Contraction of myofibroblasts in granulation tissue is dependent on Rho/Rho kinase/myosin light chain phosphatase activity
ABSTRACT During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force generating myofibroblasts. We examined whether regulation of myofibroblast contraction in granulation tissue is dominated by Ca2+‐induced phos...
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| Published in | Wound repair and regeneration Vol. 14; no. 3; pp. 313 - 320 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Malden, USA
Blackwell Publishing Inc
01.05.2006
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| Subjects | |
| Online Access | Get full text |
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| Abstract | ABSTRACT
During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force generating myofibroblasts. We examined whether regulation of myofibroblast contraction in granulation tissue is dominated by Ca2+‐induced phosphorylation of myosin light chain kinase or by Rho/Rho kinase (ROCK)‐mediated inhibition of myosin light chain phosphatase, similar to that of cultured myofibroblasts. Strips of granulation tissue obtained from rat granuloma pouches were stimulated with endothelin‐1 (ET‐1), serotonin, and angiotensin‐II and isometric force generation was measured. We here investigated ET‐1 in depth, because it was the only agonist that produced a long‐lasting and strong response. The ROCK inhibitor Y27632 completely inhibited ET‐1–promoted contraction and the phosphatase inhibitor calyculin elicited contraction in the absence of any other agonists, suggesting that activation of the Rho/ROCK/myosn light chain phosphatase pathway is critical in regulating in vivo myofibroblast contraction. Membrane depolarization with K+ also stimulated a long‐lasting contraction of granulation tissue; however, the amount of force generated was significantly less compared to ET‐1. Moreover, K+‐induced contraction was inhibited by Y27632. These results are consistent with inhibition of myosin light chain phosphatase by the Rho/ROCK signaling pathway, which would account for the long‐duration contraction of myofibroblasts necessary for wound closure. |
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| AbstractList | ABSTRACT
During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force generating myofibroblasts. We examined whether regulation of myofibroblast contraction in granulation tissue is dominated by Ca2+‐induced phosphorylation of myosin light chain kinase or by Rho/Rho kinase (ROCK)‐mediated inhibition of myosin light chain phosphatase, similar to that of cultured myofibroblasts. Strips of granulation tissue obtained from rat granuloma pouches were stimulated with endothelin‐1 (ET‐1), serotonin, and angiotensin‐II and isometric force generation was measured. We here investigated ET‐1 in depth, because it was the only agonist that produced a long‐lasting and strong response. The ROCK inhibitor Y27632 completely inhibited ET‐1–promoted contraction and the phosphatase inhibitor calyculin elicited contraction in the absence of any other agonists, suggesting that activation of the Rho/ROCK/myosn light chain phosphatase pathway is critical in regulating in vivo myofibroblast contraction. Membrane depolarization with K+ also stimulated a long‐lasting contraction of granulation tissue; however, the amount of force generated was significantly less compared to ET‐1. Moreover, K+‐induced contraction was inhibited by Y27632. These results are consistent with inhibition of myosin light chain phosphatase by the Rho/ROCK signaling pathway, which would account for the long‐duration contraction of myofibroblasts necessary for wound closure. During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell-like phenotype by differentiating into contractile force generating myofibroblasts. We examined whether regulation of myofibroblast contraction in granulation tissue is dominated by Ca2+-induced phosphorylation of myosin light chain kinase or by Rho/Rho kinase (ROCK)-mediated inhibition of myosin light chain phosphatase, similar to that of cultured myofibroblasts. Strips of granulation tissue obtained from rat granuloma pouches were stimulated with endothelin-1 (ET-1), serotonin, and angiotensin-II and isometric force generation was measured. We here investigated ET-1 in depth, because it was the only agonist that produced a long-lasting and strong response. The ROCK inhibitor Y27632 completely inhibited ET-1-promoted contraction and the phosphatase inhibitor calyculin elicited contraction in the absence of any other agonists, suggesting that activation of the Rho/ROCK/myosn light chain phosphatase pathway is critical in regulating in vivo myofibroblast contraction. Membrane depolarization with K+ also stimulated a long-lasting contraction of granulation tissue; however, the amount of force