With the use of supramolecule-based chemically reactive cytokines and growth factors, membrane receptor proteins can be covalently labeled with fluorescent small molecules. This supramolecular approach is quite simple and flexible, and various endogenous receptors can be visualized specifically; real-time imaging of the ligand-induced dynamics of the receptors is achieved in living mammalian cells.
Herein, we report a novel signal-amplifiable self-assembling fluorescent nanoprobe for turn-on detection of specific enzyme activity. This probe employed a substrate of matrix metalloproteinase 2 (MMP2) together with a self-assembling unit, and showed a detection limit of less than 830 pM, which is 84-fold lower than that of our previous ligand-tethered fluorescent nanoprobes. Using this new probe, we succeeded in monitoring the specific activity of secreted MMP even in the conditioned media of tumor cells.Real-time imaging of specific enzyme activities offers valuable information in understanding the biological processes and in development of medicine for various types of diseases.
Temporal change in G protein system -*as invcstigatcd by solving non lincar ratc cquations to show the effects of changes in rate constants on the concentrations of complexes comprising the G protein activation and inhibition reactions. In the rcgulation proccsses of G protein system as the intracellular signal transduction mechanisms, thc ratc constant for linking agonistic hormone on the receptor of targct cell has the dominativc effects on the following scqucntial recruit able reactions. It also influcnccs on the activation of G protcin that has inhibitory action of the target adenylate cyclase.Biochemical signal transduction, G protein,
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