Engineering, Expression, and Renaturation of a Collagen-Targeted Human bFGF Fusion Protein

References

• Abraham J. A, Mergia A., Whang J. L, Tumulo A., Friedman J., Hjerrild K. A, Gospodarowicz D., Fiddes J. C. Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor. Science 1986a; 233: 545–548
   PubMed Web of Science ®Google Scholar
• Abraham J. A, Whang J. L, Tumulo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J. C. Human basic fibroblast growth factor: nucleotide sequence and genomic organization. EMBO J. 1986b; 5: 2523–2528
   PubMed Web of Science ®Google Scholar
• Andrades J. A, Han B., Becerra J., Sorgente N., Hall F. L, Nimni M. E. A recombinant human TGF-β1 fusion protein with collagen-binding domain promotes migration, growth, and differentiation of bone marrow mesenchymal cells. Exp. Cell Res. 1999; 250: 485–498
   PubMed Web of Science ®Google Scholar
• Baird A., Ling N. Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: implications for a role of heparinase-like enzymes in the neovascular response. Biochem. Biophys. Res. Commun. 1987; 142: 428–435
   PubMed Web of Science ®Google Scholar
• Baird A., Mormède P., Böhlen P. Immunoreactive fibroblast growth factor in cells of peritoneal exudate suggests its identity with macrophage-derived growth factor. Biochem. Biophys. Res. Commun. 1985; 126: 358–364
   PubMed Web of Science ®Google Scholar
• Bohlen P., Baird A., Esch F., Ling N., Gospodarowicz D. Isolation of brain fibroblast growth factor by heparin Sepharose affinity chromatography: identity with pituitary fibroblast growth factor. Proc. Natl. Acad. Sci. USA 1984; 81: 6963–6967
   PubMedGoogle Scholar
• Broad T. E., Ham R. G. Growth and adipose differentiation of sheep preadipocyte fibroblasts is serum free medium. Eur. J. Biochem. 1983; 135: 33–39
   PubMedGoogle Scholar
• Burgess W. H., Maciag T. The heparin-binding (fibroblast) growth factor family of proteins. Ann. Rev. Biochem. 1989; 58: 575–606
   PubMed Web of Science ®Google Scholar
• Cardamone M., Puri N. K, Brandon M. R. Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies. Biochemistry 1995; 34: 5773–5794
   PubMedGoogle Scholar
• Cheung D. T, Benya P. D, Gorn A., Nimni M. E. An efficient method for in vitro labeling proteins to high specific radioactivity using 3H-NaBH4 in dimethylformamide. Anal. Biochem. 1981; 116: 69–74
   PubMedGoogle Scholar
• Clark R. A.F. Wound repair: overview and general considerations. The Molecular and Cellular Biology of Wound Repair, R. A.F. Clark. Plenum Press, NY 1996; 3–50
   Google Scholar
• Cleland J. L, Hedgepeth C., Wang D. I. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. Reaction stoichiometry and refolding moldel. J. Biol. Chem. 1992; 267: 13327–13334
   PubMed Web of Science ®Google Scholar
• Edelman E. R, Mathiowitz E., Langer R., Klagsbrun M. Controlled and modulated release of basic fibroblast growth factor. Biomaterials 1991; 12: 619–626
   PubMed Web of Science ®Google Scholar
• Esch F. A, Baird A., Ling N., Ueno N., Hill F., Denoroy L., Kleper R., Gospodarowicz D., Bohlen P., Guillemin R. Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF. Proc. Natl. Acad. Sci. USA 1985; 82: 6507–6511
   PubMed Web of Science ®Google Scholar
• Florkiewicz R. Z, Sommer A. Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons. Proc. Nall. Acad. Sci. USA 1989; 86: 3978–3981
   PubMed Web of Science ®Google Scholar
• Gary A. M, Mason A. J. Requirement for activin A and transforming growth factor β1 pro-regions in homodimer assembly. Science 1990; 247: 1328–1330
   PubMed Web of Science ®Google Scholar
