Versican(又称PG-M)是一种由VCAN/CSPG2基因编码的大型细胞外基质硫酸软骨素蛋白聚糖，广泛表达于包括脑ECM在内的人体间质基质中。Dick Heinegard和Anders Malmstrom的研究小组(1982年)首先在牛主动脉中描述了它，不久之后Koji Kimata的小组从鸡胚胎中分离出来。人类VCAN/CSPG2基因的克隆于1989年由Zimmermann和Ruoslahti完成，他们还将该蛋白命名为versican，以表彰其多功能的模块化结构。Versican属于凝集蛋白聚糖亚群，aggrecan、brevican和neurocan也属于该亚群，并共享n端(G1)球状结构域。它由类igg环和两个链接模块组成，负责与透明质酸的结合，透明质酸可能被链接蛋白进一步稳定，也可能不会。在高等脊椎动物中，已知至少有4种不同的、交替剪接的变种异构体(分别为V0、V1、V2和V3)，而在低等脊椎动物中，部分通过基因复制可能有额外的变种。这些异构体是通过区分利用中心核心蛋白区域(GAG-α和GAG-β)而产生的，并包含糖胺聚糖(硫酸软骨素)附着位点。V0亚型是包含上述GAG-attachment外显子的亲本亚型;V1亚型只有GAG-β结构域;V2亚型只有GAG-α结构域;V3亚型不含任何GAG附着结构域，因此是一种无GAG的蛋白聚糖。这意味着异位异构体核心蛋白的分子质量范围为50-550 kDa，当考虑到异位异构体核心蛋白的广泛糖基化时，不同异构体的分子量从约60 kDa到1500 – 2000 kDa不等。c端(G3)球状结构域由一个或两个EGF重复序列、一个c型凝集素模块和补体调节蛋白(CRP)样结构域组成。在ECM中，c端结构域与多种配体结合，从而形成了verican的大分子结构。verican在弹性基质ECM组装、细胞粘附、细胞迁移和细胞增殖中的作用已被广泛描述，其在胚胎发育中的重要作用已被CSPG2基因缺失纯合子小鼠胚胎的早期致死证实。与其他大型蛋白聚糖一样，维甘醇由多个基质蛋白酶和adamts加工，其基质沉积在退行性疾病和癌症中可能被强烈下调或上调。在某些肿瘤中，其表达模式被认为具有预后价值。
Application: ELISA, IHC(f), WB
Clonality: Monoclonal
Host: Mouse
Purification: Supernatant
Reactivity: Human, Bovine
Versican (also known as PG-M), encoded by the VCAN/CSPG2 gene, is a large extracellular matrix chondroitin sulfate proteoglycan ubiquitously expressed in interstitial matrices of the human body, including brain ECM. It was first described in the bovine aorta by the research groups of Dick Heinegard and Anders Malmstrom’s groups (1982) and shortly after isolated from the chick embryo by Koji Kimata’s group. Cloning of the human VCAN/CSPG2 gene was accomplished in 1989 by Zimmermann and Ruoslahti, who also named the protein as versican in recognition of its versatile modular structure. Versican belongs to the lectican proteoglycan subgroup, to which aggrecan, brevican and neurocan also belong and share the N-terminal (G1) globular domain. This consists of Ig-like loops and two link modules and is responsible for the binding to hyaluronan, which may or may not be further stabilized by link proteins. At least 4 different alternatively spliced versican isoforms are known in higher vertebrates (denoted V0, V1, V2 and V3) while lower vertebrates may have additional ones in part by duplication of the gene. These isoforms are generated through differential utilization of the central core protein regions denoted GAG-α and GAG-β and encompass glycosaminoglycan (chondroitin sulfate) attachment sites. The V0 isoform is the parental one containing both the above “GAG-attachment” exons; the V1 isoform has only the GAG-β domain; the V2 isoform has only the GAG-α domain; and the V3 isoform is void of any GAG attachment domains, and is therefore a GAG-free proteoglycan. This implies that the versican isoform core proteins have a molecular mass range of 50-550 kDa and, when taking also into consideration the extensive glycosylation of the versican core protein, the molecular weights of the different isoforms vary from about 60 kDa to 1,500-2,000 kDa. The C-terminal (G3) globular domain consists of one or two EGF repeats, a C-type lectin module and complement regulatory protein (CRP)-like domain. The C-terminal domain binds a variety of ligands in the ECM and thereby contributes to the macromolecular organization of versican. The role of versican in ECM assembly of elastic matrices, cell adhesion, cell migration, and cell proliferation has been extensively described and its essential role during embryonic development is confirmed by early lethality of murine embryos homozygous for CSPG2 gene deletion. Like other large proteoglycans, versican is processed by multiple MMPs and ADAMTSs and its matrix deposition may be strongly down- or up-regulated in degenerative diseases and cancer. In some tumors its expression pattern has been proposed to have a prognostic value.