Stanislawski L, De Nechaud B, Christel P
Laboratoire de Recherches Orthopédiques, Faculté de Médecine, Lariboisière-Saint Louis, Paris, France.
J Biomed Mater Res. 1995 Mar;29(3):315-23. doi: 10.1002/jbm.820290306.
The adsorption of plasma proteins onto biomedical polymers is an important factor in the biocompatibility of biomaterials. We identified the plasma proteins adsorbed onto four polymeric fibers used for synthetic ligament replacement: polyarylamide, polylactic acid, polyester, and polypropylene. The adsorbed proteins were eluted and analyzed by one-dimensional and two-dimensional gel electrophoresis. Fibrinogen, albumin, IgG, high molecular weight kininogen (HMWK), and lipoproteins ApoA-1 and ApoE were the major proteins adsorbed onto polyarylamide. The three others biomaterials bound albumin, fibrinogen, ApoA-1, and ApoE; however, the proportions of proteins bound to each polymer differed. There was an inverse relationship between ApoA-1 and fibrinogen binding for all four biomaterials; polyarylamide bound a high percentage of fibrinogen, but little ApoA-1; polylactic acid, polyester, and polypropylene bound a high percentage of ApoA-1, but little fibrinogen. These results support suggestions that low fibrinogen adsorption might be due to the preferential adsorption of Apo-1. High fibrinogen binding to polyarylamide ligaments may favor fibroblast adherence, growth, and tissue repair.
