Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors.
Acta Pharmacol Sin
; 24(9): 923-9, 2003 Sep.
Article
en En
| MEDLINE
| ID: mdl-12956943
ABSTRACT
AIM:
To investigate the actions of protease inhibitors on the enzymatic activities of tryptase and chymase in similar experimental systems.METHODS:
Human lung tryptase and human skin chymase were purified by a similar procedure involving high salt extraction of tryptase, heparin agarose affinity chromatography, and S-200 Sephacryl gel filtration chromatography. Actions of protease inhibitors on tryptase and chymase activities were examined by enzyme assays.RESULTS:
The specific activities of tryptase and chymase were 2.1 kU/g protein and 4.9 kU/g protein, respectively. Both preparations showed a single diffuse band on SDS-PAGE. Among non-native protease inhibitors, N-(1-hydroxy-2-naphthoyl)-L- arginyl-L-prolinamide hydrochloride (HNAP), leupeptin, antipain, benzamidine, and protamine inhibited more than 90 % enzymatic activity of tryptase, whereas soy bean trypsin inhibitor (SBTI), Z-Ile-Glu-Pro-Phe-CO2Me (ZIGPPM) and chymostatin inhibited more than 95 % enzymatic activity of chymase. Native protease inhibitors alpha 1-antitrypsin and secretory leukocyte protease inhibitor (SLPI) inhibited more than 90 % enzymatic activity of chymase, but lactoferrin appeared to enhance chymase enzymatic activity. All the 3 inhibitors had weak inhibitory actions on tryptase.CONCLUSION:
The protease inhibitors tested had relatively good selectivity to either tryptase or chymase.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Inhibidores de Proteasas
/
Serina Endopeptidasas
/
Mastocitos
Límite:
Humans
Idioma:
En
Revista:
Acta Pharmacol Sin
Asunto de la revista:
FARMACOLOGIA
Año:
2003
Tipo del documento:
Article
País de afiliación:
China