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Human granulocyte elastase is inhibited by the urinary trypsin inhibitor
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|October 1, 1982
Summary
Two forms of urinary trypsin inhibitor, A and B, were identified in pregnant women's urine. Inhibitor B is derived from the degradation of inhibitor A during storage, with both inhibiting trypsin and granulocyte elastase.
Area of Science:
- Biochemistry
- Proteomics
- Urine analysis
Background:
- Urinary trypsin inhibitors are crucial for regulating protease activity.
- Understanding the forms and properties of these inhibitors is important for physiological studies.
Purpose of the Study:
- To purify and characterize two forms of urinary trypsin inhibitor (A and B) from pregnant women's urine.
- To investigate the relationship between inhibitor A and B and their inhibitory activity.
Main Methods:
- Purification of inhibitors A and B using chromatography.
- Molecular mass determination via SDS-PAGE and gel filtration.
- Amino acid analysis and reduction with mercaptoethanol.
- Agarose gel electrophoresis.
- Immunological characterization using specific antisera.
- Enzyme inhibition assays with trypsin and elastase.
Main Results:
- Urinary trypsin inhibitor A and B were purified; B is a degradation product of A.
- Discrepancies in molecular mass were observed, potentially due to glycosylation.
- Reduced inhibitor A yielded two molecules of inhibitor B, suggesting a dimeric structure for A.
- Inhibitors A and B showed immunological identity with plasma inter-alpha-trypsin inhibitor.
- Both inhibitors effectively neutralized bovine trypsin and granulocyte elastase, but not porcine pancreatic elastase.
Conclusions:
- Urinary trypsin inhibitors A and B are immunologically related to plasma inter-alpha-trypsin inhibitor.
- Inhibitor A is likely a dimer that degrades into inhibitor B.
- These inhibitors play a role in regulating serine proteases like trypsin and granulocyte elastase.