Abstract
Statement of the Problem: Platelet-rich plasma (PRP), produced from autologous blood is currently used as an adjunct to bone grafting. Platelets are enriched by centrifugation and clotted with bovine thrombin, which has been associated with the development of antibodies to clotting factors V, XI, and thrombin, resulting in the risk of life-threatening coagulopathies. Thrombin causes significant shrinkage of PRP, raising concern about graft adaptation as well as the potential loss of growth factors from the graft composite. Thrombin signaling of platelets is mediated by a G protein-coupled protease-activated receptor (PAR) which is activated after thrombin binding. The amino terminal end of PAR is cleaved resulting in a new amino terminus which acts as a tethered ligand and binds intramolecularly to the body of the PAR, causing a transmembrane signal. Synthetic peptides such as thrombin receptor activator peptide-6 (TRAP) activate the receptor independent of receptor cleavage. In this report we evaluate the potential of TRAP and TRAP/bone substitutes in minimizing clot retraction and promoting maximum graft adaptation.
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