Myofibroblasts are contractile cells found in multiple tissues. They are physiological cells as in the human placenta and can be obtained from bone marrow mesenchymal stem cells after differentiation by transforming growth factor-β (TGF-β). They are also found in the stroma of cancerous tissues and can be located in non-muscle contractile tissues. When stimulated by an electric current or after exposure to KCl, these tissues contract. They relax either by lowering the intracellular Ca concentration (by means of isosorbide dinitrate or sildenafil) or by inhibiting actin-myosin interactions (by means of 2,3-butanedione monoxime or blebbistatin). Their shortening velocity and their developed tension are dramatically low compared to those of muscles. Like sarcomeric and smooth muscles, they obey Frank-Starling's law and exhibit the Hill hyperbolic tension-velocity relationship. The molecular motor of the myofibroblast is the non-muscle myosin type IIA (NMIIA). Its essential characteristic is the extreme slowness of its molecular kinetics. In contrast, NMIIA develops a unitary force similar to that of muscle myosins. From a thermodynamic point of view, non-muscle contractile tissues containing NMIIA operate extremely close to equilibrium in a linear stationary mode.
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http://dx.doi.org/10.3390/ijms22147738 | DOI Listing |
Cells
December 2024
Department of Biological Sciences, Wayne State University, Detroit, MI 48202, USA.
The myosin light chains (MLCs) of non-muscle myosin II are known to regulate cellular architecture and generate cellular forces; they also have an increasingly emerging role in the progression of cancer. The phosphorylation state of the myosin light chains controls the activity of myosins that are implicated in invasion and proliferation. In cancers, when proliferation is greatly increased, cytokinesis relies on phosphorylated light chains to activate the contractile forces used to separate the cells.
View Article and Find Full Text PDFFront Cell Dev Biol
October 2024
Department of Biology, Northeastern University, Boston, MA, United States.
bioRxiv
September 2024
Northeastern University, Department of Biology, Boston, MA 02115.
bioRxiv
August 2024
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
The non-muscle actomyosin cytoskeleton generates contractile force through the dynamic rearrangement of its constituent parts. Actomyosin rings are a specialization of the non-muscle actomyosin cytoskeleton that drive cell shape changes during division, wound healing, and other events. Contractile rings throughout phylogeny and in a range of cellular contexts are built from conserved components including non-muscle myosin II (NMMII), actin filaments (F-actin), and crosslinking proteins.
View Article and Find Full Text PDFTransl Psychiatry
August 2024
Brain Plasticity Unit, ESPCI Paris, PSL Research University, CNRS, Paris, France.
Long-term synaptic plasticity is critical for adaptive function of the brain, but presynaptic mechanisms of functional plasticity remain poorly understood. Here, we show that changes in synaptic efficacy induced by activation of the cannabinoid type-1 receptor (CBR), one of the most widespread G-protein coupled receptors in the brain, requires contractility of the neuronal actomyosin cytoskeleton. Specifically, using a synaptophysin-pHluorin probe (sypH2), we show that inhibitors of non-muscle myosin II (NMII) ATPase as well as one of its upstream effectors Rho-associated kinase (ROCK) prevent the reduction of synaptic vesicle release induced by CBR activation.
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