Protein Folding, Misfolding, Aggregation and Their Implications in Human Diseases: Discovering Therapeutic Ways to Amyloid-Associated Diseases

Cell Biochemistry and Biophysics

Volumn 70, Issue 1, 2014, Pages 51-61

  Iram, Afshin ^a   Naeem, Aabgeena ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Amyloids; Fibrils; Genetic; Misfolding; Therapy

Indexed keywords

AMYLOID; PROTEIN AGGREGATE;

CHEMISTRY; GLYCOSYLATION; HOMEOSTASIS; HUMAN; METABOLISM; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES;

AMYLOID; GLYCOSYLATION; HOMEOSTASIS; HUMANS; PROTEIN AGGREGATES; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES;

EID: 84906231542     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-014-9904-9     Document Type: Review

References (60)

1. Onuchic, J. N., & Wolynes, P. G. (2004). Theory of protein folding. Current Opinion in Structural Biology, 14, 70-75.
2. Vyas, N. K., Vyas, M. N., & Quiocho, F. A. (1991). Comparison of the periplasmic receptors for l-arabinose, d-glucose/d-galactose, and d-ribose. Structural and functional similarity. Journal of Biological Chemistry, 266, 5226-5237.
3. Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science, 319, 916-919.
4. Cohen, E., & Dillin, A. (2008). The insulin paradox: Aging, proteotoxicity and neurodegeneration. Nature Reviews Neuroscience, 9, 759-767.
5. Mizushima, N., Levine, B., Cuervo, A., & Klionsky, D. (2008). Autophagy fights disease through cellular self-digestion. Nature, 45, 1069-1075.
6. Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995). Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins, 21, 167-195.
7. Jahn, T. R., & Radford, S. E. (2005). The yin and yang of protein folding. FEBS Journal, 272, 5962-5970.
8. Leopold, P. E., Montal, M., & Onuchic, J. N. (1992). Protein folding funnels: A kinetic approach to the sequence-structure relationship. Proceedings of the National Academy of Sciences of the United States of America, 89, 8721-8725.
9. Doyle, R., Simons, K., Qian, H., & Baker, D. (1997). Local interactions and the optimization of protein folding. Proteins, 29, 282-291.
10. Lindorff-Larsen, K., Rogen, P., Paci, E., Vendruscolo, M., & Dobson, C. M. (2005). Protein folding and the organization of the protein topology universe. Trends in Biochemical Sciences, 30, 13-19.
11. Sinha, K. K., & Udgaonkar, J. B. (2009). Early events in protein folding. Current Science, 96, 1053-1070.
12. Fatima, S., Ahmad, B., & Khan, R. H. (2007). Native-like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH. IUBMB Life, 59, 179-186.
13. Srinivas, V., Raman, B., Rao, K. S., Ramakrishna, T., & Rao, Ch. M. (2005). Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of α-crystallin. Molecular Vision, 11, 249-255.
14. Srimathi, T., Kumar, T. K., Chi, Y. H., Chiu, I. M., & Yu, C. (2002). Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all β-barrel protein. Journal of Biological Chemistry, 277, 747507-747516.
15. Tapan, K. C., & Subhankar, P. (2006). Protein-misfolding diseases and chaperone based therapeutic approaches. FEBS Journal, 2273, 1331-1349.
16. Welch, W. J. (2003). Role of quality control pathways in human diseases involving protein misfolding. Seminars in Cell & Developmental Biology, 15, 31-38.
17. Mogk, A., Tomoyasu, T., Goloubinoff, P., Rudiger, S., Roder, D., Langen, H., et al. (1999). Identification of thermolabile Escherichia coli proteins: Prevention and reservation of aggregation by DnaK and ClpB. EMBO Journal, 18, 6934-6949.
18. Seonga, I. S., Oha, J. Y., Leeab, J. W., Tanakab, K., & Chunga, C. H. (2000). The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli. FEBS Letters, 477, 224-229.
19. Schrimer, E. C., Glover, J. R., Singer, M. A., & Lindquist, S. (1996). HSP100/Clp proteins: A common mechanism explains diverse functions. Trends in Biochemical Sciences, 21, 289-296.