• Gimenez-Gallego G., Rodkey J., Bennet C., Rios-Candelore M., DiSalvo J., Thomas K. A. Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies. Science 1985; 230: 1385–1388
   PubMed Web of Science ®Google Scholar
• Gordon E. M, Skotzko M., Kundu R. K, Han B., Andrades J. A, Nimni M. E, Anderson W. F, Hall F. L. Capture and expansion of bone marrow-derived mesenchymal progenitor cells with a transforming growth factor-β1-von Willebrand's factor fusion protein for retro-virus-mediated delivery of coagulation factor IX. Hum. Gene Ther. 1997; 8: 1385–1394
   PubMed Web of Science ®Google Scholar
• Gorlin R. J. Fibroblast growth factors, their receptors and receptor disorders. J. Craniomaxillofac. Surg. 1997; 25: 69–79
   PubMedGoogle Scholar
• Gospodarowicz D. Fibroblast growth factor. Critical Reviews in Oncogenesis, M. Perucho. CRC Press, Boca Raton, FL 1989; 1–26
   Google Scholar
• Gospodarowicz D., Ferrara N., Schweigerer L., Neufeld G. Structural characterization and biological functions of fibroblast growth factor. Endocr. Rev. 1987; 8: 95–114
   PubMed Web of Science ®Google Scholar
• Han B., Hall F. L, Nimni M. E. Refolding of a recombinant collagen targeted TGF-β2 fusion protein expressed in Escherichia coli. Protein Expr. Purif. 1997; 11: 169–178
   PubMedGoogle Scholar
• Handl C. E, Harel J., Flock J. I, Dubreuil J. D. High yield of active STb enterotoxin from a fusion protein (MBP-STb) expressed in Escherichia coli. Protein Expr. Purif. 1993; 4: 275–281
   PubMedGoogle Scholar
• Jaye M., Howk R., Burgess W., Ricca G. A, Chiu I. M, Ravea M. W, O'Brien S. J, Modi W. S, Maciag T., Drohan W. N. Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosomal localization. Science 1986; 233: 541–545
   PubMed Web of Science ®Google Scholar
• Klagsbrun M., Sasse J., Sullivan R., Smith J. A. Human tumor cells synthesize an endothelial cell growth factor that is structurally related to basic fibroblast growth factor. Proc. Natl. Acad. Sci. USA 1986; 83: 2448–2452
   PubMed Web of Science ®Google Scholar
• Lindner V. Role of basic fibroblast growth factor and platelet-derived growth factor (B-chain) in neointima formation after arterial injury. Z. Kardiol. 1995; 4: 137–144
   Google Scholar
• Lobb R., Sasse J., Sullivan R., Shing Y., D'Amore P., Jacobs J., Klagsbrun M. Purification and characterization of heparin-binding endothelial cell growth factors. J. Biol. Chem. 1986; 261: 1924–1928
   PubMed Web of Science ®Google Scholar
• Maciag T., Mehlman T., Freisel R., Schreiber A. Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain. Science 1984; 225: 932–935
   PubMed Web of Science ®Google Scholar
• Martin P. Wound healing-aiming for perfect skin regeneration. Science 1997; 276: 75–81
   PubMed Web of Science ®Google Scholar
• Moses M. A, Klagsbrun M., Shing Y. The role of growth factors in vascular cell development and differentiation. Int. Rev. Cytol. 1995; 161: 1–48
   PubMedGoogle Scholar
• Neufeld G., Gospodarowicz D. Basic and acidic fibroblast growth factors interact with the same cell surface receptors. J. Biol. Chem. 1986; 261: 5631–5637
   PubMed Web of Science ®Google Scholar
• Neufeld G., Gospodarowicz D., Dodge L., Fujii D. K. Heparin modulation of the neurotropic effects of acidic and basic fibroblast growth factors and nerve growth factors on PC-12. J. Cell Physiol. 1987; 131: 131–140
   PubMed Web of Science ®Google Scholar
• Nimni M. E. The molecular organization of collagen and its role in determining the biophysical properties of the connective tissues. Biorheology 1980; 17: 51–82
