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Bioscience, Biotechnology, and Biochemistry Volume 73, 2009 - Issue 3
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Original Articles

Development, Characterization, and Evaluation of a Fusion Protein of a Novel Glucagon-Like Peptide-1 (GLP-1) Analog and Human Serum Albumin in Pichia pastoris

Zhihui GAODepartment of Microbiology, College of Life Sciences, Nankai University
,
Gang BAIDepartment of Microbiology, College of Life Sciences, Nankai University;College of Pharmacy, Nankai University
,
Jiaqi CHENDepartment of Microbiology, College of Life Sciences, Nankai University
,
Qi ZHANGCollege of Pharmacy, Nankai University
,
Pengwei PANDepartment of Microbiology, College of Life Sciences, Nankai University
,
Fang BAICollege of Pharmacy, Nankai University
&
Peng GENGDepartment of Microbiology, College of Life Sciences, Nankai University
 show all
Pages 688-694 | Received 16 Oct 2008, Accepted 11 Nov 2008, Published online: 22 May 2014

  • 1) Kieffer, T. J., and Habener, J. F., The glucagons-like peptides. Endocr. Rev., 20, 876–913 (1999).
  • 2) Holst, J. J., Glucagon-like peptide-1 (GLP-1): an intestinal hormone, signaling nutritional abundance, with an unusual therapeutic potential. Trends Endocrinol. Metab., 10, 229–235 (1999).
  • 3) Hui, H., Zhao, X., and Perfetti, R., Structure and function studies of glucagons-like peptide-1 (GLP-1): the designing of a novel pharmacological agent for the treatment of diabetes. Diabetes Metab. Res. Rev., 21, 313–331 (2005).
  • 4) Nathan, D. M., Schreiber, E., Fogel, H., Mojsov, S., and Habener, J. F., Insulinotropic action of glucagons-like peptide-1(7–37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma β TC-1 cells. Diabetes Care, 130, 159–166 (1992).
  • 5) Weir, G. C., Mojsov, S., Hendrick, G. K., and Habener, J. F., Glucagon-like peptide-1(7–37) action on endocrine pancreas. Diabetes, 38, 338–342 (1989).
  • 6) Deacon, C. F., Johnsen, A. H., and Holst, J. J., Degradation of glucagons-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J. Clin. Endocrinol. Metab., 80, 952–957 (1995).
  • 7) Burcelin, R., Dolci, W., and Thorens, B., Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagons-like peptide-1. Metabolism, 48, 252–258 (1999).
  • 8) Gallwitz, B., Ropeter, T., Morys-Wortmann, C., Mentlein, R., Siegel, E. G., and Schmidt, W. E., GLP-1 analogues resistant to degradation by dipeptidyl-peptidase IV in vitro. Regul. Pept., 86, 103–111 (2000).
  • 9) Deacon, C. F., Therapeutic strategic based on glucagons-like peptide-1. Diabetes, 53, 2181–2189 (2004).
  • 10) Sudre, B., Broqua, P., White, R. B., Ashworth, D., Evans, D. M., Haigh, R., Junien, J. L., and Aubert, M. L., Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999 011 delays the occurrence of diabetes in male Zucker diabetic fatty rats. Diabetes, 51, 1461–1469 (2002).
  • 11) Meier, J. J., Nauck, M. A., Kranz, D., Holst, J. J., Deacon, C. F., Gaeckler, D., Schmidt, W. E., and Gallwitz, B., Secretion, degradation and elimination of glucagon-like peptide-1 and gastric inhibitory polypeptide in patients with chronic renal insufficiency and healthy control subjects. Diabetes, 53, 654–662 (2004).
  • 12) Holst, J. J., Glucagon-like peptide-1: from extract to agent. The Claude Bernard Lecture, 2005. Diabetologia, 49, 253–260 (2006).
  • 13) Chuang, V. T., Kragh-Hansen, U., and Otagiri, M., Pharmaceutical strategies utilizing recombinant human serum albumin. Pharm. Res., 19, 569–577 (2002).
