Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2015 (2015), Article ID 379817, 9 pages
http://dx.doi.org/10.1155/2015/379817
Research Article

Implication of Caspase-3 as a Common Therapeutic Target for Multineurodegenerative Disorders and Its Inhibition Using Nonpeptidyl Natural Compounds

1Department of Clinical Nutrition, College of Applied Medical Sciences, University of Ha’il, Ha’il 2440, Saudi Arabia
2Department of Biosciences, Integral University, Lucknow, Uttar Pradesh 226026, India
3School of Biotechnology, Yeungnam University, Gyeongsan 712749, Republic of Korea
4Department of Biotechnology, TERI University, New Delhi 110070, India
5Research and Scientific Studies Unit, College of Nursing & Allied Health Sciences, Jazan University, Jazan 45142, Saudi Arabia
6Department of Biosciences, Jamia Millia Islamia, New Delhi 110025, India

Received 4 March 2015; Revised 13 April 2015; Accepted 14 April 2015

Academic Editor: Yudong Cai

Copyright © 2015 Saif Khan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. L. E. Hebert, L. A. Beckett, P. A. Scherr, and D. A. Evans, “Annual incidence of Alzheimer disease in the United States projected to the years 2000 through 2050,” Alzheimer Disease and Associated Disorders, vol. 15, no. 4, pp. 169–173, 2001. View at Publisher · View at Google Scholar · View at Scopus
  2. L. E. Hebert, P. A. Scherr, J. L. Bienias, D. A. Bennett, and D. A. Evans, “Alzheimer disease in the US population: prevalence estimates using the 2000 census,” Archives of Neurology, vol. 60, no. 8, pp. 1119–1122, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. I. Kanazawa, “How do neurons die in neurodegenerative diseases?” Trends in Molecular Medicine, vol. 7, no. 8, pp. 339–344, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. A. G. Porter and R. U. Jänicke, “Emerging roles of caspase-3 in apoptosis,” Cell Death & Differentiation, vol. 6, no. 2, pp. 99–104, 1999. View at Publisher · View at Google Scholar · View at Scopus
  5. M. E. Nuttall, D. Lee, B. McLaughlin, and J. A. Erhardt, “Selective inhibitors of apoptotic caspases: implications for novel therapeutic strategies,” Drug Discovery Today, vol. 6, no. 2, pp. 85–91, 2001. View at Publisher · View at Google Scholar · View at Scopus
  6. M. G. Grütter, “Caspases: key players in programmed cell death,” Current Opinion in Structural Biology, vol. 10, no. 6, pp. 649–655, 2000. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Fuentes-Prior and G. S. Salvesen, “The protein structures that shape caspase activity, specificity, activation and inhibition,” Biochemical Journal, vol. 384, no. 2, pp. 201–232, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. A. Mohr and R. M. Zwacka, “In situ trapping of initiator caspases reveals intermediate surprises,” Cell Biology International, vol. 31, no. 5, pp. 526–530, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. A. Fleischer, A. Ghadiri, F. Dessauge et al., “Modulating apoptosis as a target for effective therapy,” Molecular Immunology, vol. 43, no. 8, pp. 1065–1079, 2006. View at Publisher · View at Google Scholar · View at Scopus
  10. R. C. Taylor, S. P. Cullen, and S. J. Martin, “Apoptosis: controlled demolition at the cellular level,” Nature Reviews Molecular Cell Biology, vol. 9, no. 3, pp. 231–241, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. C. A. Marques, U. Keil, A. Bonert et al., “Neurotoxic mechanisms caused by the alzheimer's disease-linked Swedish amyloid precursor protein. Mutation oxidative stress, caspases, and the JNK pathway,” The Journal of Biological Chemistry, vol. 278, no. 30, pp. 28294–28302, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. H. R. Stennicke and G. S. Salvesen, “Catalytic properties of the caspases,” Cell Death and Differentiation, vol. 6, no. 11, pp. 1054–1059, 1999. View at Publisher · View at Google Scholar · View at Scopus
