Publication: Effects of naofen on enzyme activities of serine proteases and matrix metallo-p roteinases
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Issued Date
2011
Resource Type
File Type
application/pdf
ISSN
18117775
Other identifier(s)
2-s2.0-79957818327
Rights Holder(s)
Scopus
Bibliographic Citation
International Journal of Pharmacology. Vol 7, No.3 (2011), p.388-393
Suggested Citation
Wongsawatkul O., Feng G.-G., Li C., Huang L., Kondo F., Kurokawa S., Fujiwara Y., Ishikawa N. Effects of naofen on enzyme activities of serine proteases and matrix metallo-p roteinases. International Journal of Pharmacology. Vol 7, No.3 (2011), p.388-393. doi:10.3923/ijp.2011.388.393 Retrieved from: https://hdl.handle.net/20.500.14740/7313
Abstract
The aim of this study was to investigate whether naofen affected on the activities of metallo and serine proteases. Naofen, found in both intra- and extra-cellular spaces, increased in the livers especially under pathological conditions such as CCl4-induced cirrhosis of rats. Moreover, naofen seemed to be digested into fragments which might be closely correlated to the pathological alterations of proliferations and fibrosis. Recent studies showed that metallo and serine proteases degrade the fibrous tissues. Therefore, we investigated possible influences of naofen fragment (s) on the activities of metallo-protease, gelatinase/collagenase and serine protease, trypsin, in vitro by using quenching fluorescence method. It was found that 1.2×10-1 and 4×l0-8 M naofen C-fragment had inhibitory effect on trypsin but not gelatinase/collagenase activity. Naofen N-fragment of 1.2×l0-7 and 4×-7M did not change gelatinase/collagenase activity but did enhance trypsin activity in a dose-dependent manner. Kunitz type serine protease inhibitor, bikunin inhibited both gelatinase/collagenase and trypsin activities, at bikunin concentrations of 1.2×l0-7 and 1.2×l0-6 g mL-1. Interestingly, naofen N-fragment depleted the reduction ability of bikunin on trypsin from 80 to 50%. These findings indicated that naofen C-fragments may be an endogenous serine protease inhibitor like bikunin, whereas naofen N-fragment may be an enhancer of serine protease and further counteracts the action of the inhibitor, bikunin. Therefore, naofen may be a precursor for active fragments which interacts with serine proteases. © 2011 Asian Network for Scientific Information.
Subject(s)
Carbon tetrachloride
Collagenase
Enzyme precursor
Gelatinase
Matrix metalloproteinase
Naofen
Naofen c
Naofen n
Serine proteinase
Trypsin
Ulinastatin
Unclassified drug
Amino acid sequence
Amino terminal sequence
Article
Carboxy terminal sequence
Cell proliferation
Concentration response
Controlled study
Drug mechanism
Enzyme activity
Enzyme inhibition
Extracellular space
Genomic fragment
In vitro study
Intracellular space
Liver cirrhosis
Liver fibrosis
Nonhuman
Protein expression
Protein function
Collagenase
Enzyme precursor
Gelatinase
Matrix metalloproteinase
Naofen
Naofen c
Naofen n
Serine proteinase
Trypsin
Ulinastatin
Unclassified drug
Amino acid sequence
Amino terminal sequence
Article
Carboxy terminal sequence
Cell proliferation
Concentration response
Controlled study
Drug mechanism
Enzyme activity
Enzyme inhibition
Extracellular space
Genomic fragment
In vitro study
Intracellular space
Liver cirrhosis
Liver fibrosis
Nonhuman
Protein expression
Protein function