NEUTROPHIL PROTEINASES AND MATRIX DEGRADATION - THE CELL BIOLOGY OF PERICELLULAR PROTEOLYSIS

被引:69
作者
OWEN, CA [1 ]
CAMPBELL, EJ [1 ]
机构
[1] UNIV UTAH, VET ADM MED CTR, SALT LAKE CITY, UT 84132 USA
来源
SEMINARS IN CELL BIOLOGY | 1995年 / 6卷 / 06期
关键词
EXTRACELLULAR MATRIX; HUMAN LEUKOCYTE ELASTASE; POLYMORPHONUCLEAR NEUTROPHIL; PROTEINASE; PROTEOLYSIS;
D O I
10.1016/S1043-4682(05)80007-8
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:367 / 376
页数:10
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