Expression of MMP-9 (Matrix Metalloproteinase-9)
Thesis (Dissertationen, Habilitationen)
 
ID 4627660
Author Wasescha, Alesch
Author at UniBasel Meyer zu Schwabedissen, Henriette
Year 2016
Title Expression of MMP-9 (Matrix Metalloproteinase-9)
Type of Thesis Masterarbeit
Start of thesis 11.01.2016
End of thesis 03.06.2016
Name of University University of Basel
Name of Faculty Philosophisch-Naturwissenschaftliche Fakultät
Supervisor(s) / Fachvertreter/in Meyer zu Schwabedissen, Henriette
Abstract

Glioblastoma multiforma is considered the most aggressive brain tumour. It has been shown, that the malignancy of glioblastoma and several other tumours is linked to overexpression of Matrix Metalloproteinase- 9 (MMP-9). The physiological function of this 92 kDa enzyme is to cleave surrounding tissue, ensuring angiogenesis. With this property, it pathophysiologically promotes tumour growth. Specific inhibition of MMP-9 has become a challenge due to similarities within the MMP family. Recently, the focus has switched from inhibition of MMP-9 towards using it as an activating factor of an enzymatic drug delivery system. A peptide, which is specifically cleaved by MMP-9, is linked to a cytostatic drug. This will have the
advantage of specific activation in MMP-9 expressing tissues, hoping to reduce systemic side effects. For conducting activity essays, MMP-9 is needed in larger quantities, which leads to high costs. In this thesis, the expression of MMP-9 through different established systems, namely cell transfection and expression in E. coli and alternatively cell-free expression system, was investigated. Western Blot and zymography were used to detect MMP-9. No MMP- 9 could be proven in lysate and supernatant of transfected HEK293 cells. Active MMP-9 was expressed in transformed BL21(DE3)pLysS E. coli, but was lost during purification. Protein with affinity to MMP-9 antibodies was detected after His-tag purification of the cell-free expression
system, but not after cleavage by HRV 3c protease.

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