Platelet-rich fibrin（PRF）：a second-generation platelet concentrate. Part II：Platelet-related biologic features.
Dohan DM, Choukroun J, Diss A, Dohan SL, Dohan AJ, Mouhyi J, Gogly B.
Oral Surg Oral Med Oral Pathol Oral Radiol Endod. 2006 Mar;101(3):e45-50. Epub 2006 Jan 10.
Oral Surgery, Oral Medicine, Oral Pathology, Oral Radiology, and Endodontology Volume 101, Issue 3, March 2006, Pages e45–e50
Source
Biophysics Laboratory, Faculty of Dental Surgery, University of Paris V, Paris, France. drdohand@hotmail.com
http://www.sciencedirect.com/science/article/pii/S1079210405005871
Abstract
Platelet-rich fibrin (PRF) belongs to a new generation of platelet concentrates, with simplified processing and without biochemical blood handling. In this second article, we investigate the platelet-associated features of this biomaterial. During PRF processing by centrifugation, platelets are activated and their massive degranulation implies a very significant cytokine release. Concentrated platelet-rich plasma platelet cytokines have already been quantified in many technologic configurations. To carry out a comparative study, we therefore undertook to quantify PDGF-BB, TGFbeta-1, and IGF-I within PPP（platelet-poor plasma）supernatant and PRF clot exudate serum. These initial analyses revealed that slow fibrin polymerization during PRF processing leads to the intrinsic incorporation of platelet cytokines and glycanic chains in the fibrin meshes. This result would imply that PRF, unlike the other platelet concentrates, would be able to progressively release Cytokines during Fibrin matrix remodeling; such a mechanism might explain the clinically observed healing properties of PRF.
Fig. 1. The lower part of the PRF fibrin matrix is occupied by whitish streaks looking like cell fragment aggregates on histological sections. These are the platelet accumulations and constitute a “buffy coat” (A). But there is no platelet or any other cellular body in the upper part of the PRF fibrin clot (B). Hemalun-eosin staining, 52×.
Fig. 2. The PRF fibrin clot obtained according to the Process protocol is divided into 3 parts: a red thrombus in contact with the red blood corpuscle base, an acellular fibrin gel, and a network of buffy columns corresponding to platelet accumulation.
Fig. 3. Glycanic chain distribution within PRF fibrin clot (pH 1 alcian blue staining, 52×).
Fig. 4. Schematic representation of the 3 centrifugation strata obtained after PRF processing according to Process official protocol.
Fig. 5. PDGF-BB ELISA quantifications.
Fig. 6. TGFβ-1 ELISA quantifications.
Fig. 7. IGF-1 ELISA quantifications.
Fig. 8. Theoretical computer modeling of a fibrin network resulting from fibrin glue polymerization. Note that in adhesives such as Tisseel, fibronectin is trapped in the matricial meshes (not represented here) (D-TEP v1.3).
Fig. 9. Theoretical computer modeling of a fibrin network resulting from a cPRP polymerization. The activated platelets are trapped in the fibrin meshes and release a significant quantity of cytokines extrinsically retained in the fibrin architecture (D-TEP v1.3; scales not respected). (1) Platelet trapped in the fibrin gel. (2) Platelet cytokine in solution (extrinsic).
Fig. 10. Theoretical computer modeling of a PRF clot. Note the presence of structural glycoproteins (fibronectin) and extrinsic cytokines (in solution) enmeshed in the fibrin matrix. The PRF slow polymerization process would also allow the intrinsic retaining of glycanic chains and cytokines within fibrin polymers. PRF would be thus very close to a natural fibrin thrombus (D-TEP v1.3; scales not respected). (1) Cytokine intrinsically retained within fibrin fibrillae. (2) Platelet cytokine in solution (extrinsically associated with fibrin polymers). (3) Fibrin-associated glycanic chains. (4) Circulating glycoproteins (fibronectin). (5) Fibrin fibrilla associated with glycanic chains and intrinsic cytokines.
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