Kleiner D E, Stetler-Stevenson W G
Laboratory of Pathology, Division of Clinical Sciences, National Cancer Institute, Bethesda, MD 20892, USA.
Cancer Chemother Pharmacol. 1999;43 Suppl:S42-51. doi: 10.1007/s002800051097.
Metastatic disease is responsible for the majority of cancer-related deaths, either directly due to tumor involvement of critical organs or indirectly due to complications of therapy to control tumor growth and spread. An understanding of the mechanisms of tumor cell invasion and metastasis may be important for devising therapies aimed at preventing tumor cell spread. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endoproteinases whose enzymatic activity is directed against components of the extracellular matrix (ECM). In humans, 16 members of this family have been identified by cloning and sequencing. These proteinases are linked by a core of common domain structures and by their relationship to a family of proteinase inhibitors called the tissue inhibitors of metalloproteinases (TIMPs). Four members of the TIMP family have been cloned and sequenced in humans and they inhibit MMPs by forming tight-binding, noncovalent associations with the active site of the MMPs. MMPs facilitate tumor cell invasion and metastasis by at least three distinct mechanisms. First, proteinase action removes physical barriers to invasion through degradation of ECM macromolecules such as collagens, laminins, and proteoglycans. This has been demonstrated in vitro through the use of chemoinvasion assays and in vivo by the presence of active MMPs at the invasive front of tumors. Second, MMPs have the ability to modulate cell adhesion. For cells to move through the ECM, they must be able to form new cell-matrix and cell-cell attachments and break existing ones. Using a cell transfection system that altered the ratio of MMP-2 to TIMP-2 we have demonstrated significant variation in the adhesive phenotype of tumor cells. Finally, MMPs may act on ECM components or other proteins to uncover hidden biologic activities. For example, the angiogenesis inhibitor angiostatin may be produced from plasminogen by MMP action and laminin-5 is specifically degraded by MMP-2 to produce a soluble chemotactic fragment. Thus MMPs play multiple key roles in facilitating the metastasis of tumor cells. Therapies designed to interfere with specific MMP actions may be useful in the control of metastatic disease.
转移性疾病是大多数癌症相关死亡的原因,要么是由于关键器官受到肿瘤侵犯直接导致,要么是由于控制肿瘤生长和扩散的治疗并发症间接导致。了解肿瘤细胞侵袭和转移的机制对于设计旨在防止肿瘤细胞扩散的治疗方法可能很重要。基质金属蛋白酶(MMPs)是一类锌依赖性内切蛋白酶,其酶活性针对细胞外基质(ECM)的成分。在人类中,通过克隆和测序已鉴定出该家族的16个成员。这些蛋白酶通过共同结构域的核心以及它们与一类称为金属蛋白酶组织抑制剂(TIMPs)的蛋白酶抑制剂家族的关系而联系在一起。TIMP家族的四个成员已在人类中克隆和测序,它们通过与MMPs的活性位点形成紧密结合的非共价结合来抑制MMPs。MMPs通过至少三种不同机制促进肿瘤细胞侵袭和转移。首先,蛋白酶作用通过降解ECM大分子(如胶原蛋白、层粘连蛋白和蛋白聚糖)消除侵袭的物理障碍。这已在体外通过化学侵袭试验得到证明,并且在体内通过肿瘤侵袭前沿存在活性MMPs得到证明。其次,MMPs具有调节细胞粘附的能力。为了使细胞在ECM中移动,它们必须能够形成新的细胞-基质和细胞-细胞附着并破坏现有的附着。使用改变MMP-2与TIMP-2比例的细胞转染系统,我们已经证明肿瘤细胞的粘附表型存在显著差异。最后,MMPs可能作用于ECM成分或其他蛋白质以揭示隐藏的生物学活性。例如,血管生成抑制剂血管抑素可能由MMP作用从纤溶酶原产生,并且层粘连蛋白-5被MMP-2特异性降解以产生可溶性趋化片段。因此,MMPs在促进肿瘤细胞转移中发挥多种关键作用。设计用于干扰特定MMP作用的治疗方法可能有助于控制转移性疾病。