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Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets

American Journal of Physiology-Lung Cellular and Molecular Physiology, 1992
The neutrophil-activating peptide-2 (NAP-2) is a cytokine that is generated by the proteolytic cleavage of a precursor protein and that causes neutrophil degranulation and chemotaxis. NAP-2 precursors are produced in platelets and are normally found in the circulation. We showed that NAP-2 is generated by the action of neutrophil cathepsin G on two of
A B, Cohen, M D, Stevens, E J, Miller, M A, Atkinson, G, Mullenbach   +4 more
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Renal cathepsin G and angiotensin II generation

Journal of Hypertension, 2006
Alternative pathways of angiotensin II biosynthesis play a significant role in the renin-angiotensin system. In this study porcine renal tissue was investigated for angiotensin II-generating enzymes.Protein extracts from porcine renal tissue were fractionated by liquid chromatography and tested for their angiotensin II-generating activity by the mass ...
Rykl, J., Thiemann, J., Kurzawski, S., Pohl, T., Gobom, J., Zidek, W., Schlüter, H.   +6 more
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A Cytosolic Inhibitor of Human Neutrophil Elastase and Cathepsin G

Journal of Leukocyte Biology, 1991
Abstract The neutrophil serine proteinases elastase and cathepsin G produce connective tissue injury, the extent of which depends on the balance between these enzymes and their inhibitors. The most important of these inhibitors is α1-proteinase inhibitor, a member of a superfamily of homologous proteins known as serpins.
R M, Thomas, W M, Nauseef, S S, Iyer, M W, Peterson, P J, Stone, R A, Clark   +5 more
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Role of Cathepsin G in Atherosclerosis

, 2013
Angiotensin II (Ang II) is an important modulator for development of atherosclerosis from early stage foam cell formation to advanced stage plaque rupture. Recently, the importance of locally generated Ang II, especially in macrophages, has become more evident.
Rafatian, Naimeh
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Specificity of human cathepsin G

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
A series of tetrapeptide p-nitroanilide substrates of the general formula: suc-Ala-Ala-Pro-Aaa-p-nitroanilide was used to map the S1 binding pocket of human cathepsin G. Based on the kcat/Km parameter, the following order of preference was found: Lys=Phe>Arg=Leu>Met>Nle=Nva>Ala>Asp.
J, Polanowska, I, Krokoszynska, H, Czapinska, W, Watorek, M, Dadlez, J, Otlewski   +5 more
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Turnover and distribution of cathepsin G in the rat

Scandinavian Journal of Clinical & Laboratory Investigation, 1993
The turnover of 125I labelled rat polymorphonuclear leukocyte (PMN) cathepsin G with retained enzymatic activity was followed 180 min after an intravenous injection. The plasma half-life of injected radioactivity was approximately 4.5 min. In the plasma sample 15 min after injection the main part of the radioactivity in a gel filtration eluted at the ...
P, Björk, A, Luts, F, Sundler, K, Ohlsson   +3 more
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Cathepsin G degrades denatured collagen

Inflammation, 1989
Neutrophils are known to contain several metalloproteinases that can damage collagen, a major structural component of the extracellular matrix. Here a neutrophil serine proteinase secreted from activated neutrophils was shown to cleave denatured collagen (gelatin).
C, Capodici, R A, Berg
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Activation of neutrophil collagenase by cathepsin G

Inflammation, 1989
Collagenase is secreted from neutrophils as a latent or proenzyme. In an effort to understand the mechanism of collagenase activation in inflammation, human peripheral neutrophils (PMNs) were isolated and incubated with the tumor promotor, phorbol myristate acetate (PMA), which induces the neutrophils to degranulate and secrete proteinases.
C, Capodici, G, Muthukumaran, M A, Amoruso, R A, Berg   +3 more
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Stimulation of human lymphocytes by cathepsin G

Cellular Immunology, 1995
We investigated the effect of cathepsin G, a serine protease in polymorphonuclear granulocytes, on the function of human lymphocytes. Cathepsin G increased the [3H]thymidine incorporation into human lymphocytes. This mitogenic activity was due to the proteolytic activity of cathepsin G.
T, Hase-Yamazaki, Y, Aoki
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