scholarly journals An active finite viscoelastic model for gastric smooth muscle contraction

2021 ◽  
Author(s):  
Satish Kumar Panda ◽  
Martin Lindsay Buist
Keyword(s):  
Smooth Muscle ◽  
Cell Model ◽  
Viscoelastic Model ◽  
Interaction Model ◽  
Smooth Muscle Contraction ◽  
Gastric Smooth Muscle ◽  
Proposed Model ◽  
Myosin Interaction ◽  
Stress And Deformation ◽  
Viscoelastic Constitutive Model

AbstractA coupled electromechanical model to describe the transduction process of cellular electrical activity into mechanical deformation has been presented. The model consolidates a biophysical smooth muscle cell model, a biophysical actin-myosin interaction model, a sliding filament model and a viscoelastic constitutive model to construct an active finite viscoelastic model. The key input to this model is an electrical pulse which then estimates the resulting stress and deformation in the cell. The proposed model was used to recreate experimental observations performed on canine and porcine gastric tissue strips. In all cases, the simulation results were well matched with the experimental data (R2> 0.9).

Subcellular Ca2+ Mobilization in Gastric Smooth Muscle Contraction

2002 ◽  
Vol 43 (1) ◽  
pp. 101
Author(s):  
Kwang Soo Kim ◽  
Nam Sik Woo ◽  
Ye Chul Lee ◽  
Bo Kyung Kim ◽  
Jung Hwan Kim ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Gastric Smooth Muscle

Effects of cholecystokinin-octapeptide on gastric motility of anesthetized dogs

1986 ◽  
Vol 251 (5) ◽  
pp. G678-G681 ◽  
Author(s):  
A. Kuwahara ◽  
K. Ozawa ◽  
N. Yanaihara
Keyword(s):  
Smooth Muscle ◽  
Gastric Motility ◽  
Contractile Response ◽  
Smooth Muscle Contraction ◽  
Dependent Manner ◽  
Local Effects ◽  
Cholecystokinin Octapeptide ◽  
Gastric Smooth Muscle ◽  
Anesthetized Dogs ◽  
Dose Dependent

The present experiments examined the local effects of cholecystokinin-octapeptide (CCK-8) and related peptides on gastric motility of anesthetized dogs. Peptides were injected through the gastroepiploic artery at doses of 1.0, 2.5, 5.0, 10.0, and 20.0 ng/ml. CCK-8 and its analogues (Glt-CCK-8, pGlu-CCK-8, and Suc1-MePhe8-CCK-7) increased gastric smooth muscle contraction in a dose-dependent manner. ED50 of CCK-8 was 2.97 +/- 0.63 ng/ml. Administration of atropine (100–200 micrograms/kg) inhibited the effects of both CCK-8 and pentagastrin; however, hexamethonium (5 mg/kg) failed to block the contractile response induced by CCK-8 and pentagastrin. These results indicate that CCK-8 and related peptides can act as local modulators in controlling the neural regulation of gastric motility.

scholarly journals Features of the bradykinin-induced contraction of the gastric smooth muscle depending on the concentration of compounds based on 3-substituted-1,4-benzodiazepin-2-ones

2016 ◽  
Vol 21 (2) ◽  
pp. 19-23
Author(s):  
P. Virych ◽  
O. Shelyuk ◽  
V. Martynyuk ◽  
V. Pavlovsky
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Contractile Activity ◽  
Smooth Muscles ◽  
Competitive Inhibitor ◽  
Smooth Muscle Contraction ◽  
Gastric Smooth Muscle ◽  
Low Concentrations

The effect of compounds based on 3-substituted-1,4-benzodiazepine-2-ones on contractile activity of smooth muscles of the rat's stomach was analyzed. Action substances MX-1626, MX-1775 for the smooth muscle contraction of like competitive inhibitor of bradykinin – des-Arg9- [Leu8]-Bradykinin acetate, which is observed as increase normalized rate of contraction with increasing of bradykinin concentration and characterized by a slowdown in the first phase of contraction. The most effective 3-subtituted 1,4-benzodiazepin-2-ones was at low concentrations of bradykinin, increasing it concentration their effect is reduced.

scholarly journals Mfge8 attenuates human gastric antrum smooth muscle contractions

2020 ◽  
Author(s):  
Wen Li ◽  
Ashley Olseen ◽  
Yeming Xie ◽  
Cristina Alexandru ◽  
Brian A. Perrino
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Milk Fat ◽  
Smooth Muscles ◽  
Smooth Muscle Contraction ◽  
Gastric Antrum ◽  
Mechanical Responses ◽  
Gastric Smooth Muscle ◽  
Milk Fat Globule ◽  
Smooth Muscle Contractions

AbstractCoordinated gastric smooth muscle contraction is critical for proper digestion and is adversely affected by a number of gastric motility disorders. In this study we report that the secreted protein Mfge8 (milk fat globule-EGF factor 8) inhibits the contractile responses of human gastric antrum muscles to cholinergic stimuli by reducing the inhibitory phosphorylation of the MYPT1 (myosin phosphatase-targeting subunit 1) subunit of MLCP (myosin light chain phosphatase), resulting in reduced LC20 (smooth muscle myosin regulatory light chain 2) phosphorylation. We show that endogenous Mfge8 is bound to its receptor, α8β1 integrin, in human gastric antrum muscles, suggesting that human gastric antrum muscle mechanical responses are regulated by Mfge8. The regulation of gastric antrum smooth muscles by Mfge8 and α8 integrin functions as a brake on gastric antrum mechanical activities. Further studies of the role of Mfge8 and α8 integrin in regulating gastric antrum function will likely reveal additional novel aspects of gastric smooth muscle motility mechanisms.

HSP27 phosphorylation and interaction with actin-myosin in smooth muscle contraction

2002 ◽  
Vol 282 (5) ◽  
pp. G894-G903 ◽  
Author(s):  
Khalil N. Bitar
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Signal Transduction Pathway ◽  
Muscle Cells ◽  
Smooth Muscle Contraction ◽  
Thin Filament Regulation ◽  
Kinase C ◽  
Hsp27 Phosphorylation ◽  
Myosin Interaction

We have investigated the role of heat shock protein 27 (HSP27) phosphorylation and the association of HSP27 with contractile proteins actin, myosin, and tropomyosin. Smooth muscle cells were labeled with [32P]orthophosphate. C2-ceramide (0.1 μM), an activator of protein kinase C (PKC), induced a sustained increase in HSP27 phosphorylation that was inhibited by calphostin C. C2-ceramide-induced (0.1 μM) sustained colonic smooth muscle cell contraction was accompanied by significant increases in the association of HSP27 with tropomyosin and in the association of HSP27 with actin. The significant increases occurred at 30 s after stimulation and were sustained at 4 min. Contraction was also associated with strong colocalization of HSP27 with tropomyosin and with actin as observed after immunofluorescent labeling of tropomyosin, actin, and HSP27 followed by confocal microscopy. Transfection of smooth muscle cells with HSP27 phosphorylation mutants indicated that phosphorylation of HSP27 could affect myosin association with actin. In conclusion 1) HSP27 phosphorylation appears to be necessary for reorganization of HSP27 inside the cell and seems to be directly correlated with the PKC signal transduction pathway, and 2) agonist-induced phosphorylation of HSP27 modulates actin-myosin interaction through thin-filament regulation of tropomyosin.

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