generated was significantly less compared to ET-1. Moreover, K+-induced contraction was inhibited by Y27632. These results are consistent with inhibition of myosin light chain phosphatase by the Rho/ROCK signaling pathway, which would account for the long-duration contraction of myofibroblasts necessary for wound closure. During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force generating myofibroblasts. We examined whether regulation of myofibroblast contraction in granulation tissue is dominated by Ca 2+ ‐induced phosphorylation of myosin light chain kinase or by Rho/Rho kinase (ROCK)‐mediated inhibition of myosin light chain phosphatase, similar to that of cultured myofibroblasts. Strips of granulation tissue obtained from rat granuloma pouches were stimulated with endothelin‐1 (ET‐1), serotonin, and angiotensin‐II and isometric force generation was measured. We here investigated ET‐1 in depth, because it was the only agonist that produced a long‐lasting and strong response. The ROCK inhibitor Y27632 completely inhibited ET‐1–promoted contraction and the phosphatase inhibitor calyculin elicited contraction in the absence of any other agonists, suggesting that activation of the Rho/ROCK/myosn light chain phosphatase pathway is critical in regulating in vivo myofibroblast contraction. Membrane depolarization with K + also stimulated a long‐lasting contraction of granulation tissue; however, the amount of force generated was significantly less compared to ET‐1. Moreover, K + ‐induced contraction was inhibited by Y27632. These results are consistent with inhibition of myosin light chain phosphatase by the Rho/ROCK signaling pathway, which would account for the long‐duration contraction of myofibroblasts necessary for wound closure. |
| Author | Tomasek, James J. Hinz, Boris Vaughan, Melville B. Kropp, Bradley P. Martin, Michael D. Haaksma, Carol J. Gabbiani, Giulio |
| Author_xml | – sequence: 1 givenname: James J. surname: Tomasek fullname: Tomasek, James J. organization: Department of Cell Biology – sequence: 2 givenname: Melville B. surname: Vaughan fullname: Vaughan, Melville B. organization: Department of Cell Biology – sequence: 3 givenname: Bradley P. surname: Kropp fullname: Kropp, Bradley P. organization: Department of Urology, University of Oklahoma-Health Sciences Center, Oklahoma City, Oklahoma – sequence: 4 givenname: Giulio surname: Gabbiani fullname: Gabbiani, Giulio organization: Department of Pathology, Centre Medical Universitaire, University of Geneva, Geneva, Switzerland, and – sequence: 5 givenname: Michael D. surname: Martin fullname: Martin, Michael D. organization: Department of Cell Biology – sequence: 6 givenname: Carol J. surname: Haaksma fullname: Haaksma, Carol J. organization: Department of Cell Biology – sequence: 7 givenname: Boris surname: Hinz fullname: Hinz, Boris organization: Laboratory of Cell Biophysics, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16808810$$D View this record in MEDLINE/PubMed |
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| Notes | ArticleID:WRR126 ark:/67375/WNG-LRGCR0GC-Z istex:7F90CD593DB2ADB9EF00F53D1E1F5688C471F4C2 † * Current address: Department of Neurosurgery, University of Oklahoma‐Health Sciences Center, Oklahoma City, OK. Current address: Department of Biology, University of Central Oklahoma, Edmond, OK. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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| Snippet | ABSTRACT
During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force... During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell-like phenotype by differentiating into contractile force generating... During wound healing and fibrocontractive diseases fibroblasts acquire a smooth muscle cell‐like phenotype by differentiating into contractile force generating... |
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| SubjectTerms | Amides - pharmacology Animals Endothelin-1 - pharmacology Enzyme Inhibitors - pharmacology Fibroblasts - enzymology Fibroblasts - physiology Granulation Tissue - enzymology Granulation Tissue - pathology Granulation Tissue - physiopathology Intracellular Signaling Peptides and Proteins - antagonists & inhibitors Intracellular Signaling Peptides and Proteins - metabolism Isometric Contraction - drug effects Male Muscle, Smooth - cytology Myosin-Light-Chain Phosphatase - antagonists & inhibitors Myosin-Light-Chain Phosphatase - metabolism Protein Kinase Inhibitors - pharmacology Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - metabolism Pyridines - pharmacology Rats Rats, Sprague-Dawley rho-Associated Kinases Signal Transduction Wound Healing - physiology |
| Title | Contraction of myofibroblasts in granulation tissue is dependent on Rho/Rho kinase/myosin light chain phosphatase activity |
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