Enzyme-Linked Immunoassay for Human Granulocyte Elastase in Complex with α1 -Proteinase Inhibitor

1984 ◽  
pp. 379-390 ◽  
Author(s):  
Siegfried Neumann ◽  
Norbert Hennrich ◽  
Gerhard Gunzer ◽  
Hermann Lang
Keyword(s):  
Proteinase Inhibitor ◽  
Granulocyte Elastase

Interference of cartilage surface with interaction of granulocyte elastase with ?1-proteinase inhibitor

1987 ◽  
Vol 7 (3) ◽  
pp. 133-138 ◽  
Author(s):  
H. Burkhardt ◽  
M. Kasten ◽  
S. Rauls ◽  
E. Rehkopf
Keyword(s):  
Proteinase Inhibitor ◽  
Cartilage Surface ◽  
Granulocyte Elastase

scholarly journals Limited proteolysis by macrophage elastase inactivates human alpha 1-proteinase inhibitor.

1980 ◽  
Vol 152 (6) ◽  
pp. 1563-1570 ◽  
Author(s):  
M J Banda ◽  
E J Clark ◽  
Z Werb
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Limited Proteolysis ◽  
Serine Proteinase ◽  
Apparent Molecular Weight ◽  
Peritoneal Macrophages ◽  
Granulocyte Elastase ◽  
Inhibitor Complex ◽  
Mouse Peritoneal Macrophages

Inflammatory mouse peritoneal macrophages secrete a metalloproteinase that is not inhibited by alpha 1-proteinase inhibitor. This proteinase, macrophage elastase, recognizes alpha 1-proteinase inhibitor with macrophage elastase does not involve a stable proteinase-inhibitor complex and results in the proteolytic removal of a peptide of apparent molecular weight 4,000-5,000 from the inhibitor. After degradation by macrophage elastase, alpha 1-proteinase inhibitor is no longer able to inhibit human granulocyte elastase, a serine proteinase implicated in the pathogenesis of emphysema. Macrophage elastase apparently does not degrade human granulocyte elastase-alpha 1-proteinase inhibitor complexes or release active granulocyte elastase from these complexes. The ability of macrophage elastase to degrade alpha 1-proteinase inhibitor is inhibited by EDTA and alpha 2-macroglobulin.

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