title: Mathematical modeling of the relation between myosin phosphorylation and stress development in smooth muscles.
abstract: In this paper the 4-state latch bridge model proposed by Rembold and Murphy is expanded; first by incorporation of the analytical expression of Ca2+ dependent MLCK activation from the work of Kato et al. and second, by inclusion of the myosin dephosphorylation based on the Michaelis-Menten kinetics. The analysis of the proposed model and the comparison with the original model results as well as with the experimental data is presented. The model is able to predict the steady-state isometric stress and the myosin phosphorylation in dependence on steady cytosolic [Ca2+] as well as the temporal evolution of the system in dependence on the input Ca2+ signal in the form of biphasic transient, whereby our model results are in several aspects in better agreement with experimental observations.
authors.affiliation: Faculty of Medicine, Department of Biophysics and Faculty of Education, Department of Physics, University of Maribor, Koroska cesta 160, SI-2000 Maribor, Slovenia. ales.fajmut@uni-mb.si
authors.forename: Ales
authors.initials: A
authors.lastname: Fajmut
authors.forename: Andrej
authors.initials: A
authors.lastname: Dobovisek
authors.forename: Milan
authors.initials: M
authors.lastname: Brumen
mesh_terms: D000465:Algorithms; D020013:Calcium Signaling; D002147:Calmodulin / Q000502:physiology; D003198:Computer Simulation; D007700:Kinetics; D015233:Models, Statistical; D009130:Muscle, Smooth / Q000502:physiology*; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation; D011237:Predictive Value of Tests
chemical_list: D002147:Calmodulin; D009219:Myosin-Light-Chain Kinase; D009218:Myosins