Turgeon V L, Lloyd E D, Wang S, Festoff B W, Houenou L J
Department of Neurobiology and Anatomy, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA.
J Neurosci. 1998 Sep 1;18(17):6882-91. doi: 10.1523/JNEUROSCI.18-17-06882.1998.
Increasing evidence indicates several roles for thrombin-like serine proteases and their cognate inhibitors (serpins) in normal development and/or pathology of the nervous system. In addition to its prominent role in thrombosis and/or hemostasis, thrombin inhibits neurite outgrowth in neuroblastoma and primary neuronal cells in vitro, prevents stellation of glial cells, and induces cell death in glial and neuronal cell cultures. Thrombin is known to act via a cell surface protease-activated receptor (PAR-1), and recent evidence suggests that rodent neurons express PAR-1. Previously, we have shown that the thrombin inhibitor, protease nexin-1, significantly prevents neuronal cell death both in vitro and in vivo. Here we have examined the effects of human alpha-thrombin and the presence and/or activation of PAR-1 on the survival and differentiation of highly enriched cultures of embryonic chick spinal motoneurons. We show that thrombin significantly decreased the mean neurite length, prevented neurite branching, and induced motoneuron death by an apoptosis-like mechanism in a dose-dependent manner. These effects were prevented by cotreatment with hirudin, a specific thrombin inhibitor. Treatment of the cultures with a synthetic thrombin receptor-activating peptide (SFLLRNP) mimicked the deleterious effects of thrombin on motoneurons. Furthermore, cotreatment of the cultures with inhibitors of caspase activities completely prevented the death of motoneurons induced by either thrombin or SFLLRNP. These findings indicate that (1) embryonic avian spinal motoneurons express functional PAR-1 and (2) activation of this receptor induces neuronal cell degeneration and death via stimulation of caspases. Together with previous reports, our results suggest that thrombin, its receptor(s), and endogenous thrombin inhibitors may be important regulators of neuronal cell fate during development, after injury, and in pathology of the nervous system.
越来越多的证据表明,类凝血酶丝氨酸蛋白酶及其同源抑制剂(丝氨酸蛋白酶抑制剂)在神经系统的正常发育和/或病理过程中发挥着多种作用。除了在血栓形成和/或止血方面的显著作用外,凝血酶在体外可抑制神经母细胞瘤和原代神经元细胞的神经突生长,阻止胶质细胞形成星状突起,并在胶质细胞和神经元细胞培养物中诱导细胞死亡。已知凝血酶通过细胞表面蛋白酶激活受体(PAR-1)发挥作用,最近的证据表明啮齿动物神经元表达PAR-1。此前,我们已经表明,凝血酶抑制剂蛋白酶nexin-1在体外和体内均能显著预防神经元细胞死亡。在此,我们研究了人α-凝血酶以及PAR-1的存在和/或激活对高度富集的胚胎鸡脊髓运动神经元培养物的存活和分化的影响。我们发现,凝血酶以剂量依赖的方式显著缩短了平均神经突长度,阻止了神经突分支,并通过类似凋亡的机制诱导运动神经元死亡。水蛭素(一种特异性凝血酶抑制剂)共同处理可防止这些作用。用合成的凝血酶受体激活肽(SFLLRNP)处理培养物可模拟凝血酶对运动神经元的有害作用。此外,用半胱天冬酶活性抑制剂共同处理培养物可完全防止由凝血酶或SFLLRNP诱导的运动神经元死亡。这些发现表明:(1)胚胎鸡脊髓运动神经元表达功能性PAR-1;(2)该受体的激活通过刺激半胱天冬酶诱导神经元细胞变性和死亡。与先前的报道一起,我们的结果表明,凝血酶及其受体以及内源性凝血酶抑制剂可能是发育过程中、损伤后以及神经系统病理状态下神经元细胞命运的重要调节因子。