Cloning, expression and purification of the human Islet Amyloid Polypeptide (hIAPP) from Escherichia coli

Protein Expression and Purification

Volumn 106, Issue , 2015, Pages 49-56

  Rodriguez Camargo, Diana C ^a,b   Tripsianes, Konstantinos ^c   Kapp, Tobias G ^b   Mendes, Joaquim ^a   Schubert, Jasmin ^a   Cordes, Burghard ^b   Reif, Bernd ^a,b  

^a INSTITUTE OF EPIDEMIOLOGY   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c MASARYK UNIVERSITY   (Czech Republic)

Author keywords

Amyloid; Diabetes; Escherichia coli; Nuclear magnetic resonance (NMR); Recombinant protein human Islet Amyloid Polypeptide (hIAPP)

Indexed keywords

ESCHERICHIA COLI;

AMYLIN; HYBRID PROTEIN;

AGAR GEL ELECTROPHORESIS; AMINO ACID SEQUENCE; CHEMISTRY; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROCEDURES; REVERSED PHASE LIQUID CHROMATOGRAPHY;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, REVERSE-PHASE; CLONING, MOLECULAR; ELECTROPHORESIS, AGAR GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HUMANS; ISLET AMYLOID POLYPEPTIDE; MOLECULAR SEQUENCE DATA; RECOMBINANT FUSION PROTEINS;

EID: 84911445923     PISSN: 10465928     EISSN: 10960279     Source Type: Journal    
DOI: 10.1016/j.pep.2014.10.012     Document Type: Article

References (45)