  • 14) Koehler, M. F., Zobel, K., Beresini, M. H., Caris, L. D., Combs, D., Paasch, B. D., and Lazarus, R. A., Albumin affinity tags increase peptide half-life in vivo. Bioorg. Med. Chem. Lett., 12, 2883–2886 (2002).
  • 15) Dennis, M. S., Zhang, M., Meng, Y. G., Kadkhodayan, M., Kirchhofer, D., Combs, D., and Damico, L. A., Albumin binding as a general strategy for improving the pharmacokinetics of proteins. J. Biol. Chem., 277, 35035–35043 (2002).
  • 16) Jiang, Z. Y., Gao, R., and Wang, Y. Q., Problems and solutions in PEGylation of protein and peptide drugs. Acta Pharm. Sin., 37, 396–400 (2002).
  • 17) Yeh, P., Landais, D., Lemaitre, M., Maury, I., Crenne, J. Y., Becquart, J., Murry-Brelier, A., Boucher, F., Montay, G., Fleer, R., Hirel, P. H., Mayaux, J. F., and Klatzmann, D., Design of yeast-secreted albumin derivatives for human therapy: biological and antiviral properties of a serum albumin-CD4 genetic conjugate. Proc. Natl. Acad. Sci. USA, 89, 1904–1908 (1992).
  • 18) Osborn, B. L., Olsen, H. S., Nardelli, B., Murray, J. H., Zhou, J. X., Garcia, A., Moody, G., Zaritskaya, L. S., and Sung, C., Pharmacokinetic and pharmacodynamic studies of a human serum albumin-interferon-alpha fusion protein in cynomolgus monkeys. J. Pharmacol. Exp. Ther., 303, 540–548 (2002).
  • 19) Melder, R. J., Osborn, B. L., Riccobene, T., Kanakaraj, P., Wei, P., Chen, G., Stolow, D., Halpern, W. G., Migone, T. S., Wang, Q., Grzegorzewski, K. J., and Gallant, G., Pharmacokinetics and its in vitro and its in vivo anti-tumor response of an interleukin-2-human serum albumin fusion protein in mice. Cancer Immunol. Immunother., 54, 535–547 (2005).
  • 20) Osborn, B. L., Sekut, L., Corcoran, M., Poortman, C., Sturm, B., Chen, G., Mather, D., Lin, H. L., and Parry, T. J., Albutropin: a growth hormone-albumin fusion with improved pharmacokinetic and pharmacodynamics in rats and monkeys. Eur. J. Pharmacol., 456, 149–158 (2002).
  • 21) Duttaroy, A., Kanakaraj, P., Osborn, B. L., Schneider, H., Pickeral, O. K., Chen, C., Zhang, G., Kaithamana, S., Singh, M., Schulingkamp, R., Crossan, D., Bock, J., Kaufman, T. E., Reavey, P., Carry-Barber, M., Krishnan, S. R., Garcia, A., Murphy, K., Siskind, J. K., Mclean, M. A., Cheng, S., Ruben, S., Birse, C. E., and Blondel, O., Development of a long-acting insulin analog using albumin fusion technology. Diabetes, 54, 251–258 (2005).
  • 22) Chen, J., Bai, G., Cao, Y., Gao, Z., Zhang, Q., Zhu, Y., and Yang, W., One-step purification of a fusion protein of glucagon-like peptide-1 and human serum albumin expressed in pichia pastoris by an immunomagnetic separation technique. Biosci. Biotechnol. Biochem., 71, 2655–2662 (2007).
  • 23) Tian, W., Li, Z. H., Cao, X. L., Yang, W. B., and Bai, G., Epitope maping of interfereon-α2b using a phage random peptide library. Chin. J. Microbiol. Immunol., 25, 578–582 (2005).
  • 24) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 25) Merri, C. R., Goldman, D., Sedman, S., and Ebert, M. H., Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science, 211, 1437–1438 (1981).
  • 26) Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA, 76, 4350–4354 (1979).
  • 27) Scrocchi, L. A., Brown, T. J., MacLusky, N., Brubaker, P. L., Auerbach, A. B., Joyner, A. L., and Drucker, D. J., Glucose intolerance but normal satiety in mice with a null mutation in the glucagon-like peptide a receptor gene. Nat. Med., 2, 1254–1258 (1996).
