Springer Protocols: Abstract: Radiolabeling of Amyloid-ß Peptides

Radiolabeling of Amyloid-ß Peptides

By: Miguel Calero², Jorge Ghiso³

Abstract

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Nowadays, a wide variety of protocols for labeling proteins is available. However, radiola beling remains one of the most powerful, sensitive and accurate methods to trace and quantitate proteins. Additionally, radiolabeling techniques are steadily gaining importance for diagnosis and treatment in nuclear medicine. There is a considerable number of radioisotopes, but only some are commonly used for basic biomedical research. Among them, the iodine radioisotopes (β-emitters) have several advantages for the labeling of proteins. This chapter focuses on radioiodination protocols for amyloidogenic peptides, using the Aß peptides as a paradigm. The chloramine T, Iodo-Gen®, and lactoperoxidase methods can be successfully applied to radioiodination of different amyloid peptides as long as free tyrosyl (or histidyl) groups are available. However, these methods differ in their yield and the degree of oxidative damage conto labile peptides. When no tyrosines are available, the Bolton-Hunter methodology can be used. The labeling by the tyramine-cellobiose ligand trapping method is applicable to the study of cellular uptake and catabolism of amyloid peptides.

Affiliation(s): (2) Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, Madrid, Spain
(3) Departments of Pathology and Psychiatry, New York University School of Medicine, New York, NY

Book Title: Amyloid Proteins: Methods and Protocols

Series: Methods in Molecular Biology | Volume: 299 | Pub. Date: Dec-28-2004 | Page Range: 325-348 | DOI: 10.1385/1-59259-874-9:325

Subject: Protein Science

Key Words: Amyloids - radiolabeling - chloramine T - lactoperoxidase - iodination - Bolton-Hunter - Iodo-Gen - oxidation - tyramine-cellobiose - ligand-trapping

References

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1.	Meisenhelder, J. and Hunter, J. (1988) Radioactive protein-labeling techniques. Nature 335, 120.

2.	Meisenhelder, J. and Semba, K. (1995) Safe use of radioisotopes, in Current Protocols in Protein Science (Collgan, J. E., Dunn, B. M., Ploegh, H. L., Speicher, D. W., and Wingfield, P. T., eds.). John Wiley & Sons, Inc., New York, pp. A.2B.1–12.

3.	Hunter, W. M. and Greenwood, F. C. (1962) Preparation of iodine-131 labeled human growth hormone of high specific activity. Nature 194, 495–496.

4.	Alberola-Ila, J., Places, L., De La Calle, O., et al. (1991) Stimulation through the TCE-CD3 complex up-regulates the DC2 surface expression on human T lymphocytes. J. Immunol. 146, 1085–1092.

5.	Lederkremer, G. Z. and Lodish, H. F. (1991) An alternatively spliced miniexon alters the subcellular fate of the human asialoglycoprotein receptor H2 subunit. J. Biol. Chem. 266, 1237–1244.

6.	Goding, J. W. (1996) Radiolabelling of monoclonal antibodies, in Monoclonal Antibodies: Principles and Practice (Goding, J. W., ed.). Academic Press, London, pp. 224–228.

7.	Kocisko, D. A., Come, J. H., Priola, S. A., et al. (1994) Cell-free formation of protease-resistant prion protein. Nature 370, 471–474.

8.	Caughey, B., Horiuchi, M., Demaimay, R., and Raymond, J. (1999) Assays of Protease-resistant prion protein and its formation. Methods Enzymol. 309, 122–133.

9.	Esler, W. P., Stimson, E. R., Mantyh, P. W., and Maggio, J. E. (1999) Deposition of soluble amyloid-ß onto amyloid templates: with application for the identification of amyloid fibril extension inhibitors. Methods Enzymol. 309, 350–374.

10.	Maggio, J. E., Stimson, E. R., Ghilardi, J. R., et al. (1992) Reversible in vitro growth of Alzheimer disease beta-amyloid plaques by deposition of labeled amyloid peptide. Proc. Natl. Acad. Sci. USA 89, 5462–5466.