1. A. Kanatsuka, H. Makino, H. Ohsawa, Y. Tokuyama, T. Yamaguchi, S. Yoshida, and M. Adachi Secretion of islet amyloid polypeptide in response to glucose FEBS Lett. 259 1 1989 199 201
2. B. Ludvik, A. Kautzky-Willer, R. Prager, K. Thomaseth, and G. Pacini Amylin: history and overview Diabet. Med. 14 S2 1997 S9 S13
3. T. Sanke, T. Hanabusa, Y. Nakano, C. Oki, K. Okai, S. Nishimura, M. Kondo, and K. Nanjo Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients Diabetologia 34 2 1991 129 132
4. H.J. Woerle, M. Albrecht, R. Linke, S. Zschau, C. Neumann, M. Nicolaus, J.E. Gerich, B. Göke, and J. Schirra Impaired hyperglycemia-induced delay in gastric emptying in patients with type 1 diabetes deficient for islet amyloid polypeptide Diabetes Care 31 12 2008 2325 2331
5. M.W. Cluck, C.Y. Chan, and T.E. Adrian The regulation of amylin and insulin gene expression and secretion Pancreas 30 1 2005 1 14
6. T. Sanke, G. Bell, C. Sample, A. Rubenstein, and D. Steiner An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing J. Biol. Chem. 263 33 1988 17243 17246
7. C. Betsholtz, V. Svensson, F. Rorsman, U. Engström, G.T. Westermark, E. Wilander, K. Johnson, and P. Westermark Islet amyloid polypeptide (IAPP): cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus Exp. Cell Res. 183 2 1989 484 493
8. M. Nishi, S.J. Chan, S. Nagamatsu, G.I. Bell, and D.F. Steiner Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone Proc. Natl. Acad. Sci. 86 15 1989 5738 5742
9. S. Mosselman, J. Höppener, C. Lips, and H. Jansz The complete islet amyloid polypeptide precursor is encoded by two exons FEBS Lett. 247 1 1989 154 158
10. L. Marzban, G. Trigo-Gonzalez, X. Zhu, C.J. Rhodes, P.A. Halban, D.F. Steiner, and C.B. Verchere Role of β-cell prohormone convertase (PC) 1/3 in processing of pro-islet amyloid polypeptide Diabetes 53 1 2004 141 148
11. J. Wang, J. Xu, J. Finnerty, M. Furuta, D.F. Steiner, and C.B. Verchere The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site Diabetes 50 3 2001 534 539
12. F. Evers, C. Jeworrek, S. Tiemeyer, K. Weise, D. Sellin, M. Paulus, B. Struth, M. Tolan, and R. Winter Elucidating the mechanism of lipid membrane-induced IAPP fibrillogenesis and its inhibition by the red wine compound resveratrol: a synchrotron X-ray reflectivity study J. Am. Chem. Soc. 131 27 2009 9516 9521
13. G. Cooper, A. Willis, A. Clark, R. Turner, R. Sim, and K. Reid Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients Proc. Natl. Acad. Sci. 84 23 1987 8628 8632
14. A. Andersson, S. Bohman, L.A. Borg, J.F. Paulsson, S.W. Schultz, G.T. Westermark, and P. Westermark Amyloid deposition in transplanted human pancreatic islets: a conceivable cause of their long-term failure Exp. Diabetes Res. 2008 2008 562985
15. A.J. Shapiro, J.R. Lakey, E.A. Ryan, G.S. Korbutt, E. Toth, G.L. Warnock, N.M. Kneteman, and R.V. Rajotte Islet transplantation in seven patients with type 1 diabetes mellitus using a glucocorticoid-free immunosuppressive regimen N. Engl. J. Med. 343 4 2000 230 238
16. R. Mishra, M. Geyer, and R. Winter NMR spectroscopic investigation of early events in IAPP amyloid fibril formation ChemBioChem 10 11 2009 1769 1772
17. R.P. Nanga, J.R. Brender, S. Vivekanandan, and A. Ramamoorthy Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment Biochim. Biophys. Acta 1808 10 2011 2337 2342
18. L. Wei, P. Jiang, W. Xu, H. Li, H. Zhang, L. Yan, M.B. Chan-Park, X.-W. Liu, K. Tang, and Y. Mu The molecular basis of distinct aggregation pathways of islet amyloid polypeptide J. Biol. Chem. 286 8 2011 6291 6300
19. J.R. Cort, Z. Liu, G.M. Lee, K.N. Huggins, S. Janes, K. Prickett, and N.H. Andersen Solution state structures of human pancreatic amylin and pramlintide Protein Eng. Des. Sel. 22 8 2009 497 513
20. E. Jack, M. Newsome, P.G. Stockley, S.E. Radford, and D.A. Middleton The organization of aromatic side groups in an amyloid fibril probed by solid-state 2H and 19F NMR spectroscopy J. Am. Chem. Soc. 128 25 2006 8098 8099
21. S. Luca, W.-M. Yau, R. Leapman, and R. Tycko Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR Biochemistry 46 47 2007 13505 13522
