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Rac1介导I型胶原依赖性MMP-2激活。在细胞穿过胶原屏障的侵袭中起作用。

Rac1 mediates type I collagen-dependent MMP-2 activation. role in cell invasion across collagen barrier.

作者信息

Zhuge Y, Xu J

机构信息

Department of Dermatology, School of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794, USA.

出版信息

J Biol Chem. 2001 May 11;276(19):16248-56. doi: 10.1074/jbc.m010190200.

Abstract

Cell migration and proteolysis are two essential processes during tumor invasion and metastasis. Matrix metalloproteinase (MMP)-2 (type IV collagenase; gelatinase A), is implicated in tumor metastasis as well as in primary tumor growth. The Rho family of small GTPases regulates the dynamics of actin cytoskeleton associated with cell motility. In this report, we provide evidence that Rac1, one member of Rho-related small GTPases, is a mediator of MMP-2 activation in HT1080 fibrosarcoma cells cultured in three-dimensional collagen gel (3D-col) and that MMP-2 activation is required for Rac1-promoted cell invasion through collagen barrier. Stable expression of dominant negative (Rac1V12N17) and constitutively active Rac1 (Rac1V12), respectively, in HT1080 cells demonstrates that Rac1 promoted cell invasiveness across type I collagen and collagen-dependent MMP-2 activation. Active Rac1 is sufficient to induce MMP-2 activation in cells cultured in fibrin gel, an extracellular matrix component that does not support MMP-2 activation. The Rac1-dependent MMP-2 activation occurred in a cell-associated fashion and required MMP activities. Because the cell membrane-mediated MMP-2 activation requires MT1-MMP and low amount of issue inhibitor of matrix metalloproteinase-2 (TIMP-2), their expression was examined. Rac1 modulated MT1-MMP mRNA level and the accumulation of a 43-kDa form of MT1-MMP protein, in correlation with MMP-2 activation profile. However, TIMP-2 expression was independent of Rac1 activity. The coordinate modulation of MMP-2 activity and MT1-MMP expression/processing by Rac1 is consistent with cell collagenolytic activity. The C-terminal hemopexin-like domain of MMP-2, which interferes with the cell membrane activation of MMP-2, reduced Rac1-promoted cell invasiveness as monitored by collagen invasion assay. These results suggest that collagen-dependent MMP-2 activation and MT1-MMP expression/processing contribute to Rac-promoted tumor cell invasion through interstitial collagen barrier.

摘要

细胞迁移和蛋白水解是肿瘤侵袭和转移过程中的两个基本过程。基质金属蛋白酶(MMP)-2(IV型胶原酶;明胶酶A)与肿瘤转移以及原发性肿瘤生长有关。小GTP酶的Rho家族调节与细胞运动相关的肌动蛋白细胞骨架的动态变化。在本报告中,我们提供证据表明,Rho相关小GTP酶的成员之一Rac1是在三维胶原凝胶(3D-col)中培养的HT1080纤维肉瘤细胞中MMP-2激活的介质,并且MMP-2激活是Rac1促进细胞通过胶原屏障侵袭所必需的。在HT1080细胞中分别稳定表达显性负性(Rac1V12N17)和组成型活性Rac1(Rac1V12),表明Rac1促进细胞穿过I型胶原的侵袭性以及胶原依赖性MMP-2激活。活性Rac1足以在纤维蛋白凝胶中培养的细胞中诱导MMP-2激活,纤维蛋白凝胶是一种不支持MMP-2激活的细胞外基质成分。Rac1依赖性MMP-2激活以细胞相关方式发生并且需要MMP活性。由于细胞膜介导的MMP-2激活需要MT1-MMP和少量的基质金属蛋白酶-2组织抑制剂(TIMP-2),因此检测了它们的表达。Rac1调节MT1-MMP mRNA水平和43-kDa形式的MT1-MMP蛋白的积累,与MMP-2激活谱相关。然而,TIMP-2表达与Rac1活性无关。Rac1对MMP-2活性和MT1-MMP表达/加工的协同调节与细胞胶原溶解活性一致。MMP-2的C末端血红素结合蛋白样结构域干扰MMP-2的细胞膜激活,通过胶原侵袭试验监测,其降低了Rac1促进的细胞侵袭性。这些结果表明,胶原依赖性MMP-2激活和MT1-MMP表达/加工有助于Rac促进肿瘤细胞通过间质胶原屏障的侵袭。

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