IN VITRO STUDY SHOWING THE ACTIVITY OF MATRIX METALLOPROTEINASE-2(MMP-2) ON GELATIN AND THE EFFECT OF CHELATING AGENT (1, 10 PHENANTHROLINE) ON THE REACTION
Journal Title: European Journal of Biomedical and Pharmaceutical Sciences - Year 2018, Vol 5, Issue 7
Abstract
The Matrix Metalloproteinase-2 (MMP-2) is a zn2+ dependent enzyme that plays a crucial role in degradation and remodelling of extracellular matrix. Matrix metalloproteinase-2 is expressed in gliomas and other causing cell invasion and migration. The purpose of this study is to carry out an in vitro study of matrix metalloproteinase-2 on gelatine and investigate the effect of chelating agent(1,10 phenanthroline) on the reaction. The study was demonstrated using collagenase assay, time course assay and gelatinase inhibition assay method. From the result obtained for fluoregenic activity, the fluorescence activity increased with time from 2min to 120min. But on further incubation for more than 120 minutes there was a leaving off indicating that clostridium collagenase (MMP-2) has fit in all the available substrate (gelatine). On further attempts to compare the activity of Merk enzyme that has close activity with 1U/Ml collagenase (MMP-2), the 1.5ng/mg to 100ng/mg of Merk enzyme has no close activity compare to 1U/Ml but at 120ng/mg, Merk enzyme (active human recombinant MMP-2) has a close activity with 1U/ml. However, on the other hand the mean fluorescent of 1U/ml show slight variation when compare to mean fluorescent of 120ng/mg Merk enzyme which may be attributed to temperature. The activity of MMP-2 with 1,10 phenanthroline at 50μM to 1250 μM was markedly reduced by percentage (%) fluorescent activity with an indication of high inhibitory activity. In conclusion, fluoregenic activity of MMP-2 increases with time and 1,10 phenanthroline inhibits the activity of MMP-2 in vitro at varying concentration. However, temperature was the determinant factor in the change of fluorescent activity in the collagenase and inhibition assay.
Authors and Affiliations
Gregory Elayeche Oko
Keywords
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