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白细胞和肿瘤细胞在底物上的细胞周围蛋白水解作用:局灶性激活及尿激酶型纤溶酶原激活剂的作用

Pericellular proteolysis by leukocytes and tumor cells on substrates: focal activation and the role of urokinase-type plasminogen activator.

作者信息

Kindzelskii Andrei L, Amhad Imran, Keller Donald, Zhou M-J, Haugland Richard P, Garni-Wagner B A, Gyetko Margaret R, Todd Robert F, Petty Howard R

机构信息

Department of Ophthalmology and Visual Sciences and Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48105, USA.

出版信息

Histochem Cell Biol. 2004 Apr;121(4):299-310. doi: 10.1007/s00418-004-0639-3. Epub 2004 Mar 20.

Abstract

Previous studies have shown that the urokinase-type plasminogen activator receptor (uPAR) is localized to the adherence sites of leukocytes and tumor cells suggesting that pericellular proteolysis may accompany focal activation of adherence. To assess for focused pericellular proteolytic activity, we prepared two-dimensional substrates coated with FITC-casein or Bodipy FL-BSA. These molecules are poorly fluorescent, but become highly fluorescent after proteolytic degradation. Fluorescent peptide products were observed at adherence sites of stationary human neutrophils and at lamellipodia of polarized neutrophils. During cell migration, multiple regions of proteolysis appeared sequentially beneath the cell. Similarly, proteolytic action was restricted to adherence sites of resting HT1080 tumor cells but localized to the invadopodia of active cells. Using an extracellular fluorescence quenching method, we demonstrate that these fluorescent peptide products are extracellular. The uPA/uPAR system played an important role in the observed proteolytic activation. Plasminogen activator inhibitor-1 significantly reduced focal proteolysis. Sites of focal proteolysis matched the membrane distribution of uPAR. When uPA was dissociated from uPAR by acid washing, substantially reduced pericellular proteolysis was found. uPAR-negative T47D tumor cells did not express significant levels of substrate proteolysis. However, transfectant clones expressing uPAR (for example, T47D-26) displayed high levels of fluorescence indicating proteolysis at adherence sites. To provide further evidence for the role of the uPA/uPAR system in pericellular proteolysis, peritoneal macrophages from uPA knock-out (uPA-/-) and control (uPA+/+) mice were studied. Pericellular proteolysis was dramatically reduced in uPA-negative peritoneal macrophages. Thus, we have: (1). developed a novel methodology to detect pericellular proteolytic function, (2). demonstrated focused activation of proteolytic enzymatic activity in several cell types, (3). demonstrated its usefulness in real-time studies of cell migration, and (4). showed that the uPA/uPAR system is an important contributor to focal pericellular proteolysis.

摘要

先前的研究表明,尿激酶型纤溶酶原激活剂受体(uPAR)定位于白细胞和肿瘤细胞的黏附部位,这表明细胞周蛋白水解可能伴随黏附的局部激活。为了评估局部细胞周蛋白水解活性,我们制备了包被有FITC-酪蛋白或Bodipy FL-牛血清白蛋白的二维底物。这些分子荧光较弱,但在蛋白水解降解后会变得高度荧光化。在静止的人中性粒细胞的黏附部位和极化中性粒细胞的片状伪足处观察到了荧光肽产物。在细胞迁移过程中,蛋白水解的多个区域依次出现在细胞下方。同样,蛋白水解作用仅限于静止的HT1080肿瘤细胞的黏附部位,但定位于活跃细胞的侵袭伪足。使用细胞外荧光淬灭方法,我们证明这些荧光肽产物是细胞外的。uPA/uPAR系统在观察到的蛋白水解激活中起重要作用。纤溶酶原激活剂抑制剂-1显著降低局部蛋白水解。局部蛋白水解部位与uPAR的膜分布相匹配。当通过酸洗使uPA与uPAR解离时,发现细胞周蛋白水解显著减少。uPAR阴性的T47D肿瘤细胞未表现出显著水平的底物蛋白水解。然而,表达uPAR的转染克隆(例如,T47D-26)显示出高水平的荧光,表明在黏附部位有蛋白水解。为了进一步证明uPA/uPAR系统在细胞周蛋白水解中的作用,研究了来自uPA基因敲除(uPA-/-)和对照(uPA+/+)小鼠的腹腔巨噬细胞。uPA阴性的腹腔巨噬细胞中的细胞周蛋白水解显著降低。因此,我们:(1)开发了一种检测细胞周蛋白水解功能的新方法,(2)证明了几种细胞类型中蛋白水解酶活性的局部激活,(3)证明了其在细胞迁移实时研究中的有用性,以及(4)表明uPA/uPAR系统是局部细胞周蛋白水解的重要贡献者。

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