Abstract
Leukocyte-platelet rich fibrin (L-PRF) is extensively used in the dentistry field and other clinical scenarios due to its regeneration properties. The goal of the present study was to depict the L-PRF secretome and how it changes over time. We obtained L-PRF membranes and cultured them in DMEM. The secretome was collected at days 3, 7 and 21. The secretome at day 3 was analysed by LC–MS/MS and differences over time were analysed by Sequential Window Acquisition of all Theoretical Mass Spectra (SWATH). Overall, 705 proteins were identified in the secretome of L-PRF membranes after 3 days of culture, including growth factors (EGF, PDGFA) and proteins related to platelet and neutrophil degranulation. A total of 202 differentially secreted proteins were quantified by SWATH when comparing secretomes at days 3, 7 and 21. Most of them were enriched at day 3 such as MMP9, TSP1 and CO3. On the contrary, fibrinogen and CATS were found down-regulated at day 3. Growth factor and western blotting analysis corroborated the proteomic results. This is the most detailed proteome analysis of the L-PRF secretome to date. Proteins and growth factors identified, and their kinetics, provide novel information to further understand the wound healing properties of L-PRF.
Highlights
Leukocyte-platelet rich fibrin (L-PRF) is extensively used in the dentistry field and other clinical scenarios due to its regeneration properties
In 2001, Choukroun et al developed the second generation of platelet-rich concentrates (PRC), Leukocyte platelet rich fibrin (L-PRF)[1], which is obtained by blood centrifugation without anticoagulant in the tubes
Due to their blood origin, membranes were washed twice in the first 24 h in order to eliminate the majority of plasma proteins, which could interfere with the identifications of less abundant proteins present in the secretome
Summary
Leukocyte-platelet rich fibrin (L-PRF) is extensively used in the dentistry field and other clinical scenarios due to its regeneration properties. 705 proteins were identified in the secretome of L-PRF membranes after 3 days of culture, including growth factors (EGF, PDGFA) and proteins related to platelet and neutrophil degranulation. Differences in the study design and the types of samples analysed did not allow knowing the protein composition of the PRC releasate, in the case of L-PRF. For this reason, it is important to obtain an overall picture of L-PRF releasate protein composition in order to better understand the impact of the L-PRF in wound healing. Our aim was to identify the proteins released by L-PRF membranes cultured in vitro and differences depending on the incubation time, which could reassemble what happens during the time of treatment with L-PRF in vivo
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