IRREVERSIBLE ADSORPTION OF PROTEINS ON THE SURFACE OF MESHES FOR HERNIOPLASTY – FEATURES AND POTENTIAL ROLE IN BIOCOMPATIBILITY

DOI: https://doi.org/10.29296/24999490-2018-03-09

M.N. Milyakova(1), J.V. Ponomareva(1), A.V. Laykov(2), L.V. Limareva(1) 1-Samara State Medical University, Chapaevskaya str., 89, Samara, Russian Federation, 443099; 2-Kazan Federal University, Kremlevskaya str., 18, Kazan, Russian Federation, 420008 E-mail: [email protected]

Introduction. Interaction of prosthetic devices with surrounding tissues is based on protein absorption. Protein adsorption is the first stage of the interaction between prosthetic materials with tissues in the body. The number, composition, conformation changes of proteins bound to the prosthetic matrix determine the chemical composition, free energy, polarity of surface functional groups and hydrophilicity of the surface. The aim of the study. Proteomic analysis of proteins irreversibly adsorbed from human plasma on the surfaces of the meshes for hernioplasty. Methods. Plasma samples from patients with hernia were incubated with such matrixes as titanium, polypropylene or polyester with fluoropolymer coating meshes. Bound peptides were analyzed by electrophoresis. Qualitative analysis of the peptides extracted from the gel was performed by chromatography–mass spectrometry. Quantitative analysis was performed by the method of Multiple Reaction Monitoring. Results. Qualitative analysis identified more than 60 proteins. The results of the quantitative analysis showed fluoropolymer coated polyester to adsorb mainly following proteins: vitronectin (58,6±3,3%), albumin (11,4±2,2%), fibrinogen α – (10,5±1,8%), IgG (7,2±0,9%); Рolypropylene: albumin (21,4±9,1%), vitronectin (22,9±2,9%) and fibrinogen (24,2±3,8%), IgG (12,7±1,4%); Titan: vitronectin (85,7±3,1%), С1ѕ component of the complement system (7,8±2,2%), albumin (3,3±1,1%). Conclusion. Thus, vitronectin is able mostly irreversibly absorb on meshes with different characteristics. Perhaps vitronectin undergoes various conformational changes. These changes lead to peculiarities of reaction to a foreign body and the degree of fibrosis and opens the way for the establishment of molecular mechanisms of the development of сomplications and recurrence of hernias with the implantation of different materials.
Keywords: 
Hernia mesh, protein adsorption, biocompatibility, hernia

Список литературы: 
  1. Rastegarpour A., Cheung M., Vardhan M., Ibrahim M.M., Butler C.E., Levinson H. Surgical mesh for ventral incisional hernia repairs: Understanding mesh design. Plast Surg. 2016; 24 (1): 41–50.
  2. Carrillo-Conde B.R., Ramer-Tait A.E., Wannemuehler M.J., Narasimhan B. Acta Biomater. Chemistry-dependent adsorption of serum proteins onto polyanhydride microparticles differentially influences dendritic cell uptake and activation. Acta Biomater. 2012; 8 (10): 3618–28.
  3. Wang X., Schmidt D.R., Joyce E.J., Kao W.J. Application of MS- Based Proteomics to Study Serum Protein Adsorption/Absorption and Complement C3 Activation on Poly (ethylene glycol). J. Biomater Sci Polym Ed. 2011; 22 (10):1343–62.
  4. Szott L.M., Stein M.J., Ratner B.D., Horbett T.A. Complement activation on polyethylene oxide- like PFGD- deposited surfaces. J Biomed Mater Res A. 2011; 96 (1): 150–61.
  5. Bale M.D., Wohlfahrt L.A., Mosher D.F., Tomasini B.,Sutton R.C. Identification of Vitronectin as a Major Plasma Protein Adsorbed on Polymer Surfaces of Different Copolymer Composition. Blood. 1989; 74 (8): 2698–706.
  6. Cornelius R.M., Shankar S.P., Brash J.L., Babensee J.E. Immunoblot analysis of proteins associated with self-assembled monolayer surfaces of defined chemistries. J. Biomed Mater Res A. 2011; 98 (1): 7–18.
  7. Engberg A.E., Rosengren-Holmberg J.P., Chen H., Nilsson B., Lambris J.D., Nicholls I.A., Ekdahl K.N. Blood protein-polymer adsorption: Implications for understanding complement-mediated hemoincompatibility. J. Biomed Mater Res A. 2011; 97 (1): 74–84.
  8. Tsai I.Y., Tomczyk N., Eckmann J.I., Composto R.J., Eckmann D.M. Human plasma protein adsorption onto dextranized surfaces: a two-dimensional electroforesis and mass spectrometry study. Colloids Surf B Biointerfaces. 2011; 84 (1): 241–52.
  9. Nilsson B., Ekdahl K.N., Mollnes T.E., Lambris J.D. The role of complement in biomaterial-induced inflammation. Mol. Immunol. 2007; 44 (1–3): 82–94.
  10. McNally A.K., Jones J.A., Mac Ewan S.R., Colton E.,Anderson J.M. Vitronectin is a Critical Protein Adhesion Substrate for IL-4-induced Forein Body Giant Cell Formation. J Biomed Mater Res A. 2008; 86 (2): 535–43.
  11. Reed N.I., Jo H., Chen C., Tsujino K.,Arnold T.D., DeGrado W.F., Sheppard D. The αvβ1 integrin plays a critical in vivo role in tissue fibrosis. Sci Transl Med. 2015; 7 (288): 288ra79.
  12. Junge K., Binnebosel M., von Trotha K.T., Rosch R, Klinge U., Neumann U.P., Lynen Jansen P. Mesh biocompatibility: effects of cellular inflammation and tissue remodelling. Langenbecks Arch Surg. 2012; 397 (2): 255–70.