  • 28) Chou, J. Z., Place, G. D., Waters, D. G., and Kirkwood, J., A radioimmunoassay for LY315902, an analog of glucagon-like insulinotropic peptide, and its application in the study of canine pharmacokinetics. J. Pharm. Sci., 86, 768–773 (1997).
  • 29) Rolin, B., Larsen, M. O., Gotfredsen, C. F., Deacon, C. F., Carr, R. D., Wilken, M., and Knudsen, L. B., The long-acting GLP-1 derivative NN2211 ameliorates glycemia and increases beta-cell mass in diabetic mice. Am. J. Physiol. Endocrinol. Metab., 283, E745–E752 (2002).
  • 30) Harder, H., Nielsen, L., Tu, D. T., and Astrup, A., The effect of liraglutide, a long-acting glucagon-like peptide-1 derivative, on glycolic control, body composition, and 24-h energy expenditure in patients with type 2 diabetes. Diabetes Care, 27, 1915–1921 (2004).
  • 31) Kim, J. G., Baggio, L. L., Bridon, D. P., Castaigne, J. P., Robitaille, M. F., Jetté, L., Benquet, C., and Drucker, D. J., Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo. Diabetes, 52, 751–759 (2003).
  • 32) Bloom, M., Block, J., Duttaroy, A., Grzegorzewski, K., Moor, P., Ou, Y., Wojcik, S., Zhou, X., and Bell, A., Albugon fusion protein: a long acting analogue of GLP-1 that provides lasting antidiabetic effect in animals. Diabetes, 52 (Suppl. 1), A112 (2003).
  • 33) Dou, W. F., Lei, J. Y., Zhang, L. F., Xu, Z. H., Chen, Y., and Jin, J., Expression, purification, and characterization of recombinant human serum albumin fusion protein with two human glucagon-like peptide-1 mutants in Pichia pastoris. Protein Expr. Purif., 61, 45–49 (2008).
  • 34) Huang, J., Sakamuri, S., Leedom, T., Fu, Y. W., Oates, B., Desharnais, J., Tumelty, D., Del Rosario, J., Callans, S., Murphy, R., Lappe, R., Bradshaw, C., Woodnutt, G., and Levin, N., CVX-73: a GLP-1 mimetic CovX-Body (TM) with potent incretin bioactivity and extended pharmacokinetics in rodents and non-human primates. Diabetes, 56, A141 (2007).
  • 35) Lee, S. H., Lee, S., Youn, Y. S., Na, D. H., Chae, S. Y., Byun, Y., and Lee, K. C., Synthesis characterization, and pharmacokinetic studies of PEGylated glucagons-like peptide-1. Bioconj. Chem., 6, 377–382 (2005).
  • 36) Huang, Y. S., Chen, Z., Yang, Z. Y., Wang, T. Y., Zhou, L., Wu, J. B., and Zhou, L. F., Preparation and characterization of a potent, long-lasting recombinant human serum albumin-interferon-alpha2b fusion protein expressed in Pichia pastoris. Eur. J. Pharm. Biopharm., 67, 301–308 (2007).
  • 37) Huang, Y. S., Chen, Z., Chen, Y. Q., Ma, G. C., Shan, J. F., Liu, W., and Zhou, L. F., Preparation and characterization of a novel exendin-4 human serum albumin fusion protein expressed in Pichia pastoris. J. Pept. Sci., 14, 588–595 (2008).
  • 38) Peter, T. J., Serum albumin. Adv. Protein Chem., 37, 161–245 (1985).
  • 39) Plamboeck, A., Holst, J. J., Carr, R. D., and Deacon, C. F., Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetized pig. Diabetologia, 48, 1882–1890 (2005).
  • 40) O’Harte, F. P., Mooney, M. H., Kelly, C. M., McKillop, A. M., and Flatt, P. R., Degradation and glycemic effects of His(7)-glucitol glucagon-like peptide-1(7–36)amide in obese diabetic ob/ob mice. Regul. Pept., 96, 95–104 (2001).

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