Versican is a large chondroitin sulfate/dermatan sulfate proteoglycan belonging to the aggrecan/lectican family. In adults, this proteoglycan serves as a structural macromolecule of the extracellular matrix in the brain and large blood vessels. In contrast, versican is transiently expressed at high levels during development and under pathological conditions when the extracellular matrix dramatically changes, including in the inflammation and repair process. There are many reports showing the upregulation of versican in cancer, which correlates with cancer aggressiveness. Versican has four classical splice variants, and all the variants contain G1 and G3 domains at N- and C-termini, respectively. There are two glycosaminoglycan attachment domains CSα and CSβ. The largest V0 variant contains both CSα and CSβ, V1 contains CSβ, V2 contains CSα, and the shortest G3 variant has neither of them. Versican degradation is initiated by cleavage at a site in the CSβ domain by ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases. The N-terminal fragment containing the G1 domain has been reported to exert various biological functions, although its mechanisms of action have not yet been elucidated. In this review, we describe the role of versican in inflammation and cancer and also address the biological function of versikine.

Versican 是一种大的硫酸软骨素/硫酸皮肤素蛋白聚糖，属于蛋白聚糖/蛋白聚糖家族。在成人中，这种蛋白聚糖是大脑和大血管中细胞外基质的结构大分子。相比之下，当细胞外基质发生显着变化（包括在炎症和修复过程中）时，在发育过程中和病理条件下，多糖蛋白会以高水平瞬时表达。有许多报告显示癌症中 versican 的上调，这与癌症的侵袭性有关。Versican 有四种经典剪接变体，所有变体分别在 N 端和 C 端包含 G1 和 G3 结构域。有两个糖胺聚糖附着结构域 CSα 和 CSβ。最大的 V0 变体包含 CSα 和 CSβ，V1 包含 CSβ，V2 包含 CSα，最短的 G3 变体两者都没有。Versican 降解是通过 ADAMTS（一种具有血小板反应蛋白基序的去整合素和金属蛋白酶）蛋白酶在 CSβ 结构域中的一个位点切割而引发的。据报道，含有 G1 结构域的 N 端片段具有多种生物学功能，但其作用机制尚未阐明。在这篇综述中，我们描述了 versicine 在炎症和癌症中的作用，并讨论了 versikine 的生物学功能。虽然其作用机制尚未阐明。在这篇综述中，我们描述了 versicine 在炎症和癌症中的作用，并讨论了 versikine 的生物学功能。虽然其作用机制尚未阐明。在这篇综述中，我们描述了 versicine 在炎症和癌症中的作用，并讨论了 versikine 的生物学功能。