20. Goloubinoff, P., Mogk, A., Zvi, A. P. B., Tomoyasu, T., & Bukau, B. (1999). Sequential mechanism of solubilisation and refolding of stable protein aggregates by a bichaperone network. Proceedings of the National Academy of Sciences of the United States of America, 96, 13732-13737.
21. Wetzel, R. (1994). Mutations and off-pathway aggregation of proteins. Trends in Biotechnology, 12, 193-198.
22. Fink, A. L. (1998). Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Folding and Design, 3, 129-223.
23. Westermark, P., Benson, M. D., Buxbaum, J. N., Cohen, A. S., Frangione, B., Ikeda, S., et al. (2005). Amyloid: Toward terminology clarification. Amyloid, 12, 1-4.
24. Stefani, M., & Dobson, C. M. (2003). Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine, 81, 678-699.
25. Hoang, T. X., Marsella, L., Trovato, A., Seno, F., Banavar, J. R., & Maritan, A. (2006). Common attributes of native-state structures of proteins, disordered proteins, and amyloid. Proceedings of the National Academy of Sciences of the United States of America, 103, 6883-6888.
26. Sunde, M., & Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advances in Protein Chemistry, 50, 123-159.
27. Astbury, W. T., Dickinson, S., & Bailey, K. (1935). The X-ray interpretation of denaturation and the structure of the seed globulins. Biochemical Journal, 29, 2351-2360.
28. Rudall, K. M. (1952). The proteins of the mammalian epidermis. Advances in Protein Chemistry, 7, 253-290.
29. Meredith, S. C. (2005). Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins. Annals of the New York Academy of Sciences, 1066, 181-221.
30. Jenkins, J., & Pickersgill, R. (2001). The architecture of parallel βα-helices and related folds. Progress in Biophysics and Molecular Biology, 77, 111-175.
31. Chan, J. C., Oyler, N. A., Yau, W. M., & Tycko, R. (2005). Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry, 44, 10669-10680.
32. Roher, A. E., Baudry, J., Chaney, M. O., Kuo, Y. M., Stine, W. B., & Emmerling, M. R. (2000). Oligomerization and fibril assembly of the amyloid-β protein. Biochimica et Biophysica Acta, 1502, 31-34.
33. Chaney, M. O., Webster, S. D., Kuo, Y. M., & Roher, A. E. (1998). Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Engineering, 11, 761-767.
34. Stempfer, G., & Rudolph, R. (1996). Improved refolding of a matrixbound fusion protein. Annals of the New York Academy of Sciences, 782, 506-512.
35. Pekar, A. H., & Frank, B. H. (1972). Conformation of proinsulin: A comparison of insulin and proinsulin self-association at neutral pH. Biochemistry, 11, 4013-4016.
36. Alford, J. R., Kendrick, B. S., Carpenter, J. F., & Randolph, T. W. (2007). High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics. Journal of Pharmaceutical Sciences, 97, 3005-3021.
37. Chi, E. Y., Krishnan, S., Randolph, T. W., & Carpenter, J. F. (2003). Physical stability of proteins in aqueous solution: Mechanism and driving forces in non-native protein aggregation. Pharmaceutical Research, 20, 1325-1336.
38. Wang, W. (2005). Protein aggregation and its inhibition in bioinformatics. International Journal of Pharmaceutics, 289, 1-30.
39. Kendrick, B. S., Carpenter, J. F., Cleland, J. L., & Randolph, T. W. (1998). A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma. Proceedings of the National Academy of Sciences of the United States of America, 95, 14142-14146.
40. Krishnan, S., Chi, E. Y., Webb, J. N., Chang, B. S., Shan, D., Goldenberg, M., et al. (2002). Aggregation of granulocytes colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition. Biochemistry, 41, 6422-6431.
41. Hermeling, S., Schellekens, H., Maas, C., Gebbink, M. F., Crommelin, D. J., & Jiskoot, W. (2006). Antibody response to aggregated human interferon alpha 2b in wild type and transgenic immune tolerant mice depends on type and level of aggregation. Journal of Pharmaceutical Sciences, 95, 1084-1096.
42. Chi, E. Y., Weickmann, J., Carpenter, J. F., Manning, M. C., & Randolph, T. W. (2005). heterogenous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation. Journal of Pharmaceutical Sciences, 94, 256-274.
