Department of Oncology, University of Cambridge, Cancer Research UK Cambridge Institute, Li Ka Shing Centre, Cambridge, UK.
FEBS J. 2011 Jan;278(1):2-15. doi: 10.1111/j.1742-4658.2010.07918.x. Epub 2010 Nov 19.
Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane-type MMPs (MT-MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane-anchored proteins or cell-associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.
基质金属蛋白酶（MMPs）是一组结构相关的蛋白水解酶，其活性位点含有锌离子。它们从细胞中分泌出来或与质膜结合，水解细胞外基质（ECM）和细胞表面结合的分子。因此，它们在癌症和关节炎等疾病的形态发生、伤口愈合、组织修复和重塑中发挥关键作用。尽管细胞锚定的膜型 MMPs（MT-MMPs）在细胞旁起作用，但分泌的 MMPs 被认为在 ECM 中发挥作用，远离它们合成的细胞。然而，最近的研究表明，分泌的 MMPs 与特定的细胞表面受体、膜锚定蛋白或细胞相关的 ECM 分子结合，并在聚焦位置在细胞旁起作用。这篇综述描述了 MMPs 的细胞表面和细胞旁伙伴的例子，以及它们如何改变酶的功能和细胞行为。
