Profilin-1 binds to actin monomers (G-actin) and catalyzes the exchange of ADP for ATP on actin, which is a critical step in actin polymerization . This interaction is vital for the formation of actin filaments (F-actin), which are necessary for maintaining cell shape, enabling cell movement, and facilitating intracellular transport . Additionally, Profilin-1 interacts with other proteins such as phosphoinositide lipids and formins, further influencing actin dynamics and microtubule assembly .
Recombinant Profilin-1 refers to the protein that has been genetically engineered and produced in a laboratory setting. This recombinant form is used extensively in research to study its functions and interactions within cells. By using recombinant Profilin-1, scientists can investigate its role in various cellular processes and its involvement in diseases.
Profilin-1 has been implicated in several pathological conditions. For instance, its levels are increased in the vascular endothelium under pathological conditions such as diabetes . Overexpression of Profilin-1 has been shown to trigger indicators of endothelial dysfunction downstream of LDL signaling, contributing to atherosclerosis . Studies have demonstrated that recombinant Profilin-1 can induce atherogenic effects on vascular smooth muscle cells (VSMCs), such as DNA synthesis and chemotaxis . Elevated serum levels of Profilin-1 have also been correlated with the degree of atherosclerosis in humans .
Recombinant Profilin-1 is a valuable tool in biochemical and cell biology research. It allows scientists to visualize and study the dynamic interactions of Profilin-1 with actin and microtubules in vitro and in live cells . Fluorescently tagged versions of Profilin-1 have been developed to study its cellular dynamics and interactions with different components of the cytoskeleton . These tools are particularly useful for understanding the consequences of different mutations and for investigating the role of Profilin-1 in various cellular processes and disease states .