Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14514
ชื่อเรื่อง: Effects of naofen on enzyme activities of serine proteases and matrix metallo-p roteinases
ผู้แต่ง: Wongsawatkul O.
Feng G.-G.
Li C.
Huang L.
Kondo F.
Kurokawa S.
Fujiwara Y.
Ishikawa N.
Keywords: 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
วันที่เผยแพร่: 2011
บทคัดย่อ: 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.
URI: https://ir.swu.ac.th/jspui/handle/123456789/14514
https://www.scopus.com/inward/record.uri?eid=2-s2.0-79957818327&doi=10.3923%2fijp.2011.388.393&partnerID=40&md5=ae2db1cddeccc424ad94d0fd1f400849
ISSN: 18117775
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.