Non-thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: Myoglobin

Journal of Cellular Biochemistry

Volumn 93, Issue 1, 2004, Pages 188-196

  Mancinelli, Fabrizio ^a   Caraglia, Michele ^a   Abbruzzese, Alberto ^a   D'Ambrosio, Guglielmo ^b   Massa, Rita ^b   Bismuto, Ettore ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Frequency domain fluorometry; Microwaves non thermal effects; Protein conformational dynamics; Protein folding, misfolding

Indexed keywords

CELL PROTEIN; MYOGLOBIN; HEME;

ACIDITY; ARTICLE; CRYSTALLOGRAPHY; ELECTROMAGNETIC FIELD; MICROWAVE RADIATION; MOBILE PHONE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; SIGNAL DETECTION; SPECTROSCOPY; ANIMAL; CHEMISTRY; KINETICS; METABOLISM; PROTEIN BINDING; RADIATION EXPOSURE; SPECTROFLUOROMETRY; THERMODYNAMICS; TUNA;

EUKARYOTA; SCOMBRIDAE GEN. SP.;

ANIMALS; CELLULAR PHONE; ELECTROMAGNETIC FIELDS; HEME; KINETICS; MICROWAVES; MYOGLOBIN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TUNA;

EID: 16644370190     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.20164     Document Type: Article

References (52)

