Research: Profilin-1 (Pfn1) is an important protein involved with the dynamics of the actin cytoskeleton. Given its ubiquitous nature, various studies have linked Pfn1 to different elements of cardiovascular homeostasis such as angiogenesis, wound healing, and arteriosclerosis. It has recently been elucidated that Pfn1 is posttranslationally regulated through a serine phosphorylation via a phosphoinositide-3 kinase (PI3K)-dependent pathway. This regulation affects both Pfn1's ability to bind G-actin, downregulating actin polymerization rate, and Pfn1's ability to bind poly-L-proline (PLP), a key motif for many of Pfn1's binding partners. While the actin cytoskeleton and Pfn1 expression levels have been linked to different facets of the cardiovascular system, the role of post-translational control has yet to be elucidated. Mr. Veon's research focuses on how the post-translational regulation of Pfn1 impacts cardiovascular disease and repair. The default mechanism of healing for damaged / ischemic heart tissue in adult mammals is characterized by inflammation and the deposition of fibrous connective tissue with resultant scar tissue formation. No regeneration of functional myocardium can be expected. Studies have shown that placement of (acellular) extracellular matrix (ECM) scaffolds in experimentally created defects of the right ventricular and left ventricular wall can facilitate the constructive remodeling of myocardial tissue. Stated differently, The mechanisms by which such remodeling occurs is largely unknown, but has been shown to be associated with the recruitment of multipotential bone marrow-derived progenitor cells
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