22. J.T. Nielsen, M. Bjerring, M.D. Jeppesen, R.O. Pedersen, J.M. Pedersen, K.L. Hein, T. Vosegaard, T. Skrydstrup, D.E. Otzen, and N.C. Nielsen Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy Angew. Chem. Int. Ed. Engl. 48 12 2009 2118 2121
23. 15N-labeled recombinant human amylin for solid-state NMR investigation Protein Expr. Purif. 99 2014 119 130
24. M.R. Nilsson, L.L. Nguyen, and D.P. Raleigh Synthesis and purification of amyloidogenic peptides Anal. Biochem. 288 1 2001 76 82
25. V.H. Finder, I. Vodopivec, R.M. Nitsch, and R. Glockshuber The recombinant amyloid-β peptide Aβ1-42 aggregates faster and is more neurotoxic than synthetic Aβ1-42 J. Mol. Biol. 396 1 2010 9 18
26. F. Meng, A. Abedini, A. Plesner, C.B. Verchere, and D.P. Raleigh The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity Biochemistry 49 37 2010 8127 8133
27. J.F. Paulsson, S.W. Schultz, M. Köhler, I. Leibiger, P.-O. Berggren, and G.T. Westermark Real-time monitoring of apoptosis by caspase-3-like protease induced FRET reduction triggered by amyloid aggregation Exp. Diabetes Res. 2008 2008
28. S.M. Patil, S. Xu, S.R. Sheftic, and A.T. Alexandrescu Dynamic alpha-helix structure of micelle-bound human amylin J. Biol. Chem. 284 18 2009 11982 11991
29. D.H. Lopes, C. Colin, T.L. Degaki, A.C. de Sousa, M.N. Vieira, A. Sebollela, A.M. Martinez, C. Bloch Jr., S.T. Ferreira, and M.C. Sogayar Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP) J. Biol. Chem. 279 41 2004 42803 42810
30. E.A. Mireck, L. Gremer, S. Schiefer, F. Oesterhelt, M. Stoldt, D. Willbold, and W. Hoyer Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide J. Biotechnol. 2014
31. J.A. Williamson, and A.D. Miranker Direct detection of transient α-helical states in islet amyloid polypeptide Protein Sci. 16 1 2007 110 117
32. Y. Mazor, S. Gilead, I. Benhar, and E. Gazit Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide J. Mol. Biol. 322 5 2002 1013 1024
33. P. Westermark, A. Andersson, and G.T. Westermark Islet amyloid polypeptide, islet amyloid, and diabetes mellitus Physiol. Rev. 91 3 2011 795 826
34. A. Roberts, B. Leighton, J. Todd, D. Cockburn, P. Schofield, R. Sutton, S. Holt, Y. Boyd, A. Day, and E. Foot Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus Proc. Natl. Acad. Sci. 86 24 1989 9662 9666
35. G.J.S. Cooper, A.J. Day, A.C. Willis, A.N. Roberts, K.B.M. Reid, and B. Leighton Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus Biochim. Biophys. Acta - Mol. Cell Res. 1014 3 1989 247 258
36. G. Forloni, E. Lucca, N. Angeretti, P. Della Torre, and M. Salmona Amidation of β-amyloid peptide strongly reduced the amyloidogenic activity without alteration of the neurotoxicity J. Neurochem. 69 5 1997 2048 2054
37. J.A. Williamson, J.P. Loria, and A.D. Miranker Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide J. Mol. Biol. 393 2 2009 383 396
38. Y. Anraku, R. Mizutani, and Y. Satow Protein splicing: its discovery and structural insight into novel chemical mechanisms IUBMB Life 57 8 2005 563 574
39. S. Chong, F.B. Mersha, D.G. Comb, M.E. Scott, D. Landry, L.M. Vence, F.B. Perler, J. Benner, R.B. Kucera, C.A. Hirvonen, J.J. Pelletier, H. Paulus, and M.-Q. Xu Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element Gene 192 2 1997 271 281
40. G.R. Drapeau, Y. Boily, and J. Houmard Purification and properties of an extracellular protease of Staphylococcus aureus J. Biol. Chem. 247 20 1972 6720 6726
41. J. Houmard, and G.R. Drapeau Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds Proc. Natl. Acad. Sci. 69 12 1972 3506 3509
42. C. Cui, W. Zhao, J. Chen, J. Wang, and Q. Li Elimination of in vivo cleavage between target protein and intein in the intein-mediated protein purification systems Protein Expr. Purif. 50 1 2006 74 81
43. J. Marley, M. Lu, and C. Bracken A method for efficient isotopic labeling of recombinant proteins J. Biomol. NMR 20 1 2001 71 75
44. I.R. Cottingham, A. Millar, E. Emslie, A. Colman, A.E. Schnieke, and C. McKee A method for the amidation of recombinant peptides expressed as intein fusion proteins in Escherichia coli Nat. Biotechnol. 19 10 2001 974 977
45. H. Schägger Tricine-SDS-PAGE Nat. Protoc. 1 1 2006 16 22