Rosnoblet C, Vischer U M, Gerard R D, Irminger J C, Halban P A, Kruithof E K
Division of Angiology and Hemostasis, and Clinical Biochemistry, Louis Jeantet Research Laboratories, University Hospital Geneva, Switzerland.
Arterioscler Thromb Vasc Biol. 1999 Jul;19(7):1796-803. doi: 10.1161/01.atv.19.7.1796.
Tissue-type plasminogen activator (t-PA) is acutely released by endothelial cells. Although its endothelial storage compartment is still not well defined, t-PA release is often accompanied by release of von Willebrand factor (vWf), a protein stored in Weibel-Palade bodies. We investigated, therefore, whether t-PA is stored in these secretory organelles. Under basal culture conditions, a minority of human umbilical vein endothelial cells (HUVEC) exhibited immunofluorescent staining for t-PA, which was observed only in Weibel-Palade bodies. To increase t-PA expression, HUVEC were infected with a t-PA recombinant adenovirus (AdCMVt-PA). Overexpressed t-PA was detected in Weibel-Palade bodies and acutely released together with endogenous vWf by thrombin or calcium ionophore stimulation. In contrast, plasminogen activator inhibitor type 1 and urokinase were not detected in Weibel-Palade bodies after adenovirus-mediated overexpression. Infection of HUVEC with proinsulin recombinant adenovirus resulted in the storage of insulin in Weibel-Palade bodies, indicating that these organelles can also store nonendothelial proteins that show regulated secretion. Infection of AtT-20 pituitary cells, a cell type with regulated secretion, with AdCMVt-PA resulted in the localization of t-PA in adrenocorticotropic hormone-containing granules, indicating that t-PA can be diverted to secretory granules independently of vWf. Coinfection of AtT-20 cells with AdCMVt-PA and proinsulin recombinant adenovirus resulted in the colocalization of t-PA and insulin in the same granules. Taken together, these results suggest that HUVEC have protein sorting mechanisms similar to those of other regulated secretory cells. Although the results did not exclude an alternative storage site for t-PA in HUVEC, they established that t-PA can be stored in Weibel-Palade bodies. This finding may explain the acute coordinate secretion of t-PA and vWf.
组织型纤溶酶原激活物(t-PA)由内皮细胞急性释放。尽管其在内皮细胞中的储存部位仍未明确界定,但t-PA的释放通常伴随着血管性血友病因子(vWf)的释放,vWf是一种储存在魏尔-帕拉德小体中的蛋白质。因此,我们研究了t-PA是否储存在这些分泌细胞器中。在基础培养条件下,少数人脐静脉内皮细胞(HUVEC)呈现t-PA免疫荧光染色,且仅在魏尔-帕拉德小体中观察到。为增加t-PA表达,用t-PA重组腺病毒(AdCMVt-PA)感染HUVEC。过表达的t-PA在魏尔-帕拉德小体中被检测到,并在凝血酶或钙离子载体刺激下与内源性vWf一起急性释放。相反,腺病毒介导的过表达后,在魏尔-帕拉德小体中未检测到纤溶酶原激活物抑制剂1型和尿激酶。用胰岛素原重组腺病毒感染HUVEC导致胰岛素储存在魏尔-帕拉德小体中,表明这些细胞器也可储存显示调节性分泌的非内皮蛋白。用AdCMVt-PA感染AtT-20垂体细胞(一种具有调节性分泌的细胞类型)导致t-PA定位于含促肾上腺皮质激素的颗粒中,表明t-PA可独立于vWf被转运至分泌颗粒。AtT-20细胞用AdCMVt-PA和胰岛素原重组腺病毒共感染导致t-PA和胰岛素在同一颗粒中共定位。综上所述,这些结果表明HUVEC具有与其他调节性分泌细胞类似的蛋白质分选机制。尽管结果并未排除HUVEC中t-PA的其他储存位点,但证实了t-PA可储存在魏尔-帕拉德小体中。这一发现可能解释了t-PA和vWf的急性协同分泌。