Date of Graduation
Bachelor of Science in Biomedical Engineering
Wolchok, Jeffrey C
In order to lengthen the functional time of implantable ECM, the mechanism of degradation must be inhibited. The matrix metalloproteases are the primary method by which ECM is broken down, and the TIMP family of proteins exists as proof that inhibition of these proteases is possible naturally. In particular, the glycoprotein TIMP-1 plays an inhibitory role with most of the MMPs including the collagenases. Furthermore, there exist synthetic or chemical molecules that likewise inhibit the catalytic actions of MMPs. One such molecule is Batimastat (BB-94) which has been proven to be a dose dependent inhibitor of MMPs during the inflammatory response. In order to evaluate the potential to increase the effective time of ECM based implants, an in vitro assay was developed to monitor the natural degradation rate of ECM in culture with DQ collagen and 3T3 fibroblasts. The protein TIMP-1 and the molecule BB-94 were incorporated into this model to evaluate their potential use in controlling the degradation rate of ECM implants.
Jones, J. D. (2015). Monitoring the Effects of MMP Inhibitors on Extracellular Matrix Degradation for use in Implant Protection. Biomedical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/bmeguht/14