Behn, Daniela and Bosk, Sabine and Hoffmeister, Helen and Janshoff, Andreas and Witzgall, Ralph and Steinem, Claudia (2010) Quantifying the interaction of the C-terminal regions of polycystin-2 and polycystin-1 attached to a lipid bilayer by means of QCM. BIOPHYSICAL CHEMISTRY, 150 (1-3). pp. 47-53. ISSN 0301-4622, 1873-4200
Full text not available from this repository. (Request a copy)Abstract
The pkd1 and pkd2 genes encode for the proteins polycystin-1 (PC1) and polycystin-2 (PC2). These genes are mutated in patients diagnosed with autosomal dominant polycystic kidney disease. PC1 and PC2 interact via their C-terminal, cytosolic regions, which is an essential step in the regulation of cell proliferation and differentiation. Here, we developed an assay that allowed us to quantitatively monitor the interaction of the C-terminal region of PC1 (cPC1) with that of PC2 (cPC2) to be able to answer the question of how Ca2+ influences the PC1/PC2 complex formation. By means of the quartz crystal microbalance (QCM) technique, we were able to determine binding affinities and kinetic constants of the cPC1/cPC2 interaction using a model based on the scaled particle theory. The results suggest that cPC2 forms trimers in solution in the absence of Ca2+, which bind in a one step process to cPC1. (C) 2010 Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | QUARTZ-CRYSTAL MICROBALANCE; PLASMA-MEMBRANE; CATION CHANNEL; KIDNEY-DISEASE; ADSORPTION; DOMAIN; BIOSENSORS; COMPLEX; Autosomal dominant polycystic kidney disease; Quartz crystal microbalance; Membrane; Scaled particle theory; TRPP2 |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Anatomie > Lehrstuhl für Molekulare und zelluläre Anatomie > Prof. Dr. Ralph Witzgall |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 20 Jul 2020 06:35 |
| Last Modified: | 20 Jul 2020 06:35 |
| URI: | https://pred.uni-regensburg.de/id/eprint/24348 |
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