Abstract
Purified recombinant human monocyte plasminogen activator inhibitor 2 (PAI-2) retained inhibitory activity after exposure to a number of oxidants, including hypochlorite anion (OCl-), chloramine-T (CT) and hydrogen peroxide (H2O2). Analysis of PAI-2 exposed to oxidants by gel filtration chromatography and SDS-PAGE indicated that although the protein could no longer be detected by silver staining, this was not due to fragmentation of the PAI- 2 molecule. The sensitivity of a number of serine protease inhibitors (serpins), (eg. α1 proteinase inhibitor (α1PI) and plasminogen activator inhibitor 1 (PAI-1)) to oxidative inactivation has been attributed to oxidation of reactive site methionine residues and/or tertiary structural modifications. The relevance of these phenomena and the potential for PAI-2 to be used as a therapeutic inhibitor of urokinase (uPA)-dependent proteolysis during inflammation and tumour metastasis is discussed.
Original language | English |
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Pages (from-to) | 993-1000 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 166 |
Issue number | 2 |
DOIs | |
Publication status | Published - 30 Jan 1990 |
Externally published | Yes |