Guo Keyu, You Baoqing, Zhou Wenwen, Li Yan, Wang Zhen, Zhang Jing, Si Shuyi
Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Bio Protoc. 2025 Jul 20;15(14):e5400. doi: 10.21769/BioProtoc.5400.
Cathepsin L (CTSL), a lysosomal cysteine protease belonging to the papain-like protease family, is primarily involved in intracellular protein degradation, antigen processing, and extracellular matrix remodeling. It plays critical roles in pathological conditions, including cancer metastasis, neurodegenerative disorders, and viral infection, due to dysregulated activity or overexpression. Thus, inhibitors targeting CTSL are under investigation for therapeutic applications. Current approaches for identifying CTSL inhibitors predominantly rely on fluorescence-labeled substrates, fluorescence resonance energy transfer (FRET), and cell-based screening assays. Here, we applied the principle of fluorescence polarization (FP) to the detection of substrate cleavage activity by CTSL through changes in millipolarization unit (mp) values and established a cost-effective, quantitative, reagent- and time-saving inhibitor high-throughput screening (HTS) assay. We also provide detailed steps for the expression and purification of highly active CTSL from eukaryotic cells, which lays a solid foundation for the FP-based assay. A key advantage of this assay lies in its reduced susceptibility to fluorescence interference, as the fluorescein isothiocyanate (FITC) fluorophore exhibits high quantum efficiency with an emission peak at 535 nm-a wavelength range distinct from most naturally occurring fluorescent molecules. The assay's adaptability to reaction time, temperature, and dimethyl sulfoxide (DMSO) concentration minimizes false-positive or false-negative results caused by minor experimental inconsistencies, streamlining the screening process. Furthermore, the protocol requires fewer operational steps, reduced incubation time, and lower quantities of CTSL and substrates compared to conventional methods. This rapid, cost-effective, and scalable approach aligns well with the demands of HTS platforms. Key features • Detailed procedures for eukaryotic expression, purification, and identification of active recombinant CTSL and determination of its biological activity. • Full description for application of fluorescence polarization (FP)-based high-throughput screening (HTS) assay targeting CTSL. • Elaboration for the application of the FP-based assay in CTSL activity evaluation or drug discovery. • Protocol is readily adaptable to other proteases with a similar catalytic mechanism.
组织蛋白酶L(CTSL)是一种属于木瓜蛋白酶样蛋白酶家族的溶酶体半胱氨酸蛋白酶,主要参与细胞内蛋白质降解、抗原加工和细胞外基质重塑。由于其活性失调或过度表达,它在包括癌症转移、神经退行性疾病和病毒感染在内的病理状况中发挥着关键作用。因此,针对CTSL的抑制剂正在进行治疗应用研究。目前鉴定CTSL抑制剂的方法主要依赖于荧光标记底物、荧光共振能量转移(FRET)和基于细胞的筛选测定。在此,我们将荧光偏振(FP)原理应用于通过毫偏振单位(mp)值的变化检测CTSL的底物切割活性,并建立了一种经济高效、定量、节省试剂和时间的抑制剂高通量筛选(HTS)测定方法。我们还提供了从真核细胞中表达和纯化高活性CTSL的详细步骤,这为基于FP的测定奠定了坚实基础。该测定的一个关键优势在于其对荧光干扰的敏感性降低,因为异硫氰酸荧光素(FITC)荧光团具有高量子效率,发射峰在535nm——这是一个与大多数天然存在的荧光分子不同的波长范围。该测定对反应时间、温度和二甲基亚砜(DMSO)浓度的适应性最大限度地减少了由微小实验不一致导致的假阳性或假阴性结果,简化了筛选过程。此外,与传统方法相比,该方案所需的操作步骤更少、孵育时间更短,并且CTSL和底物的用量更低。这种快速、经济高效且可扩展的方法与HTS平台的要求非常契合。关键特性 • 真核表达、纯化和鉴定活性重组CTSL及其生物学活性测定的详细程序。 • 基于荧光偏振(FP)的针对CTSL的高通量筛选(HTS)测定方法的完整描述。 • 基于FP的测定方法在CTSL活性评估或药物发现中的应用阐述。 • 该方案易于适用于具有类似催化机制的其他蛋白酶。