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

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 11, 2007, Pages 2655-2662

  Chen, Jiaqi ^a   Bai, Gang ^a   Cao, Yu ^a   Gao, Zhihui ^a   Zhang, Qi ^a   Zhu, Yuanyuan ^a   Yang, Wenbo ^a  

^a NANKAI UNIVERSITY   (China)

Author keywords

Fusion protein; Glucagon like peptide 1; Human serum albumin; Immunomagnetic cellulose microspheres; Immunomagnetic separation

Indexed keywords

ENZYME ACTIVITY; GENES; GLUCOSE; INSULIN; MEDICAL PROBLEMS;

FUSION PROTEINS; GLUCAGON LIKE PEPTIDE; HUMAN SERUM ALBUMIN; IMMUNOMAGNETIC CELLULOSE MICROSPHERES; IMMUNOMAGNETIC SEPARATION TECHNIQUES;

PROTEINS;

GLUCAGON LIKE PEPTIDE 1; HYBRID PROTEIN; SERUM ALBUMIN;

ANIMAL; ARTICLE; BIOSYNTHESIS; CHEMISTRY; DRUG EFFECT; GENE VECTOR; GENETICS; GLUCOSE BLOOD LEVEL; HUMAN; IMMUNOMAGNETIC SEPARATION; ISOLATION AND PURIFICATION; METHODOLOGY; MOUSE; MOUSE STRAIN; PICHIA;

ANIMALS; BLOOD GLUCOSE; GENETIC VECTORS; GLUCAGON-LIKE PEPTIDE 1; HUMANS; IMMUNOMAGNETIC SEPARATION; MICE; MICE, INBRED STRAINS; PICHIA; RECOMBINANT FUSION PROTEINS; SERUM ALBUMIN;

MUS; PICHIA PASTORIS;

EID: 36448974915     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70190     Document Type: Article

References (34)

1. Drucker, D. J., The glucagon-like peptides. Diabetes, 47, 159-169 (1998).
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. Vella, A., Shah, P., Basu, R., Basu, A., Holst, J. J., and Rizza, R. A., Effect of glucagon-like peptide 1(7-36) amide on glucose effectiveness and insulin action in people with type 2 diabetes. Diabetes, 49, 611-617 (2000).
4. Flint, A., Raben, A., Astrup, A., and Holst, J. J., Glucagon-like peptide 1 promotes satiety and suppresses energy intake in humans. J. Clin. Invest., 101, 515-520 (1998).
5. Turton, M. D., O'Shea, D., Gunn, I., Beak, S. A., Edwards, C. M., Meeran, K., Choi, S. J., Taylor, G. M., Heath, M. M., Lambert, P. D., Wilding, J. P., Smith, D. M., Ghatei, M. A., Herbert, J., and Bloom, S. R., A role for glucagon-like peptide-1 in the central regulation of feeding. Nature, 379, 69-72 (1996).
6. Stoffers, D. A., Kieffer, T. J., Hussain, M. A., Drucker, D. J., Bonner-Weir, S., Habener, J. F., and Egan, J. M., Insulinotropic glucagon-like peptide-1 agonists stimulate expression of homeodomain protein IDX-1 and increase β-cell mass in mouse pancreas. Diabetes, 49, 741-748 (2000).
7. Deacon, C. F., Johnsen, A. H., and Holst, J. J., Degradation of glucagon-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).
8. Drucker, D. J., Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Curr. Pharm. Des., 7, 1399-1412 (2001).
9. Burcelin, R., Dolci, W., and Thorens, B., Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagon-like peptide-1. Metabolism, 48, 252-258 (1999).
10. 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).
11. Kim, J. G., Baggio, L. L., Bridon, D. P., Castaigne, J. P., Robitaille, M. F., Jette, L., Benquet, C., and Drucker, D. J., Development and characterization of a glucagon-like peptide 1-albumin conjugate. Diabetes, 52, 751-759 (2003).
12. 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).
13. Ahren, B., Landin-Olsson, M., Jansson, P. A., Svensson, M., Holmes, D., and Schweizer, A., Inhibition of dipeptidyl peptidase-4 reduces glycemia, sustains insulin levels, and reduces glucagons levels in type 2 diabetes. J. Clin. Endocrinol. Metab., 89, 2078-2084 (2004).
14. 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).
15. 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).
16. 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).
17. 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).
18. Elbrond, B., Jakobsen, G., Larsen, S., Agerso, H., Jensen, L. B., Rolan, P., Sturis, J., Hatorp, V., and Zdravkovic, M., Pharmacokinetics, pharmacodynamics, safety, and tolerability of a single-dose of NN2211, a long-acting glucagon-like peptide 1 derivative, in healthy male subjects. Diabetes Care, 25, 1398-1404 (2002).
19. Ogiue-Ikeda, M., Sato, Y., and Ueno, S., A new method to destruct targeted cells using magnetizable beads and pulsed magnetic force. IEE Trans. Nanobiosci., 2, 262-265 (2003).
20. Hanau, D., Schmitt, D. A., Fabre, M., and Cazenave, J. P., A method for the rapid isolation of human epidermal Langerhans cells using immunomagnetic microspheres. J. Invest. Dermatol., 91, 274-279 (1988).
21. Clarke, C., Titley, J., Davies, S., and O'Hare, M. J., An immunomagnetic separation method using superparamagnetic (MACS) beads for large-scale purification of human mammary luminal and myoepithelial cells. Epithelial Cell Biol., 3, 38-46 (1994).
22. Prioult, G., Turcotte, C., Labarre, L., Lacroix, C., and Fliss, I., Rapid purification of nisin A using specific monoclonal antibody-coated magnetic beads. Int. Dairy J., 10, 627-633 (2000).
23. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
24. Merril, 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).
25. 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).
26. Tian, W., Li, Z. H., Cao, X. L., Yang, W. B., and Bai, G., Epitope mapping of interferon-α2b using phage random peptide library. Chin. J. Microbiol. Immunol., 25, 578-582 (2005).
27. Cao, Y., Bai, G., Chen, J. Q., Tian, W., Wang, S. Q., and Yang, W. B., Preparation and characterization of magnetic microspheres for the purification of interferon α-2b. J. Chromatogr. B, 833, 236-244 (2006).
28. 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 1 receptor gene. Nat. Med., 2, 1254-1258 (1996).
29. Cereghino, J. L., and Cregg, J. M., Heterologous protein expression in the methylotrophic yeast Pichia pastor. Microbiol. Rev., 24, 45-66 (2000).
30. Ugelstad, J., Soderberg, L., Berge, A., and Bergstrom, J., Monodisperse polymer particles: a step forward for chromatography. Nature, 303, 95-96 (1983).
31. Mosbach, K., and Andersson, L., Magnetic ferrofluids for preparation of magnetic polymers and their application in affinity chromatography. Nature, 270, 259-261 (1977).
32. Shinkai, M., and Ito, A., Functional magnetic particles for medical application. Adv. Biochem. Eng. Biotechnol., 91, 191-220 (2004).
33. Bilkova, Z., Slovakova, M., Lycka, A., Horak, D., Lenfeld, J., Turkova, J., and Churacek, J., Oriented immobilization of galactose oxidase to bead and magnetic bead cellulose and poly(HEMA-co-EDMA) and magnetic poly(HEMA-co-EDMA) microspheres. J. Chromatogr. B, 770, 25-34 (2002).
34. Brandl, M., Hartmann, J., Posnicek, T., Ausenegg, F. R., Leitner, A., and Falkenhagen, D., Detection of fluorescently labeled microparticles in blood. Blood Purif., 23, 181-189 (2005).