Engineered aprotinin for improved stability of fibrin biomaterials

Biomaterials

Volumn 32, Issue 2, 2011, Pages 430-438

  Lorentz, Kristen M ^a   Kontos, Stephan ^a   Frey, Peter ^a,b   Hubbell, Jeffrey A ^a,b  

^a EPFL   (Switzerland)

^b LAUSANNE UNIVERSITY HOSPITAL   (Switzerland)

Author keywords

Crosslinking; Degradation; Fibrin; Recombinant protein

Indexed keywords

APROTININ; CROSSLINKED; FIBRIN; FIBRIN MATRIX; HUMAN DERMAL FIBROBLASTS; IN-VITRO; IN-VIVO; OTHER APPLICATIONS; PROTEASE INHIBITOR; RECOMBINANT APROTININ; RECOMBINANT PROTEIN; TRANSGLUTAMINASES; WILD TYPES;

BIOLOGICAL MATERIALS; BIOMATERIALS; CELL CULTURE; DEGRADATION; GROWTH KINETICS;

CROSSLINKING;

ALPHA 2 ANTIPLASMIN; APROTININ; BIOMATERIAL; BLOOD CLOTTING FACTOR 13A; FIBRIN; FIBRIN GLUE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RECOMBINANT PROTEIN;

ARTICLE; CELL GROWTH; CELL PROLIFERATION; CONCENTRATION (PARAMETERS); CROSS LINKING; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; NANOENGINEERING; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN POLYMERIZATION; PROTEIN STABILITY; PROTEIN VARIANT;

ANIMALS; APROTININ; BIOCOMPATIBLE MATERIALS; CELLS, CULTURED; FEMALE; FIBRIN; FIBRIN TISSUE ADHESIVE; FIBRINOLYSIN; HUMANS; MICE; MICE, INBRED C57BL; WOUND HEALING;

MUS;

EID: 78449258828     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2010.08.109     Document Type: Article

References (34)