  13. P. J. Lakshmi, B. V. S. Suneel Kumar, R. S. Nayana et al., “Design, synthesis, and discovery of novel non-peptide inhibitor of Caspase-3 using ligand based and structure based virtual screening approach,” Bioorganic and Medicinal Chemistry, vol. 17, no. 16, pp. 6040–6047, 2009. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Sharma, A. Basu, and R. K. Agrawal, “Pharmacophore modeling and docking studies on some nonpeptide-based caspase-3 inhibitors,” BioMed Research International, vol. 2013, Article ID 306081, 15 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  15. M. D'Amelio, M. Sheng, and F. Cecconi, “Caspase-3 in the central nervous system: beyond apoptosis,” Trends in Neurosciences, vol. 35, no. 11, pp. 700–709, 2012. View at Publisher · View at Google Scholar · View at Scopus
  16. N. Louneva, J. W. Cohen, L.-Y. Han et al., “Caspase-3 is enriched in postsynaptic densities and increased in Alzheimer's disease,” The American Journal of Pathology, vol. 173, no. 5, pp. 1488–1495, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. L. J. Martin, A. C. Price, A. Kaiser, A. Y. Shaikh, and Z. Liu, “Mechanisms for neuronal degeneration in amyotrophic lateral sclerosis and in models of motor neuron death (review),” International Journal of Molecular Medicine, vol. 5, no. 1, pp. 3–13, 2000. View at Google Scholar · View at Scopus
  18. M. Li, V. O. Ona, C. Guégan et al., “Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model,” Science, vol. 288, no. 5464, pp. 335–339, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. W. Boston-Howes, S. L. Gibb, E. O. Williams, P. Pasinelli, R. H. Brown Jr., and D. Trotti, “Caspase-3 cleaves and inactivates the glutamate transporter EAAT2,” The Journal of Biological Chemistry, vol. 281, no. 20, pp. 14076–14084, 2006. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Hartmann, S. Hunot, P. P. Michel et al., “Caspase-3: a vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 6, pp. 2875–2880, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. N. A. Tatton, “Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson's disease,” Experimental Neurology, vol. 166, no. 1, pp. 29–43, 2000. View at Publisher · View at Google Scholar · View at Scopus
  22. M. Chen, V. O. Ona, M. Li et al., “Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease,” Nature Medicine, vol. 6, no. 7, pp. 797–801, 2000. View at Publisher · View at Google Scholar · View at Scopus
  23. M. Tewari, L. T. Quan, K. O'Rourke et al., “Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase,” Cell, vol. 81, no. 5, pp. 801–809, 1995. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. J. Kim, Y. Yi, E. Sapp et al., “Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 22, pp. 12784–12789, 2001. View at Google Scholar
  25. R. E. Castro, M. M. M. Santos, P. M. C. Glória et al., “Cell death targets and potential modulators in alzheimer's disease,” Current Pharmaceutical Design, vol. 16, no. 25, pp. 2851–2864, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Yamada, K. Kida, W. Amutuhaire, F. Ichinose, and M. Kaneki, “Gene disruption of caspase-3 prevents MPTP-induced Parkinson's disease in mice,” Biochemical and Biophysical Research Communications, vol. 402, no. 2, pp. 312–318, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. S. Toulmond, K. Tang, Y. Bureau et al., “Neuroprotective effects of M826, a reversible caspase-3 inhibitor, in the rat malonate model of Huntington's disease,” British Journal of Pharmacology, vol. 141, no. 4, pp. 689–697, 2004. View at Publisher · View at Google Scholar · View at Scopus
  28. P. Pasinelli and R. H. Brown, “Molecular biology of amyotrophic lateral sclerosis: insights from genetics,” Nature Reviews Neuroscience, vol. 7, no. 9, pp. 710–723, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. J. D. Rothstein, “Current hypotheses for the underlying biology of amyotrophic lateral sclerosis,” Annals of Neurology, vol. 65, no. 1, pp. S3–S9, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Vukosavic, L. Stefanis, V. Jackson-Lewis et al., “Delaying caspase activation by Bcl-2: a clue to disease retardation in a transgenic mouse model of amyotrophic lateral sclerosis,” Journal of Neuroscience, vol. 20, no. 24, pp. 9119–9125, 2000. View at Google Scholar · View at Scopus
