Owen C A, Campbell E J
Division of Respiratory, Critical Care and Occupational Pulmonary Medicine, University of Utah Health Sciences Center and Salt Lake VAMC 84132, USA.
Semin Cell Biol. 1995 Dec;6(6):367-76. doi: 10.1016/s1043-4682(05)80007-8.
Neutrophil proteinases have the capacity to degrade almost every component of the extracellular matrix. In marked contrast to the wealth of available data about the structure and activity of these proteinases when they are free in solution, there has been relatively little information about the mechanisms by which neutrophils use and control their proteolytic enzymes in an extracellular milieu that is replete with proteinase inhibitors. However, recent data have provided insights into several mechanisms that permit these enzymes to evade inhibition: (1) compartmentalization; (2) localized inactivation of proteinase inhibitors; (3) tight binding of enzymes to substrates; and (4) binding of proteinases to the neutrophil's cell surface.
中性粒细胞蛋白酶有能力降解细胞外基质的几乎每一种成分。与这些蛋白酶在溶液中游离时关于其结构和活性的丰富现有数据形成鲜明对比的是,关于中性粒细胞在富含蛋白酶抑制剂的细胞外环境中使用和控制其蛋白水解酶的机制的信息相对较少。然而,最近的数据提供了对几种使这些酶逃避抑制的机制的见解:(1)区室化;(2)蛋白酶抑制剂的局部失活;(3)酶与底物的紧密结合;以及(4)蛋白酶与中性粒细胞细胞表面的结合。