| Autor: |
Debreczeni ML; 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary., Szekacs I; Nanobiosensorics Momentum Group, Institute of Technical Physics and Materials Science, Centre for Energy Research, Konkoly-Thege M. út 29-33, H-1120, Budapest, Hungary., Kovacs B; Nanobiosensorics Momentum Group, Institute of Technical Physics and Materials Science, Centre for Energy Research, Konkoly-Thege M. út 29-33, H-1120, Budapest, Hungary., Saftics A; Nanobiosensorics Momentum Group, Institute of Technical Physics and Materials Science, Centre for Energy Research, Konkoly-Thege M. út 29-33, H-1120, Budapest, Hungary., Kurunczi S; Nanobiosensorics Momentum Group, Institute of Technical Physics and Materials Science, Centre for Energy Research, Konkoly-Thege M. út 29-33, H-1120, Budapest, Hungary., Gál P; Institute of Enzymology, Research Centre for Natural Sciences, H-1113, Budapest, Hungary., Dobó J; Institute of Enzymology, Research Centre for Natural Sciences, H-1113, Budapest, Hungary., Cervenak L; 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary. cervenak.laszlo@gmail.com., Horvath R; 3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary. r74horvath@gmail.com. |
| Abstrakt: |
Tissue-on-a-chip technologies are more and more important in the investigation of cellular function and in the development of novel drugs by allowing the direct screening of substances on human cells. Constituting the inner lining of vessel walls, endothelial cells are the key players in various physiological processes, moreover, they are the first to be exposed to most drugs currently used. However, to date, there is still no appropriate technology for the label-free, real-time and high-throughput monitoring of endothelial function. To this end, we developed an optical biosensor-based endothelial label-free biochip (EnLaB) assay that meets all the above requirements. Using our EnLaB platform, we screened a set of plasma serine proteases as possible endothelial cell activators, and first identified the endothelial cell activating function of three important serine proteases - namely kallikrein, C1r and mannan-binding lectin-associated serine-protease 2 (MASP-2) - and verified these results in well-established functional assays. EnLaB proved to be an effective tool for revealing novel cellular mechanisms as well as for the high-throughput screening of various compounds on endothelial cells. |
