Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research (CSIR), Indian Institute of Chemical Biology (IICB), 4, Raja S.C. Mullick Road, Jadavpur, Kolkata, 700032, West Bengal, India.
National Institute of Pharmaceutical Education and Research, IICB, CSIR, Kolkata, 700032, West Bengal, India.
Cell Death Dis. 2018 Feb 12;9(2):210. doi: 10.1038/s41419-017-0191-4.
Modulation of sialylation by sialyltransferases and sialidases plays essential role in carcinogenesis. There are few reports on sialyltransferase, however, the contribution of cytosolic sialidase (Neu2) remains unexplored in pancreatic ductal adenocarcinoma (PDAC). We observed lower expression of Neu2 in different PDAC cells, patient tissues, and a significant strong association with clinicopathological characteristics. Neu2 overexpression guided drug-resistant MIAPaCa2 and AsPC1 cells toward apoptosis as evidenced by decreased Bcl2/Bax ratio, activation of caspase-3/caspase-6/caspase-8, PARP reduction, reduced CDK2/CDK4/CDK6, and cyclin-B1/cyclin-E with unaffected caspase-9. Neu2-overexpressed cells exhibited higher expression of Fas/CD95-death receptor, FasL, FADD, and Bid cleavage confirming extrinsic pathway-mediated apoptosis. α2,6-linked sialylation of Fas helps cancer cells to survive, which is a substrate for Neu2. Therefore, their removal should enhance Fas-mediated apoptosis. Neu2-overexpressed cells indeed showed increased enzyme activity even on membrane. Interestingly, this membrane-bound Neu2 exhibited enhanced association with Fas causing its desialylation and activation as corroborated by decreased association of Fas with α2,6-sialic acid-binding lectin. Additionally, enhanced cytosolic Neu2 inhibited the expression of several growth factor-mediated signaling molecules involved in PI3K/Akt-mTOR pathway probably through desialylation which in turn also causes Fas activation. Furthermore, Neu2-overexpressed cells exhibited reduced cell migration, invasion with decreased VEGF, VEGFR, and MMP9 levels. To the best of our knowledge, this is the first report of cytosolic Neu2 on membrane, its association with Fas, enhanced desialylation, activation, and Fas-mediated apoptosis. Taken together, our study ascertains a novel concept by which the function of Fas/CD95 could be modulated indicating a critical role of upstream Neu2 as a promising target for inducing apoptosis in pancreatic cancer.
唾液酸转移酶和唾液酸酶通过调节唾液酸化在致癌作用中发挥重要作用。然而,关于唾液酸转移酶的报道很少,而细胞质唾液酸酶(Neu2)在胰腺导管腺癌(PDAC)中的作用仍未被探索。我们观察到不同 PDAC 细胞、患者组织中的 Neu2 表达较低,并且与临床病理特征有很强的关联。Neu2 过表达指导耐药的 MIAPaCa2 和 AsPC1 细胞向凋亡,表现为 Bcl2/Bax 比例降低、caspase-3/caspase-6/caspase-8 激活、PARP 减少、CDK2/CDK4/CDK6 减少和 cyclin-B1/cyclin-E 不变,而 caspase-9 不受影响。Neu2 过表达的细胞表现出 Fas/CD95 死亡受体、FasL、FADD 和 Bid 切割的更高表达,证实了外源性途径介导的凋亡。Fas 上的α2,6-连接唾液酸化有助于癌细胞存活,这是 Neu2 的底物。因此,去除它们应该增强 Fas 介导的凋亡。Neu2 过表达的细胞即使在膜上也表现出更高的酶活性。有趣的是,这种膜结合的 Neu2 与 Fas 的结合增强,导致其去唾液酸化和激活,这得到了 Fas 与α2,6-唾液酸结合凝集素结合减少的证实。此外,增强的细胞质 Neu2 抑制了参与 PI3K/Akt-mTOR 途径的几种生长因子介导的信号分子的表达,这可能是通过去唾液酸化,这反过来也导致 Fas 激活。此外,Neu2 过表达的细胞表现出降低的细胞迁移、侵袭和降低的 VEGF、VEGFR 和 MMP9 水平。据我们所知,这是关于细胞质 Neu2 在膜上的第一个报告,它与 Fas 的关联、增强的去唾液酸化、激活和 Fas 介导的凋亡。综上所述,我们的研究确定了一个新的概念,即 Fas/CD95 的功能可以通过调节来修饰,表明上游 Neu2 作为诱导胰腺癌凋亡的有前途的靶点具有重要作用。