Model discrimination for Ca2+‐dependent regulation of myosin light chain kinase in smooth muscle contraction. Issue 16 (13th August 2018)

• Record Type: Journal Article
• Authors: Dexter, Joseph P.; Biddle, John W.; Gunawardena, Jeremy
• Is Part Of: FEBS letters. Volume 592:Issue 16(2018)
• Page Start: 2811
• Page End: 2821
• Publication Date: 2018-08-13
• Subjects: calcium signaling -- calmodulin -- excitation‐contraction coupling -- linear framework -- mathematical modeling -- myosin light chain kinase; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13207
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Excitation‐contraction coupling in smooth muscle is mediated by the Ca 2+ ‐ and calmodulin‐dependent regulation of myosin light chain kinase. The precise mechanism of this regulation remains controversial, and several mathematical models have been proposed for the interaction of the three species. These models have previously been analyzed at steady state primarily by numerical simulation of differential equations, for which parameter values must be estimated from data. Here, we use the linear framework for timescale separation to demonstrate that models of this general kind can be solved analytically for an equilibrium steady state, without having to determine parameter values. This analysis leads to parameter‐independent methods for discriminating between the models, for which we propose experiments that could be performed with existing methods. Abstract :