11.	Makover, A., Moriwaki, H., Ramakrishnan, R., Saraiva, M. J. M., Blaner, W. S., and Goodman, D. S. (1988) Plasma transthyretin. Tissue sites of degradation and turnover in the rat. J. Biol. Chem. 263, 8598–8603.

12.	Hutchinson, W. L., Noble, G. E., Hawkins, P. N., and Pepys, M. B. (1994) The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo. J. Clin. Invest. 94, 1390–1396.

13.	Behr, T. M., Gotthardt, M., Becker, W., and Behe, M. (2002) Radioiodination of monoclonal antibodies, proteins and peptides for diagnosis and therapy. A review of standardized, reliable and safe procedures for clinical grade levels kBq to GBq in the Gottingen/Marburg experience. Nuklearmedizin 41, 71–79.

14.	Salacinski, P. R. P., McLean, C., Sykes, J. E. C., Clement-Jones, V. V., and Lowry, P. J.(1981) Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3α,6α-dipenyl glycoluril (IODO-GEN®). Anal. Biochem. 117, 136–146.

15.	Bolton, A. E. and Hunter, W. M. (1973) The labelling of proteins to high specific radioactivities by conjugation to a ¹²⁵I-containing acylating agent. Biochem. J. 133, 529–539.

16.	Zagorski, M. G., Yang, J., Shao, H., Ma, K., Zeng, H., and Hong, A. (1999) Methodological and chemical factors affecting amyloid ß peptide amyloidogenicity. Methods Enzymol. 309, 189–204.

17.	Bailey, G. S. (1996) The chloramine T method for radiolabeling protein, in The Protein Protocols (Walker, J. M., ed.), Humana Press, Totowa, NJ, USA, pp. 665–667.

18.	Fraker, P. J. and Speck, J. C. Jr. (1978) Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3α, 6α-diphenylglycoluril. Biochem. Biophys. Res. Commun. 80, 849–857.

19.	Markwell, M. A. K. and Fox, C. F. (1978) Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1,3,4,6-tetrachloro-3α,6α-diphenylglycoluril. Biochem. 17, 4807–4817.

20.	McClard, R. W. (1981) Removal of sulfhydryl groups with 1,3,4,6-tetrachloro-3α, 6α-diphenylglycoluril: application to the assay of protein in the presence of thiol reagents. Anal. Biochem. 112, 278–281.

21.	Marchalonis, J. J. (1969) An enzymatic method for trace iodination of immunoglobulins and other proteins. Biochem. J. 113, 299–305.

22.	Morrison, M. (1980) Lactoperoxidase catalyzed iododination as a tool for investigation of proteins. Meth. Enzymol. 70, 214–220.

23.	Bailey G. S. (1996) The lactoperoxidase method for radiolabeling protein, in The Protein Protocols (Walker, J. M., ed.), Humana Press, Totowa, NJ, USA, pp. 668–669.

24.	Thompson, J. A., Lau, A. L., and Cunningham, D. D. (1987) Selective radiolabeling of cell surface proteins to a high specific activity. Biochemistry 26, 743–750.

25.	Pittman, R. C., Carew, T. E., Glass, C. K., Green, S. R., Taylor, C. A. Jr., and Attie, A. D. (1983) A radioiodinated, intracellularly trapped ligand for determining the sites of plasma protein degradation in vivo. Biochem. J. 212, 791–800.

26.	Hysing, J. and Tolleshaug, H. (1986) Quantitative aspects of the uptake and degradation of lysozyme in the rat kidney in vivo Bioch. Bioph. Acta 887, 42–50.

27.	Thorpe, S. R. and, Baynes, J. W. (1994) Residualizing glycoconjugates: biologically inert tracers for studies on protein endocytosis and catabolism. Methods Enzymol. 242, 3–17.

28.	Maxwell, J. L., Baynes, J. W., and Thorpe, S. R. (1988) Inulin-¹²⁵I-tyramine, an improved residualizing label for studies on sites of catabolism of circulating proteins. J. Biol. Chem. 263, 14122–14127.

29.	Näslund, J., Karlstrom, A. R., Tjernberg, L. O., Schierhorn, A., Terenius, L., and Nordstedt, C. (1996) High-resolution separation of amyloid ß-peptides: structural variants present in Alzheimer's disease amyloid. J. Neurochem. 67, 294–301.

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