单分子力谱揭示硫酸乙酰肝素链与玻连蛋白结合过程中的结构差异
Single-molecule force spectroscopy reveals structural differences of heparan sulfate chains during binding to vitronectin
摘要：
多配体蛋白聚糖代表了一个正在进行的研究领域，重点是它们在正常和病理条件下的调节作用。Syndecan在癌症进展中的作用得到了充分的证明，暗示了它们在诊断中的重要性，甚至提出了各种癌症潜在的治疗方法。因此，在单分子水平上的非结合特性的表征将吸引它们作为治疗靶点的用途。在我们的研究中，在与玻连蛋白HEP II结合位点的相互作用期间测量多配体蛋白聚糖-1和多配体蛋白聚糖-4。我们的研究结果表明，多配体蛋白聚糖是钙离子依赖性分子，揭示不同的，非约束性的性质，表明硫酸肝素链结构的改变，可能在链序列或硫酸化模式。通过这种方式，我们假设HS链对ECM蛋白的亲和力可能通过改变多配体蛋白聚糖与肿瘤微环境中存在的癌症相关受体相互作用的能力来控制癌症侵袭，从而促进调节肿瘤细胞行为的各种信号级联的激活。
英文摘要：
The syndecans represent an ongoing research field focused on their regulatory roles in normal and pathological conditions. Syndecan's role in cancer progression becomes well-documented, implicating their importance in diagnosis and even proposing various cancer potential treatments. Thus, the characterization of the unbinding properties at the single molecules level will appeal to their use as targets for therapeutics. In our study, syndecan-1 and syndecan-4 were measured during the interaction with the vitronectin HEP II binding site. Our findings show that syndecans are calcium ion-dependent molecules that reveal distinct, unbinding properties indicating the alterations in heparin sulfate chain structure, possibly in the chain sequence or sulfation pattern. In that way, we suppose that HS chain affinity to ECM proteins may govern cancer invasion by altering syndecan ability to interact with cancer-related receptors present in the tumor microenvironment, thereby promoting the activation of various signaling cascades regulating tumor cell behavior.
机构、总结、中文摘要均由AI分析而来，可能存在错误，请以论文正文为准。
