Neutrophil proteinases and matrix degradation. The cell biology of pericellular proteolysis.
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.
Owen
C A
CA
Division of Respiratory, Critical Care and Occupational Pulmonary Medicine, University of Utah Health Sciences Center and Salt Lake VAMC 84132, USA.
Campbell
E J
EJ
D001665:Binding Sites; D002462:Cell Membrane; D010450:Endopeptidases / Q000145:classification / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009504:Neutrophils / Q000201:enzymology*; D015530:Nuclear Matrix / Q000378:metabolism*; D011480:Protease Inhibitors; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010450:Endopeptidases