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Noelle Koo

Biochemical Mechanisms and Capabilities of Follistatin-like protein 1 (part 1)




Written by: Noelle A. Koo (12th grade / Ashburn, VA USA)


In a study conducted in 2008, the biochemical mechanisms and molecular functions of protein FSTL1 were explored through the study of the function of FSTL1 in muscle tissue and endothelial cell function. Researchers in the study focused on the role of FSTL1 in the regulation of endothelial cell function and blood vessel growth in muscle through an endothelial cell culture in order to further the understanding of molecular functions and microscopic pathways, signaling, and expressions present which facilitates the role of FSTL1 in endothelial cells and muscle tissue (Ouchi et al., 2008).


Through the study, researchers discovered that ad-FSTL1 stimulated migration and differentiation into network structures that inhibited apoptosis under conditions of serum deprivation (Ouchi et al., 2008). In simpler terms, they discovered that the ad-FSTL1 ultimately inhibited cell death, thereby protecting the cells from injury and promoting endothelial cell function. It was further discovered that the cell responses were associated with the activating phosphorylation of Akt, a serine/threonine-specific protein kinase that plays an important role in many cellular processes like cell proliferation, metabolism of glucose, apoptosis, transcription, etc., and eNOS (endothelial NOS), an enzyme that functions to catalyze the production of nitric oxide (NO) from L-arginine.

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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