Abstract
α-Crystallin is a protein that is expressed at high levels in all vertebrate eye lenses. It has a molecular weight of 20 kDa and is composed of two subunits: αA and αB. α-Crystallin is a member of the small heat shock protein (sHsps) family that has been shown to prevent protein aggregation. Small molecules are organic compounds that have low molecular weight (<800 Da). Arginin (Arg) is a small molecule and has been shown to prevent protein aggregation through interaction with partially folded intermediates. In this study, the effect of Arg on the chaperone activity of α-crystallin in the presence of dextran, as a crowding agent, against ordered and disordered aggregation of different target proteins (α-lactalbumin, ovotransferrin, and catalase) has been investigated. The experiments were done using visible absorption spectroscopy, ThT-binding assay, fluorescence spectroscopy, and CD spectroscopy. The results showed that in amorphous aggregation and amyloid fibril formation, both in the presence and absence of dextran, Arg had a positive effect on the chaperone action of α-crystallin. However, in the presence of dextran, the effect of Arg on the chaperone ability of α-crystallin was less than in its absence. Thus, our result suggests that crowding interior media decreases the positive effect of Arg on the chaperone ability of α-crystallin. This is a very important issue, since we are trying to find a mechanism to protect living cells against the toxic effect of protein aggregation.
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Tyco, R. (2000). Current Opinion in Chemical Biology, 4, 500–506.
Wetzel, R. (2002). Structure, 11, 137–138.
Inouye, H., Sharma, D., Goux, W. J., & Kirschner, D. A. (2006). Biophysical Journal, 90, 1774–1789.
Dobson, C. M. (1994). Current Biology, 4, 636–640.
Stefani, M., & Dobson, C. M. (2003). Journal of Molecular Medicine, 81, 678–699.
Dokholyan, N. V. (2006). Current Opinion in Structural Biology, 16, 79–85.
Chiti, F., & Dobson, C. M. (2006). Annual Review of Biochemistry, 75, 333–366.
Flaugh, S. L., Kosinski-Collins, M. S., & King, D. J. (2005). Protein Science, 14, 69–81.
Capaldi, A. P., Kleanthous, C., & Radford, S. E. (2002). Nature Structure & Molecular Biology, 9, 209–216.
Truscott, R. J. W. (2005). Experimental Eye Research, 80, 709–725.
Carver, J. A., Aquilina, J. A., & Truscott, R. J. W. (1994). Experimental Eye Research, 59, 231–234.
Ganea, E. (2001). Current Protein & Peptide Science, 2, 205–255.
Horwitz, J. (2000). Cell & Developmental Biology, 11, 53–60.
Horwitz, J. (2003). Experimental Eye Research, 76, 45–153.
Ingolia, T., & Craig, E. (1982). Proceedings of the National Academy of Sciences, 79, 2360–2364.
Horwitz, J. (1992). Proceedings of the National Academy of Sciences, 89, 10449–10453.
Wang, K., & Spector, A. (2000). European Journal of Biochemistry, 267, 4705–4712.
Xie, Q., Guo, T., Lu, J., & Zhou, H. M. (2004). International Journal of Biochemistry & Cell Biology, 36, 296–306.
Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J. S., & Arakawa, T. (2004). Biotechnology Progress, 20, 1301–1308.
Ecroyed, H., & Carver, J. A. (2008). FEBS Journal, 275, 935–947.
Srinivas, V., Raman, B., Rao, K. S., Ramakrishna, T., & Rao, C. M. (2003). Protein Science, 12, 1262–1270.
Srinivas, V., Raman, B., Rao, K. S., Ramakrishna, T., & Rao, C. H. M. (2005). Molecular Vision, 11, 249–255.
Ghahghaei, A., & Karfarma, A. (2013). Dairy Science & Technology, 93, 177–190.
Ellis, R. J. (2001). Trends in Biochemical Sciences, 26, 597–604.
Ellis, R. J. (2001). Current Opinion in Structural Biology, 11, 114–119.
Minton, A. P. (2001). Journal of Biological Chemistry, 276, 10577–10580.
Garner, M. M., & Burg, M. B. (1994). American Journal of Physics, 266, C877–C892.
Sasahara, K., Macphee, P., & Minton, A. P. (2003). Journal of Molecular Biology, 326, 1227–1237.
Banks, D. S., & Fradin, C. (2005). Biophysics Journal, 89, 2960–2971.
Winzor, D. J., & Wills, P. R. (2006). Biophysical Chemistry, 119, 186–195.
Slingsby, C., & Bateman, O. A. (1990). Experimental Eye Research, 51, 21–26.
Lindner, R. A., Kapur, A., Mariani, M., Stephen, J., Titmuss, S. J., & Carver, J. A. (1998). European Journal of Biochemistry, 258, 170–183.
Raman, B., Ramakrishna, T., & Rao, M. C. (1995). FEBS Letters, 365, 133–136.
Das, B. K., Liang, J. J., & Chakrabarti, B. (1997). Current Eye Research, 16, 303–309.
Smith, J. B., Liu, Y., & Smith, D. L. (1996). Experimental Eye Research, 63, 125–128.
Rao, C. M., Raman, B., Ramakrishna, T., Rajaraman, K., Ghosh, D., Datta, S., Trivedi, V. D., & Sukhaswami, M. B. (1998). International Journal of Biological Macromolecules, 22, 271–281.
Goers, J., Permyakov, S. E., Uversky, V. N., & Fink, L. A. (2002). Biochemistry, 41, 12546–12551.
Ghahghaei, A., Divsalar, A., & Faridi, N. (2010). Protein Journal, 29, 257–264.
Ghahghaei, A., Rekas, A., Price, W. E., & Carver, J. A. (2007). Biochimica et Biophysica Acta, 1774, 102–111.
Swaisgood, H. E. (1992). Advanced dairy chemistry-1: protein (2nd ed., pp. 63–110). London: Elsevier Applied Science.
Pasta, S. Y., Raman, B., Ramakrishna, T., & Rao, C. M. (2002). Journal of Biological Chemistry, 277, 45821–45828.
Ghahghaei, A., & Neyestani, M. (2013). Biologia Section Cell and Molecular Biology, 68, 779–787.
Minton, A. P. (2000). Current Opinion in Structural Biology, 10, 34–39.
Arakawa, T., & Tsumoto, K. (2003). Biochemical and Biophysical Research Communications, 304, 148–152.
Hatters, D. M., Minton, A. P., & Howlett, G. J. (2002). Journal of Biological Chemistry, 227, 7824–7830.
Bova, M. P., Ding, L. L., Horwitz, J., & Fung, B. K. K. (1997). Journal of Biological Chemistry, 272, 29511–29517.
Bova, M. P., Mchaourab, H. S., Han, Y., & Fung, B. K. K. (2000). Journal of Biological Chemistry, 275, 1035–1042.
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Ghahghaei, A., Mohammadian, S. The Effect of Arg on the Structure Perturbation and Chaperone Activity of α-Crystallin in the Presence of the Crowding Agent, Dextran. Appl Biochem Biotechnol 174, 739–750 (2014). https://doi.org/10.1007/s12010-014-1092-y
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DOI: https://doi.org/10.1007/s12010-014-1092-y