1. Adair R. 2002. Vibrational resonances in biological systems at microwave frequencies. Biophys J 82:1147-1152.
2. Alcalà R, Gratton E, Prendergast F. 1987a. Fluorescence lifetime distributions in proteins. Biophys J 51:597-604.
3. Alcalà R, Gratton E, Prendergast F. 1987b. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. Biophys J 51:925-936.
4. Baldwin RL, Rose GD. 1999a. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 24:26-33.
5. Baldwin RL, Rose GD. 1999b. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem Sci 24:77-83.
6. Barrick D, Baldwin RL. 1993. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci 2:869-876.
7. Beechem JM. 1992. Global analysis of biochemical and biophysical data. Methods Enzimol 210:37-54.
8. Bevington PR, Robinson DK. 2003. Data reduction and error analysis for the physical sciences (3rd edn). NY: McGraw-Hill.
9. Bismuto E, Irace G. 1994. Unfolding pathway of apomyoglobin. Simultaneous characterization of acidic conformational states by frequency domain fluorometry. J Mol Biol 241:103-109.
10. Bismuto E, Colonna G, Irace G. 1983. Unfolding pathway of myoglobin. Evidences for a multistep process. Biochemistry 22:4165-4170.
11. Bismuto E, Gratton E, Irace G. 1988. Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin. Biochemistry 27(6):2132-2136.
12. Bismuto E, Sirangelo I, Irace G. 1989. Conformational substrates of myoglobin detected by extrinsic dynamic fluorescence studies. Biochemistry 28:7542-7545.
13. Bismuto E, Gratton E, Sirangelo I, Irace G. 1993. Structure and dynamics of the acidic compact state of apomyoglobin by frequency domain fluorometry. Eur J Biochem 218:213-219.
14. Bismuto E, Irace G, Sirangelo I, Gratton E. 1996. Pressure-induced perturbation of ANS-apomyoglobin complex: Frequency domain fluorescence studies on native and acidic compact states. Protein Sci 5(1):121-126.
15. Bismuto E, Gratton E, Lamb D. 2001. Dynamics of ANS binding to tuna apomyoglobin measured with fluorescence correlation spectroscopy. Biophys J 81:3510-3521.
16. Bismuto E, Mancinelli F, d'Ambrosio G, Massa R. 2003. Are the conformational dynamics and the binding ligand properties of myoglobin affected by exposure to microwave radiation? Eur Biophys J 32:628-634.
17. Bohr H, Bohr J. 2000. Microwave-enhanced folding and denaturation of globular proteins. Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics 61(4 Pt B):4310-4314.
18. Challender RH, Dyer RB, Gilmanshin R, Woodruff WH. 1998. Fast events in protein folding: The time evolution of primary processes. Annu Rev Phys Chem 49:173-202.
19. Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, Dobson CM. 1999. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 96:3590-3594.
20. Colonna G, Irace G, Bismuto E, Servillo L, Balestrieri C. 1983. Structural and functional aspects of the hearth ventricle myoglobin of bluefin tuna. Comp Biochem Physiol 76A:481-485.
21. Creighton TE. 1993. Proteins: Structures and molecular properties. New York: W.H. Freeman & Co.
22. Creighton TE. 1997. How important is the molten globule for correct protein folding? Trends Biochem Sci 22:6-10.
23. De Pomerai D, Daniells C, David H, Allan J, Duce I, Mutwakil M, Thomas D, Sewell P, Tattersall J, Jones D, Candido P. 2000. Non-thermal heat-shock response to microwaves. Nature 405:417-418.
24. De Pomerai DI, Smith B, Dawe A, North K, Smith T, Archer DB, Duce IR, Jones D, Candido EP. 2003. Microwave radiation can alter protein conformation without bulk heating. FEBS Lett 543(1-3):93-97.
25. Dobson CM. 1999. Protein misfolding, evolution, and disease. Trends Biochem Sci 24:329-332.
26. Eliezer D, Yao J, Dyson HJ, Wright PE. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol 5(2):148-155.
27. Englander SW. 2000. Protein folding intermediates and pathways studied by hydrogen exchange. Annu Rev Biophys Biomol Struct 29:213-238.
28. Fink A. 1995. Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24:495-522.
29. Frauenfelder H, Parak F, Young R. 1988. Conformational substates in proteins. Ann Rev Biophys Biophys Chem 17:451-479.
30. French PW, Penny R, Laurence JA, McKenzie DR. 2000. Mobile phones, heat shock proteins and cancer. Differentiation 67:93-97.
31. Goldsmith JR. 1995. Epidemiological evidence of radiofrequency radiation (microwave) effects on health in military, broadcasting, and occupational studies. Int J Occup Eviron Health 1:47-57.
32. Gratton E, Limkeman M. 1983. A continuous variable frequency cross-correlation phase fluorometer with picosecond resolution. Biophys J 44:315-324.
33. Gruebele M. 1999. The fast protein folding problem. Annu Rev Phys Chem 50:485-516.
34. Higashikubo R, Ragouzis M, Moros EG, Straube WL, Roti Roti JL. 2001. Radiofrequency electromagnetic fields do not alter the cell cycle progression of C3H 10T and U87MG cells. Radiat Res 156(6):786-795.
35. Hochstrasser RM, Negus DK. 1984. Picosecond fluorescence decay of tryptophans in myoglobin. Proc Natl Acad Sci USA 81(14):4399-4403.
36. Hyland GJ. 2000. Physics and biology of mobile telephony. Lancet 356:1833-1836.
37. Kalns J, Ryan KL, Mason PA, Bruno JG, Gooden R, Kiel JL. 2000. Oxidative stress precedes circulatory failure induced by 35-GHz microwave heating. Shock 13(1):52-59.
38. Lakowicz JR, Gratton E, Laczko G, Cherek H, Limkeman M. 1984. Analysis of the fluorescence decay kinetics from variable-frequency phase shift and modulation data. Biophys J 46:463-477.
39. Laurence JA, French PW, Lidner RA, McKenzie DR. 2000. Biological effects of electromagnetic fields: Mechanisms for the effects of pulsed microwave radiation on protein conformation. J Theor Biol 206:291-298.
40. Leszczynski D, Joenvaara S, Reivinen J, Kuokka R. 2002. Non-thermal activation of the hsp27/p38MAPK stress pathway by mobile phone radiation in human endothelial cell: Molecular mechanism for cancer and blood-brain barrier-related effects. Differentiation 70:120-129.
41. Malyapa RS, Aherm EW, Bi C. 1998. DNA damage in rat brain cells after in vivo exposure to 2,450 MHz electromagnetic radiation and various methods of euthanasia. Radiat Res 149:637-645.
42. Mashevich M, Folkman D, Kesar A, Barbul A, Korenstein R, Jerby E, Avivi L. 2003. Exposure of human peripheral blood lymphocytes to electromagnetic fields associated with cellular phones leads to chromosomal instability. Bioelectromagnetics 24(2):82-90.
43. Pfeil W. 1998. Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin. Proteins: Structure, Function, and Genetics 30:43-48.
44. Press WH, Flannery BP, Teukolsky WQT. 1989. Numerical recipes in C. Cambridge U.K: Cambridge University Press.
45. Prusiner SB. 1998. Prions. Proc Natl Acad Sci USA 95:13363-13383.
46. Repacholi MH. 2001. Health risks from the use of mobile phones. Toxicol Lett 120:323-331.
47. Rothman KJ. 2000. Epidemiological evidence on health risk of cellular telephones. Lancet 356:1837-1840.
48. Sirangelo I, Malmo C, Casillo M, Mezzogiorno A, Papa M, Irace G. 2002. Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH. J Biol Chem 277(48):45887-45891.
49. Subbiah S. 1996. Protein motions. R.G. Austin, Texas: Landes Company.
50. Teale FW. 1959. Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta 35:543.
51. Youbicier-Simo BJ, Bastide M. 2000. Pathological effects induced by embrionic and postnatal exposure to EMFs radiation by cellular mobile phones. Radiat Protect 1:218-223.
52. Zook BC, Simmens SJ. 2001. The effects of 860 MHz radiofrequency radiofrquency radiation on the induction or promotion of brain tumors and other neoplasms in rats. Radiat Res 155:572-583.