43. Tyagi, A. K., Randolph, T. W., Dong, A., Maloney, K. M., Hitscherich, C., Jr., & Carpenter, J. F. (2008). IgG particle formation during filling pump operation: A case study of heterogenous nucleation on stainless steel nanoparticles. Journal of Pharmaceutical Sciences, 93, 1390-1402.
44. Vlassara, H., Bucala, R., & Striker, L. (1994). Pathogenic effects of advanced glycosylation: Biochemical, biologic, and clinical implications for diabetes and aging. Laboratory Investigation, 70, 138-151.
45. Raj, D. S., Choudhury, D., Welbourne, T. C., & Levi, M. (2000). Advanced glycation end products: a Nephrologist's perspective. American Journal of Kidney Diseases, 35, 365-380.
46. Trueb, B., Fluckiger, R., & Winterhalter, K. H. (1984). Nonenzymatic glycosylation of basement membrane collagen in diabetes mellitus. Collagen and Related Research, 4, 239-251.
47. Cribbs, D. H., Azizeh, B. Y., Cotman, C. W., & LaFerla, F. M. (2000). Fibril formation and neurotoxicity by a herpes simplex virus glycoprotein B fragment with homology to the Alzheimer's A beta peptide. Biochemistry, 39, 5988-5994.
48. Kirpichnikov, D., & Sowers, J. R. (2001). Diabetes mellitus and diabetes-associated vascular disease. Trends in Endocrinology and Metabolism, 12, 225-230.
49. Sakata, N., Imanaga, Y., Meng, J., Tachikawa, Y., Takebayashi, S., Nagai, R., et al. (1999). Increased advanced glycation end products in atherosclerotic lesions of patient with end-stage renal disease. Atherosclerosis, 142, 67-77.
50. Kume, S., Takeya, M., Mori, T., Araki, N., Suzuki, H., Horiuchi, S., et al. (1995). Immunohistochemical and ultrastructural detection of advanced glycation end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody. American Journal of Pathology, 147, 654-667.
51. Schmidt, A. M., Yan, S. D., Wautierand, J. L., & Stern, D. (1999). Activation of receptor for advanced glycation end products: A mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis. Circulation Research, 84, 489-497.
52. Min, C., Kang, E., Yu, S. H., Shinn, S. H., & Kim, Y. S. (1999). Advanced glycation end products induce apoptosis and procoagulant activity in cultured human umbilical vein endothelial cells. Diabetes Research and Clinical Practice, 46, 197-202.
53. Takeuchi, M., Bucala, R., Suzuki, T., Ohkubo, T., Yamazaki, M., Koike, T., et al. (2000). Neurotoxicity of advanced glycation end-products for cultured cortical neurons. Journal of Neuropathology and Experimental Neurology, 59, 1094-1105.
54. Yamagishi, S., Inagaki, Y., Okamoto, T., Amano, S., Koga, K., Takeuchi, M., et al. (2002). Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells. Journal of Biological Chemistry, 277, 20309-20315.
55. Loske, C., Neumann, A., Cunningham, A. M., Nichol, K., Schinzel, R., Riederer, P., et al. (1998). Cytotoxicity of advanced glycation endproducts is mediated by oxidative stress. Journal of Neural Transmission, 105, 1005-1015.
56. Chibber, R., Molinatti, P. A., Rosatto, N., Lambourne, B., & Kohner, E. M. (1997). Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: Relevance to diabetic retinopathy. Diabetologia, 40, 156-164.
57. Hayden, M. R., Tyagi, S. C., Kerklo, M. M., & Nicolls, M. R. (2005). Type 2 diabetes mellitus as a conformational disease. JOP, 6, 287-302.
58. Rousseau, F., Serrano, L., & Schymkowitz, J. W. (2006). How evolutionary pressure against protein aggregation shaped chaperone specificity. Journal of Molecular Biology, 355, 1037-1047.
59. Wang, X., Zhou, Y., Ren, J. J., Hammer, N. D., & Chapman, M. R. (2010). Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis. Proceedings of the National Academy of Sciences of the United States of America, 107, 163-168.
60. Huntington, J. A., & Stein, P. E. (2001). Structure and properties of ovalbumin. Journal of Chromatography B: Biomedical Sciences and Applications, 756, 189-198.