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首页> 外文期刊>Journal of Cellular Physiology >Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP).
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Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP).

机译：处理、脱落和内吞作用的膜1)矩阵型金属蛋白酶(MT1-MMP)。

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摘要

Matrix metalloproteinases (MMPs) are multidomain zinc-dependent proteolytic enzymes that play pivotal roles in many normal and pathological processes. Some members of the MMP family are anchored to the plasma membrane via specialized domains and thus are perfectly suited for pericellular proteolysis. Membrane-anchoring also confers the membrane type-MMPs (MT-MMPs) a unique and complex array of regulatory processes that endow cells with the ability to control MT-MMP-dependent proteolytic activity independently of the levels of endogenous protease inhibitors. Emerging evidence indicates that mechanisms as diverse as autocatalytic processing, ectodomain shedding, homodimerization and internalization can all contribute to the modulation of MT-MMP activity on the cell surface. How these distinct processes interact to attain the optimal level of enzyme activity in a particular setting and the molecular signals that trigger them constitute a new paradigm in MMP regulation. This review will discuss the recent findings concerning these diverse regulatory mechanisms in the context of MT1-MMP (MMP-14).
机译：基质金属蛋白酶(MMPs)是多畴的zinc-dependent蛋白水解酶关键的角色在许多正常和病理流程。通过专门的固定在质膜域,因此非常适合pericellular蛋白水解作用。赋予薄膜type-MMPs (MT-MMPs)独一无二的和复杂的一系列管理过程赋予细胞控制的能力MT-MMP-dependent蛋白水解活性独立于内生的水平蛋白酶抑制剂。催化等机制处理,homodimerization ectodomain脱落和内化都可以做出贡献调制MT-MMP活动的细胞表面。达到最优水平的酶活性特定的设置和分子信号引发MMP构成一个新的范式监管。发现关于这些不同的监管机制的上下文中MT1-MMP (MMP-14)。

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