   PubMed Web of Science ®Google Scholar
• Nimni M. E. Polypeptide growth factors: targeted delivery systems. Biomaterials 1997; 18: 1201–1225
   PubMed Web of Science ®Google Scholar
• Okumura M., Okuda T., Nakamura T., Yajima M. Acceleration of wound healing in diabetic mice by fibroblast growth factor. Biol. Pharm. Bull. 1996; 19: 530–535
   PubMedGoogle Scholar
• Pierce G. F, Tarpley J. E, Yanagihara D., Mustoe T. A, Fox G. M, Thomason A. Platelet-derived growth factor (BB homodimer), transforming growth factor-β1, and basic fibroblast growth factor in dermal wound healing. Neovessel and matrix formation and cessation of repair. Am. J. Pathol. 1992; 140: 1375–1388
   PubMed Web of Science ®Google Scholar
• Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 1996; 10: 49–56
   PubMed Web of Science ®Google Scholar
• Sato Y., Rifkin D. Autocrine activities of basic fibroblast growth factor: regulation of endothelial cell movement, plasminogen activator synthesis, and DNA synthesis. J. Cell Biol. 1988; 107: 1199–1205
   PubMed Web of Science ®Google Scholar
• Satoh H., Shino A., Sato F., Asano S., Murakami I., Inatomi N., Nagaya H., Kato K., Szabo S., Folkman J. Role of endogenous basic fibroblast growth factor in the healing of gastric ulcers in rats. Jpn. J. Pharmacol. 1997; 73: 59–71
   PubMedGoogle Scholar
• Schumann J., Bohm G., Schumacher G., Rudolph R., Jaenicke R. Stabilization of creatinase from Pseudomonas putida by random mutagenesis. Protein Sci. 1993; 2: 1612–1620
   PubMed Web of Science ®Google Scholar
• Schweigerer L., Neufeld G., Friedman J., Abraham J. A, Fiddes J. C, Gospodarowicz D. Capillary endothelial cells express basic fibroblast growth factor, a mitogen that promotes their own growth. Nature (London) 1987; 325: 257–259
   PubMed Web of Science ®Google Scholar
• Shing Y., Folkman J., Sullivan R., Butterfield C., Murray J., Klagsbrun M. Heparin affinity purification of a tumor-derived capillary endothelial cell growth factor. Science 1984; 223: 1296–1299
   PubMed Web of Science ®Google Scholar
• Sullivan R., Klagsbrun M. Purification of cartilage-derived growth factor by heparin affinity chromatography. J. Biol. Chem. 1985; 260: 2399–2403
   PubMed Web of Science ®Google Scholar
• Takagi J., Jujisawa T., Sekiya F., Saito Y. Collagen-binding domain within bovine propolypeptide of von Willebrand factor. J. Biol. Chem. 1991; 266: 5575–5579
   PubMedGoogle Scholar
• Takagi J., Asai H., Saito Y. A collagen/gelatin-binding decapeptide derived from bovine propolypeptide of von Willebrand factor. Biochem. 1992; 31: 8530–8534
   PubMed Web of Science ®Google Scholar
• Tuan T.-L., Cheung D. T, Wu L-T., Yee A., Gabriel S., Han B., Morton L., Nimni M. E, Hall F. L. Engineering, expression and renaturation of targeted TGF-β fusion proteins. Connect. Tissue Res. 1996; 34: 1–9
   PubMed Web of Science ®Google Scholar
• Vlodavsky I., Folkman J., Sullivan R., Friedman R., Ishal-Michaeli R., Sasse J., Klagsbrun M. Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix. Proc. Natl. Acad. Sci. USA 1987; 84: 2292–2296
   PubMed Web of Science ®Google Scholar
• Walker K. W, Gilbert H. F. Effect of redox environment on the in vitro and in vivo folding of RTEM-1 β-lactamase and Escherichia coli alkaline phosphatase. J. Biol. Chem. 1994; 269: 28487–28493
   PubMedGoogle Scholar
• Zenjari C., Boilly B., Hondermarck H., Boilly-Marer Y. Nerve-blastema interactions induce fibroblast growth factor-1 release during limb regeneration in Pleurodeles waltl. Dev. Growth Differ. 1997; 39: 15–22
   PubMedGoogle Scholar