Written by: Noelle A. Koo (12th grade / Ashburn, VA USA)
The discovery of the impact that FSTL1 had on the cell responses involving activating phosphorylation of eNOS was quite significant, as the production of nitric oxide has previously been found to be an important factor as it functions as a cellular signaling molecule and helps with various processes like insulin secretion, modulating vascular tone, and more. It was also discovered that FSTL1 was upregulated in myocardium in cardiac-specific Akt1 transgenic (TG) mice, having anti-apoptotic actions in cardiac myocytes, which supports many of the recent findings that FSTL1 functions as a cardioprotective molecule.
Results of the study indicated that FSTL1 was a secreted factor in myogenic cells that favored ischemia-induced revascularization through the activation of Akt-eNOS-dependent signaling within endothelial cells (Ouchi et al., 2008). Ultimately, the activation of the Akt-eNOS dependent signaling enabled the FSTL1 to be secreted in myogenic cells and helped revascularization after ischemic injury. Results determined from the study supports the findings that FSTL1 expression was significantly heightened in the presence of ischemic injury in heart tissue and in ischemic muscle - specifically ischemic adductor muscle following femoral artery excision.
It was concluded that the FSTL1 contributed to the promotion of the formation of network structures in endothelial cell function and this led to the promotion of the cell function and greater survival rates in-vitro. This research shed light on the molecular mechanisms and properties of FSTL1, allowing for further understanding of the microscopic functions that promote and stimulate proliferation in certain cell types.
Paper Citation:
Ouchi, N., Oshima, Y., Ohashi, K., Higuchi, A., Ikegami, C., Izumiya, Y., & Walsh, K. (2008). Follistatin-like 1, a secreted muscle protein, promotes endothelial cell function and revascularization in ischemic tissue through a nitric-oxide synthase-dependent mechanism. The Journal of biological chemistry, 283(47), 32802–32811. https://doi.org/10.1074/jbc.M803440200
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