ArticleNeurogastroenterology and motility2012
Decreased myosin phosphatase target subunit 1(MYPT1) phosphorylation via attenuated rho kinase and zipper-interacting kinase activities in edematous intestinal smooth muscle.
Article in Neurogastroenterology and motility, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- MLC2: Physiological Functions and Potential Roles in Tumorigenesis.Cell biochemistry and biophysics · 2025Review
- Stretch-Induced Down-Regulation of HCN2 Suppresses Contractile Activity.Molecules (Basel, Switzerland) · 2023Article
- Mechanosensing in the Physiology and Pathology of the Gastrointestinal Tract.International journal of molecular sciences · 2022Review
- Mechanotransduction at the Plasma Membrane-Cytoskeleton Interface.International journal of molecular sciences · 2021Review
- Early-life malnutrition causes gastrointestinal dysmotility that is sexually dimorphic.Neurogastroenterology and motility · 2020Article
- Postoperative Ileus and Postoperative Gastrointestinal Tract Dysfunction: Pathogenic Mechanisms and Novel Treatment Strategies Beyond Colorectal Enhanced Recovery After Surgery Protocols.Frontiers in pharmacology · 2020Review
- ZIPK mediates endothelial cell contraction through myosin light chain phosphorylation and is required for ischemic-reperfusion injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Ameliorative effect of melatonin against increased intestinal permeability in diabetic rats: possible involvement of MLCK-dependent MLC phosphorylation.Molecular and cellular biochemistry · 2016Article
- Suppression of contractile activity in the small intestine by indomethacin and omeprazole.American journal of physiology. Gastrointestinal and liver physiology · 2015Article
- Biphasic regulation of myosin light chain phosphorylation by p21-activated kinase modulates intestinal smooth muscle contractility.The Journal of biological chemistry · 2013Article
- The vasorelaxant mechanisms of a Rho kinase inhibitor DL0805 in rat thoracic aorta.Molecules (Basel, Switzerland) · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
backgroundIntestinal edema development after trauma resuscitation inhibits intestinal motility which results in ileus, preventing enteral feeding and compromising patient outcome. We have shown previously that decreased intestinal motility is associated with decreased smooth muscle myosin light chain (MLC) phosphorylation. The purpose of the present study was to investigate the mechanism of edema-induced decreases in MLC in a rodent model of intestinal edema.
methodsIntestinal edema was induced by a combination of resuscitation fluid administration and mesenteric venous hypertension. Sham operated animals served as controls. Contractile activity and alterations in the regulation of MLC including the regulation of MLC kinase (MLCK) and MLC phosphatase (MLCP) were measured. KEY
resultsContraction amplitude and basal tone were significantly decreased in edematous intestinal smooth muscle compared with non-edematous tissue. Calcium sensitivity was also decreased in edematous tissue compared with non-edematous intestinal smooth muscle. Although inhibition of MLCK decreased contractile activity significantly less in edematous tissue compared with non-edematous tissue, MLCK activity in tissue lysates was not significantly different. Phosphorylation of MYPT was significantly lower in edematous tissue compared with non-edematous tissue. In addition, activities of both rho kinase and zipper-interacting kinase were significantly lower in edematous tissue. CONCLUSIONS & INFERENCES: We conclude from these data that interstitial intestinal edema inhibits MLC phosphorylation predominantly by decreasing inhibitory phosphorylation of the MLC targeting subunit (MYPT1) of MLC phosphatase via decreased ROCK and ZIPK activities, resulting in more MLC phosphatase activity.
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