  31. R. M. Friedlander, “Apoptosis and caspases in neurodegenerative diseases,” The New England Journal of Medicine, vol. 348, no. 14, pp. 1365–1375, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. D. Szklarczyk, A. Franceschini, M. Kuhn et al., “The STRING database in 2011: functional interaction networks of proteins, globally integrated and scored,” Nucleic Acids Research, vol. 39, no. 1, pp. D561–D568, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. A. Franceschini, D. Szklarczyk, S. Frankild et al., “STRING v9.1: protein-protein interaction networks, with increased coverage and integration,” Nucleic Acids Research, vol. 41, no. 1, pp. D808–D815, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. M. L. Verdonk, J. C. Cole, M. J. Hartshorn, C. W. Murray, and R. D. Taylor, “Improved protein-ligand docking using GOLD,” Proteins: Structure, Function and Genetics, vol. 52, no. 4, pp. 609–623, 2003. View at Publisher · View at Google Scholar · View at Scopus
  35. G. Jones, P. Willett, R. C. Glen, A. R. Leach, and R. Taylor, “Development and validation of a genetic algorithm for flexible docking,” Journal of Molecular Biology, vol. 267, no. 3, pp. 727–748, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. R. Wang, L. Lai, and S. Wang, “Further development and validation of empirical scoring functions for structure-based binding affinity prediction,” Journal of Computer-Aided Molecular Design, vol. 16, no. 1, pp. 11–26, 2002. View at Publisher · View at Google Scholar · View at Scopus
  37. S.-Y. Huang and X. Zou, “An iterative knowledge-based scoring function to predict protein-ligand interactions: II. Validation of the scoring function,” Journal of Computational Chemistry, vol. 27, no. 15, pp. 1876–1882, 2006. View at Publisher · View at Google Scholar · View at Scopus
  38. K. Vanommeslaeghe, E. Hatcher, C. Acharya et al., “STRING v9.1: protein-protein interaction networks, with increased coverage and integration,” Journal of Computational Chemistry, vol. 31, no. 4, pp. 671–690, 2010. View at Publisher · View at Google Scholar · View at Scopus
  39. M. Petersen and M. S. J. Simmonds, “Rosmarinic acid,” Phytochemistry, vol. 62, no. 2, pp. 121–125, 2003. View at Publisher · View at Google Scholar · View at Scopus
  40. F. Shaerzadeh, A. Ahmadiani, M. A. Esmaeili et al., “Antioxidant and antiglycating activities of Salvia sahendica and its protective effect against oxidative stress in neuron-like PC12 cells,” Journal of Natural Medicines, vol. 65, no. 3-4, pp. 455–465, 2011. View at Publisher · View at Google Scholar · View at Scopus
  41. T. Iuvone, D. de Filippis, G. Esposito, A. D'Amico, and A. A. Izzo, “The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-β peptide-induced neurotoxicity,” Journal of Pharmacology and Experimental Therapeutics, vol. 317, no. 3, pp. 1143–1149, 2006. View at Publisher · View at Google Scholar · View at Scopus
  42. R. M. Srivastava, S. Singh, S. K. Dubey, K. Misra, and A. Khar, “Immunomodulatory and therapeutic activity of curcumin,” International Immunopharmacology, vol. 11, no. 3, pp. 331–341, 2011. View at Publisher · View at Google Scholar · View at Scopus
  43. T. Jiang, X.-L. Zhi, Y.-H. Zhang, L.-F. Pan, and P. Zhou, “Inhibitory effect of curcumin on the Al(III)-induced Aβ42 aggregation and neurotoxicity in vitro,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1822, no. 8, pp. 1207–1215, 2012. View at Publisher · View at Google Scholar · View at Scopus
  44. G. Seelinger, I. Merfort, and C. M. Schempp, “Anti-oxidant, anti-inflammatory and anti-allergic activities of luteolin,” Planta Medica, vol. 74, no. 14, pp. 1667–1677, 2008. View at Publisher · View at Google Scholar · View at Scopus
  45. J. Pepping, “Huperzine A,” The American Journal of Health-System Pharmacy, vol. 57, no. 6, pp. 533–534, 2000. View at Google Scholar · View at Scopus
  46. H. Y. Zhang and X. C. Tang, “Neuroprotective effects of huperzine A: new therapeutic targets for neurodegenerative disease,” Trends in Pharmacological Sciences, vol. 27, no. 12, pp. 619–625, 2006. View at Google Scholar