Serine proteinase fromStaphylococcus aureusenhances elastin degradation by elastases in the presence of human α-1-proteinase inhibitor
✍ Scribed by Dariusz Nowak; Jacek Międzobrodzki
- Publisher
- Springer Netherlands
- Year
- 1991
- Tongue
- English
- Weight
- 424 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0003-6072
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✦ Synopsis
During staphylococcal pneumonia massive destruction of lung tissue is often observed. Staphylococcal serine proteinase (SSP) inactivates a-l-proteinase inhibitor (alPI) a major factor which protects lungs from phagocyte proteases. We investigated the effect of SSP on elastin degradation by porcine pancreatic elastase (PE) and crude extract of human neutrophil elastase (NE) in solution and gel containing alPI. SSP having no elastase activity enhanced PE and NE-induced elastinolysis in solution when added to ctlPI before mixing with elastase and then with elastin. SSP added simultaneously with alPI to PE had no influence on elastin degradation. However, SSP added simultaneously, 30 min before or 30 min after PE significantly increased elastin digestion in elastin-agarose plate with alPI. Maximal increase in elastinolysis about 3-fold was for SSP added 30 min prior to PE. Since elastin is the major component of the alveolar walls it is possible that lung damage in the course of staphylococcal infection may partly depend on action of SSP.