scholarly journals Mathematical model of excitation-contraction in a uterine smooth muscle cell

Physiome ◽  
2021 ◽  
Author(s):  
Weiwei Ai ◽  
Limor Freifeld ◽  
David Nickerson
Keyword(s):  
Mathematical Model ◽  
Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Myosin Light Chain ◽  
Original Data ◽  
Uterine Smooth Muscle ◽  
Intracellular Ca ◽  
Myometrial Smooth Muscle Cell ◽  
Mlc Phosphorylation

The Bursztyn et al. (2007) paper proposes a mathematical model of excitation-contraction in a myometrial smooth muscle cell (SMC). The model incorporates processes of intracellular Ca^2+ concentration control, myosin light chain (MLC) phosphorylation and stress production. We create a modularized CellML implementation of the model, which is able to simulate these processes against the original data.

scholarly journals Mathematical model of excitation-contraction in a uterine smooth muscle cell

Physiome ◽  
2021 ◽  
Author(s):  
Weiwei Ai ◽  
Limor Freifeld ◽  
David Nickerson
Keyword(s):  
Mathematical Model ◽  
Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Myosin Light Chain ◽  
Original Data ◽  
Uterine Smooth Muscle ◽  
Intracellular Ca ◽  
Myometrial Smooth Muscle Cell ◽  
Mlc Phosphorylation

The Bursztyn et al. (2007) paper proposes a mathematical model of excitation-contraction in a myometrial smooth muscle cell (SMC). The model incorporates processes of intracellular Ca^2+ concentration control, myosin light chain (MLC) phosphorylation and stress production. We create a modularized CellML implementation of the model, which is able to simulate these processes against the original data.

scholarly journals Inhibitor κB Kinase 2 Is a Myosin Light Chain Kinase in Vascular Smooth Muscle

2013 ◽  
Vol 113 (5) ◽  
pp. 562-570 ◽  
Author(s):  
Zhekang Ying ◽  
Jussara M. do Carmo ◽  
Lusha Xiang ◽  
Alexandre A. da Silva ◽  
Minjie Chen ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Living Cells ◽  
Physiological Importance ◽  
Mlc Phosphorylation

Rationale: Myosin light chain (MLC) phosphorylation determines vascular contractile status. In addition to the classic Ca 2+ -dependent MLC kinase (MLCK), another unidentified kinase(s) also contributes to MLC phosphorylation in living cells. Inhibitor κB kinase 2 (IKK2)–deficient mouse embryonic fibroblasts demonstrate abnormal morphology and migration, suggesting that IKK2 may be involved in MLC phosphorylation. Objective: Therefore, we tested whether IKK2 is an MLCK in living cells and the role of IKK2 in mediating vasoconstriction and blood pressure regulation. Methods and Results: In the present study, we showed that recombinant IKK2–phosphorylated MLC and intact myosin in vitro, and the kinetic parameters were comparable with those of the classic MLCK. Overexpression of IKK2 increased cellular MLC phosphorylation level, and pharmacological inhibition of IKK2 markedly decreased vascular smooth muscle cell MLC phosphorylation, suggesting that IKK2 is an MLCK in living cells. IKK2 inhibitors dose- and time-dependently attenuated vasoconstriction elicited by diverse agonists, suggesting the physiological importance of IKK2 as an MLCK. Vascular smooth muscle cell-specific IKK2-deficient mice had decreased aortic contractile responses, and reduced hypertensive responses to several vasoconstrictors, compared with wild-type mice, confirming the physiological importance of IKK2 as an MLCK. Conclusions: Our data provide a novel mechanism whereby IKK2 regulates MLC phosphorylation as an MLCK and, thus, vascular function and blood pressure.

A mathematical model of Ca2+ dynamics in rat mesenteric smooth muscle cell: Agonist and NO stimulation

2008 ◽  
Vol 253 (2) ◽  
pp. 238-260 ◽  
Author(s):  
Adam Kapela ◽  
Anastasios Bezerianos ◽  
Nikolaos M. Tsoukias
Keyword(s):  
Mathematical Model ◽  
Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Muscle Cell

scholarly journals Impairment of IKCa channels contributes to uteroplacental endothelial dysfunction in rat diabetic pregnancy

2015 ◽  
Vol 309 (4) ◽  
pp. H592-H604 ◽  
Author(s):  
Natalia I. Gokina ◽  
Adrian D. Bonev ◽  
Julie Phillips ◽  
Alexander P. Gokin ◽  
Kelsey Veilleux ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Membrane Potential ◽  
Endothelial Dysfunction ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Vascular Dysfunction ◽  
Citrate Buffer ◽  
Pregnant Rats ◽  
Intracellular Ca ◽  
The Impact

