Manna Dipankar, Pust Sascha, Torgersen Maria L, Cordara Gabriele, Künzler Markus, Krengel Ute, Sandvig Kirsten
Department of Chemistry, University of Oslo, Oslo, Norway.
Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, Oslo, Norway.
PLoS One. 2017 Jan 23;12(1):e0170716. doi: 10.1371/journal.pone.0170716. eCollection 2017.
PSL1a is a lectin from the mushroom Polyporus squamosus that binds to sialylated glycans and glycoconjugates with high specificity and selectivity. In addition to its N-terminal carbohydrate-binding domain, PSL1a possesses a Ca2+-dependent proteolytic activity in the C-terminal domain. In the present study, we demonstrate that PSL1a has cytotoxic effects on mammalian cancer cells, and we show that the cytotoxicity is dependent on the cysteine protease activity. PSL1a treatment leads to cell rounding and detachment from the substratum, concomitant with disruption of vinculin complexes in focal adhesions. We also demonstrate that PSL1a inhibits protein synthesis and induces apoptosis in HeLa cells, in a time- and concentration-dependent manner.
PSL1a是一种来自鳞多孔菌的凝集素,它能以高特异性和选择性结合唾液酸化聚糖和糖缀合物。除了其N端碳水化合物结合结构域,PSL1a在C端结构域具有Ca2+依赖性蛋白水解活性。在本研究中,我们证明PSL1a对哺乳动物癌细胞具有细胞毒性作用,并且我们表明细胞毒性取决于半胱氨酸蛋白酶活性。PSL1a处理导致细胞变圆并从基质上脱离,同时粘着斑中的纽蛋白复合物被破坏。我们还证明PSL1a以时间和浓度依赖性方式抑制HeLa细胞中的蛋白质合成并诱导细胞凋亡。