes their structural domains, expression patterns and functions, and regulation of their expression.
聚集蛋白聚糖(Acan)和多配体蛋白聚糖(Vcan)是细胞外基质中大型的软骨素硫酸蛋白聚糖。它们在 N 端和 C 端都有相同的结构域。N 端的 G1 结构域与透明质酸(HA)结合,形成富含 HA 的基质,并调节 HA 介导的信号转导。C 端的 G3 结构域与其他细胞外基质分子结合,形成一个超分子结构,储存转化生长因子β(TGFβ)和骨形态发生蛋白(BMPs),并调节它们的信号转导。G3 结构域中的表皮生长因子样结构域可能直接像表皮生长因子配体一样发挥作用。Acan 和 Vcan 都存在于软骨、椎间盘、脑、心脏和主动脉中。它们的定位基本上是相互的。本文综述了它们的结构域、表达模式和功能,以及它们表达的调控。