| First Author | Tomasek JJ | Year | 2013 |
| Journal | Wound Repair Regen | Volume | 21 |
| Issue | 1 | Pages | 166-76 |
| PubMed ID | 23253249 | Mgi Jnum | J:315510 |
| Mgi Id | MGI:6829123 | Doi | 10.1111/wrr.12001 |
| Citation | Tomasek JJ, et al. (2013) Whole animal knockout of smooth muscle alpha-actin does not alter excisional wound healing or the fibroblast-to-myofibroblast transition. Wound Repair Regen 21(1):166-76 |
| abstractText | The contractile phenotype and function of myofibroblasts have been proposed to play a critical role in wound closure. It has been hypothesized that smooth muscle alpha-actin expressed in myofibroblasts is critical for its formation and function. We have used smooth muscle alpha-actin-null mice to test this hypothesis. Full-thickness excisional wounds closed at a similar rate in smooth muscle alpha-actin-null and wild-type mice. In addition, fibroblasts in smooth muscle alpha-actin-null granulation tissue when immunostained with a monoclonal antibody that recognizes all muscle actin isoforms exhibited a myofibroblast-like distribution and a stress fiber-like pattern, showing that these cells acquired the myofibroblast phenotype. Dermal fibroblasts from smooth muscle alpha-actin-null and wild-type mice formed stress fibers and supermature focal adhesions, and generated similar amounts of contractile force in response to transforming growth factor-beta1. Smooth muscle gamma-actin and skeletal muscle alpha-actin were expressed in smooth muscle alpha-actin-null myofibroblasts, as shown by immunostaining, real-time polymerase chain reaction, and mass spectrometry. These results show that smooth muscle alpha-actin is not necessary for myofibroblast formation and function and for wound closure, and that smooth muscle gamma-actin and skeletal muscle alpha-actin may be able to functionally compensate for the lack of smooth muscle alpha-actin in myofibroblasts. |