1. Spotnitz W.D. Fibrin sealant: past, present, and future: a brief review. World J Surg 2010, 34:632-634.
2. Fu J.Z., Li J., Yu Z.L. Effect of implanting fibrin sealant with ropivacaine on pain after laparoscopic cholecystectomy. World J Gastroenterol 2009, 15:5851-5854.
3. Danielsen P.L., Agren M.S., Jorgensen L.N. Platelet-rich fibrin versus albumin in surgical wound repair: a randomized trial with paired design. Ann Surg 2010, 251:825-831.
4. Garcia-Olmo D., Herreros D., Pascual I., Pascual J.A., Del-Valle E., Zorrilla J., et al. Expanded adipose-derived stem cells for the treatment of complex perianal fistula: a phase II clinical trial. Dis Colon Rectum 2009, 52:79-86.
5. Ahmed T.A., Dare E.V., Hincke M. Fibrin: a versatile scaffold for tissue engineering applications. Tissue Eng Part B Rev 2008, 14:199-215.
6. Buchta C., Hedrich H.C., Macher M., Hocker P., Redl H. Biochemical characterization of autologous fibrin sealants produced by CryoSeal and Vivostat in comparison to the homologous fibrin sealant product Tissucol/Tisseel. Biomaterials 2005, 26:6233-6241.
7. Barker T.H., Fuller G.M., Klinger M.M., Feldman D.S., Hagood J.S. Modification of fibrinogen with poly(ethylene glycol) and its effects on fibrin clot characteristics. J Biomed Mater Res 2001, 56:529-535.
8. Ahmed T.A., Griffith M., Hincke M. Characterization and inhibition of fibrin hydrogel-degrading enzymes during development of tissue engineering scaffolds. Tissue Eng 2007, 13:1469-1477.
9. Kupcsik L., Alini M., Stoddart M.J. Epsilon-aminocaproic acid is a useful fibrin degradation inhibitor for cartilage tissue engineering. Tissue Eng Part A 2009, 15:2309-2313.
10. Sperzel M., Huetter J. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost 2007, 5:2113-2118.
11. Kang H.M., Kalnoski M.H., Frederick M., Chandler W.L. The kinetics of plasmin inhibition by aprotinin in vivo. Thromb Res 2005, 115:327-340.
12. Smith J.D., Chen A., Ernst L.A., Waggoner A.S., Campbell P.G. Immobilization of aprotinin to fibrinogen as a novel method for controlling degradation of fibrin gels. Bioconjug Chem 2007, 18:695-701.
13. Schense J.C., Hubbell J.A. Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconjug Chem 1999, 10:75-81.
14. Chandler W.L., Alessi M.C., Aillaud M.F., Vague P., Juhan-Vague I. Formation, inhibition and clearance of plasmin in vivo. Haemostasis 2000, 30:204-218.
15. Martino M.M., Mochizuki M., Rothenfluh D.A., Rempel S.A., Hubbell J.A., Barker T.H. Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability. Biomaterials 2009, 30:1089-1097.
16. Koch S., Flanagan T.C., Sachweh J.S., Tanios F., Schnoering H., Deichmann T., et al. Fibrin-polylactide-based tissue-engineered vascular graft in the arterial circulation. Biomaterials 2010, 31:4731-4739.
17. Yao L., Swartz D.D., Gugino S.F., Russell J.A., Andreadis S.T. Fibrin-based tissue-engineered blood vessels: differential effects of biomaterial and culture parameters on mechanical strength and vascular reactivity. Tissue Eng 2005, 11:991-1003.
18. Francis C.W., Marder V.J., Barlow G.H. Plasmic degradation of crosslinked fibrin. Characterization of new macromolecular soluble complexes and a model of their structure. J Clin Invest 1980, 66:1033-1043.
19. Francis C.W., Marder V.J., Martin S.E. Plasmic degradation of crosslinked fibrin. I. Structural analysis of the particulate clot and identification of new macromolecular-soluble complexes. Blood 1980, 56:456-464.
20. Kimura S., Aoki N. Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. J Biol Chem 1986, 261:15591-15595.
21. Watt K.W., Cottrell B.A., Strong D.D., Doolittle R.F. Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry 1979, 18:5410-5416.
22. Dyckes D.F., Creighton T., Sheppard R.C. Spontaneous re-formation of a broken peptide chain. Nature 1974, 247:202-204.
23. Sun Z., Lu W., Jiang A., Chen J., Tang F., Liu J.N. Expression, purification and characterization of aprotinin and a human analogue of aprotinin. Protein Expr Purif 2009, 65:238-243.
24. Novokhatny V. Structure and activity of plasmin and other direct thrombolytic agents. Thromb Res 2008, 122(Suppl. 3):S3-S8.
25. Weisel J.W., Litvinov R.I. The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate. Cardiovasc Hematol Agents Med Chem 2008, 6:161-180.
26. Turner B.T., Maurer M.C. Evaluating the roles of thrombin and calcium in the activation of coagulation factor XIII using H/D exchange and MALDI-TOF MS. Biochemistry 2002, 41:7947-7954.
27. He C.S., Wilhelm S.M., Pentland A.P., Marmer B.L., Grant G.A., Eisen A.Z., et al. Tissue cooperation in a proteolytic cascade activating human interstitial collagenase. Proc Natl Acad Sci U S A 1989, 86:2632-2636.
28. Makowski G.S., Ramsby M.L. Binding of latent matrix metalloproteinase 9 to fibrin: activation via a plasmin-dependent pathway. Inflammation 1998, 22:287-305.
29. Monea S., Lehti K., Keski-Oja J., Mignatti P. Plasmin activates pro-matrix metalloproteinase-2 with a membrane-type 1 matrix metalloproteinase-dependent mechanism. J Cell Physiol 2002, 192:160-170.
30. Ries C., Popp T., Egea V., Kehe K., Jochum M. Matrix metalloproteinase-9 expression and release from skin fibroblasts interacting with keratinocytes: upregulation in response to sulphur mustard. Toxicology 2009, 263:26-31.
31. Stoff A., Rivera A.A., Mathis J.M., Moore S.T., Banerjee N.S., Everts M., et al. Effect of adenoviral mediated overexpression of fibromodulin on human dermal fibroblasts and scar formation in full-thickness incisional wounds. J Mol Med 2007, 85:481-496.
32. de Giorgio-Miller A., Bottoms S., Laurent G., Carmeliet P., Herrick S. Fibrin-induced skin fibrosis in mice deficient in tissue plasminogen activator. Am J Pathol 2005, 167:721-732.
33. Herrick S., Blanc-Brude O., Gray A., Laurent G. Fibrinogen. Int J Biochem Cell Biol 1999, 31:741-746.
34. Martin P., Leibovich S.J. Inflammatory cells during wound repair: the good, the bad and the ugly. Trends Cell Biol 2005, 15:599-607.