Diabetes in rat pregnancy is associated with impaired vasodilation of the maternal uteroplacental vasculature. In the present study, we explored the role of endothelial cell (EC) Ca2+-activated K+ channels of small conductance (SKCa channels) and intermediate conductance (IKCa channels) in diabetes-induced uterine vascular dysfunction. Diabetes was induced by injection of streptozotocin to second-day pregnant rats and confirmed by the development of maternal hyperglycemia. Control rats were injected with citrate buffer. Changes in smooth muscle cell intracellular Ca2+ concentration, membrane potential, and vasodilation induced by SKCa/IKCa channel activators were studied in uteroplacental arteries of control and diabetic rats. The impact of diabetes on SKCa- and IKCa-mediated currents was explored in freshly dissociated ECs. NS309 evoked a potent vasodilation that was effectively inhibited by TRAM-34 but not by apamin. NS309-induced smooth muscle cell intracellular Ca2+ concentration, membrane potential, and dilator responses were significantly diminished by diabetes; N-cyclohexyl- N-2-(3,5-dimethyl-pyrazol-1-yl)-6-methyl-4-pyrimidinamine (CyPPA)-evoked responses were not affected. Ca2+-activated ion currents in ECs were insensitive to paxilline, markedly inhibited by charybdotoxin (ChTX), and diminished by apamin. NS309-induced EC currents were generated mostly due to activation of ChTX-sensitive channels. Maternal diabetes resulted in a significant reduction in ChTX-sensitive currents with no effect on apamin-sensitive or CyPPA-induced currents. We concluded that IKCa channels play a prevalent role over SKCa channels in the generation of endothelial K+ currents and vasodilation of uteroplacental arteries. Impaired function of IKCa channels importantly contributes to diabetes-induced uterine endothelial dysfunction. Therapeutic restoration of IKCa channel function may be a novel strategy for improvement of maternal uteroplacental blood flow in pregnancies complicated by diabetes.

scholarly journals Anthrax toxin receptor 2 promotes human uterine smooth muscle cell viability, migration and contractility

2014 ◽  
Vol 210 (2) ◽  
pp. 154.e1-154.e8 ◽  
Author(s):  
Joy Yumiko Vink ◽  
Pelisa Cheryll Charles-Horvath ◽  
Jan Krzysztof Kitajewski ◽  
Claire Vech Reeves
Keyword(s):  
Smooth Muscle ◽  
Cell Viability ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Anthrax Toxin ◽  
Uterine Smooth Muscle ◽  
Toxin Receptor ◽  
Anthrax Toxin Receptor 2

Telokin expression and the effect of hypoxia on its phosphorylation status in smooth muscle cells from small and large pulmonary arteries

2008 ◽  
Vol 294 (6) ◽  
pp. L1166-L1173 ◽  
Author(s):  
Jane A. Madden ◽  
Mark W. Dantuma ◽  
Elena A. Sorokina ◽  
Dorothee Weihrauch ◽  
Jack G. Kleinman
Keyword(s):  
Smooth Muscle ◽  
Muscle Cell ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Muscle Relaxation ◽  
Cerebral Arteries ◽  
Pulmonary Arteries ◽  
Smooth Muscle Relaxation ◽  
Myosin Phosphatase ◽  
Mlc Phosphorylation

Small pulmonary arteries (SPA), <500 μm diameter of the cat, constrict when exposed to hypoxia, whereas larger arteries (large pulmonary arteries; LPA), >800 μm diameter, show little or no response. It is unknown why different contractile responses occur within the same vascular bed, but activator or repressor proteins within the smooth muscle cell (SMC) can modify myosin phosphatase and myosin light chain kinase (MLCK), thereby influencing the phosphorylation state of myosin light chain (MLC) and ultimately, contraction. Telokin, a protein with a sequence identical to the COOH-terminal domain of MLCK, is expressed in smooth muscle where in its phosphorylated state it inhibits myosin phosphatase, binds to unphosphorylated myosin, and helps maintain smooth muscle relaxation. We measured telokin mRNA and telokin protein in smooth muscle from different diameter feline pulmonary arteries and sought to determine whether changes in the phosphorylation status of telokin and MLC occurred during hypoxia. In pulmonary arteries, telokin expression varied inversely with artery diameter, but cerebral arteries showed neither telokin protein nor telokin mRNA. Although telokin and MLC were distributed uniformly throughout the SPA muscle cell cytoplasm, they were not colocalized. During hypoxia, telokin dephosphorylated, and MLC became increasingly phosphorylated in SPA SMC, whereas in LPA SMC there was no change in either telokin or MLC phosphorylation. When LPA SMC were exposed to phenylephrine, MLC phosphorylation increased with no change in telokin phosphorylation. These results suggest that in SPA, phosphorylated telokin may help maintain relaxation under unstimulated conditions, whereas in LPA, telokin's function remains undetermined.

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