Inhibition effects of peptide hydrolysates from Astragalus membranaceus Bunge. on the expression of the matrix metalloproteinases (MMPs) in human dermal fibroblasts were evaluated in vitro. Crude peptides were obtained by the hydrolysis of proteins extracted from A. membranaceus. Peptides were purified partially by the basis on the molecular weight using 40% polyacrylamide gel electrophoresis before treatment with human dermal fibroblasts. Basis on the doseeffect experiments, expressions of MMPs including MMP-1, MMP-3, MMP-8, MMP-13 in human dermal fibroblasts were evaluated. Expressions of MMP-1, MMP-3, MMP-8 and MMP-13 were reduced in 43%, 5%, 22% and 57% respectively. The mass spectrometric analysis of partially purified peptides from A. membranaceus, which strongly inhibit expressions of MMPs, indicated that the peptides were composed of molecules below 1500 Da.
A study was made in a number of parallel experiments
of the superoxide dismutase activity change in human
placentae in relation to their age. It was found that the
enzyme activity calculated for a given wet weight increased
with the age of the placenta. The increasing amount of enzyme
presumably protects the fetus from the destructive effect of
the 0(2)- radical.
Consideration and comparison of specific superoxide
dismutase activities shows that - of the values calculated for the
same wet weight - the superoxide dismutase activity of the liver is
more than twice that of the other tissues. This indicates the important
metabolism-directing role of the liver. The large amount
of superoxide dismutase (even the tissular superoxide dismutase
alone) protects the tissues from the effects of the 0(2-) radical, and the function of the superoxide
dismutase probably opposing the cytochrome P-450 may be important as regards
the hydroxylase effect.
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