Apoptosis and Cancer: Mutations Relationship within Caspase 2 Genes in Turk Male Patients

  • Dr Orcun İŞLER Selcuk University, Science Faculty, Department of Molecular Biology, 42079 Selçuklu, Konya, Turkey
  • Dr Nesrin TURAÇLAR Vocational School of Health Services, Selcuk University, Konya, Turkey
  • Dr Hasibe Cingilli VURAL Selcuk University, Science Faculty, Department of Molecular Biology, 42079 Selçuklu, Konya, Turkey
Keywords: Apoptosis, caspase, mutation, RT-PCR

Abstract

Introduction: Prostate cancer is the most frequently diagnosed male cancer in developed countries. Prostate cancer is the most common cancer diagnosed among men in Turkey, accounting for 42.5% of all cancer cases in men. It ranks second after lung cancer as the underlying cause of cancer death in Turk men. If cancer is a disease where too little apoptosis occurs there are other diseases where too much apoptosis is thought to be part of the problem. Caspases and apoptotic process very important role in modern cancer treatment.

Material & Methods: For this reason, we study and analyzed 2 exons of the human caspase 2 gene, using a strategy combining RT-PCR amplification and HRM, followed in the second study, considered to investigate the associations between prostate cancer and caspase 2 gene expression and nucleotide sequence analysis in 12 individulas with prostate cancer and healthy persons.

Result: As a result of working, variant-1 and variant-2 of caspase-2 gene mutation was identified in the tissues of the prostate using HRM method. For variant-1, 4 number one mutation was detected in the samples, while for variant-2, 2 numbered examples of mutation has been identified.

Conclusion: According to the statistical evaluation in our study, there was significant difference in CSP2 mutations. At the same time, it has been evaluated with one-to-one correspondence tests whether presence of CSP2 mutation has relationship with the development of any clinical symptoms while diagnostic criteria.

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References

1. Rosenthal, S. A. & Sandler, H. M., Treatment strategies for high-risk locally advanced prostate cancer. Nat. Rev. Urol. 7, 31–38; doi:10.1038/.237, 2010. [PubMed]

2. Xu, J., and the International Consortium for the Prostate Cancer Genetics. Combined analysis of hereditary prostate cancer linkage to 1q24–25: results from the 772 hereditary prostate cancer families from the International Consortium for Prostate Cancer Genetics. Am. J. Hum. Genet., 66: 945–957, 2000. [PubMed]

3. Bowen, C., Voeller, H. J., Kikly, K., Gelmann, E. P. , Synthesis of procaspases-3 and -7 during apoptosis in prostate cancer cells. Cell Death Differ., 6, 394–401, 1999. [PubMed]

4. Bruckheimer, E. M. and Kyprianou, N., Apoptosis in prostate carcinogenesis. A growth regulator and a therapeutic target. Cell Tissue Res., 301, 153–162, 2000. [PubMed]

5. Coffey, R. N., Watson, R. W. and Fitzpatrick, J. M., Signaling for the caspases: their role in prostate cell apoptosis. J Urol., 165, 5–14, 2001. [PubMed]

6. Cote, J. et al. Caspase-2 pre-mRNA alternative splicing: Identification of an intronic element containing a decoy 3’ acceptor site. Proc. Natl. Acad. Sci. U.S.A., 98, 938–943, 2001. [PubMed]

7. Fischer, U. et al., Does caspase inhibition promote clonogenic tumor growth? Cell Cycle, 6, 3048–3053, 2007. [PubMed]

8. Fisher, D. E., Apoptosis in cancer therapy: crossing the threshold. Cell, 78, 539–542, 1994. [PubMed]

9. Salvesen, G.S. Caspases and apoptosis. Essays Biochem. ,38, 9–19, 2002.

10. Hombach-Klonisch, S., Paranjothy, T., Wiechec, E., Pocar, P., Mustafa, T., Seifert, A., Zahl, C., Gerlach, K. L., Biermann, K., Steger, K., Hoang-Vu, C., Schulze-Osthoff, K., Los, M. Cancer stem cells as targets for cancer therapy: selected cancers as examples. Arch. Immunol. Ther. Exp., 56, 165–80, 2008.

11. Jiang, G., Yang, F., Li, M., Weissbecker, K., Price, S., Kim, K. C., La Russa, V. F., Safah, H., Ehrlich, M. Imatinib (ST1571) provides only limited selectivity for CML cells and treatment might be complicated by silent BCR-ABL genes. Cancer Biol. Ther., 2, 103–8, 2003. [PubMed]

12. Jin, S., DiPaola, R. S., Mathew, R., White, E. Metabolic catastrophe as a means to cancer cell death. J. Cell Sci., 120, 379–83. ,2007.

13. Klonisch, T., Wiechec, E., Hombach-Klonisch, S., Ande, S. R., Wesselborg, S., Schulze- Osthoff, K., Los, M., Cancer stem cell markers in common cancers – therapeutic implications. Trends Mol. Med., 14, 450–60, 2008. [PubMed]

14. Kops, G. J., Weaver, B. A., Cleveland, D. W., On the road to cancer: aneuploidy and the mitotic checkpoint. Nat. Rev. Cancer, 5, 773–85, 2005.

15. Read, S. H., Baliga, B. C., Ekert, P. G., Vaux, D. L., Kumar, S., A novel Apaf-1-independent putative caspase-2 activation complex. J. Cell Biol., 159, 739–45, 2002. [PubMed]

16. Toh, W. H. et al., TAp73beta and DNp73beta activate the expression of the pro-survival caspase-2S. Nucleic Acids Res., 36, 4498–4509, 2008. [PubMed]

17. Shi, Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell., 9, 459-470, 2002. [PubMed]

18. Robertson, J. D., Gogvadze, V., Kropotov, A., Vakifahmetoglu, H., Zhivotovsky, B., Orrenius, S., Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity. EMBO Rep., 5, 643–8, 2004.

19. Wu L, Patten N, Yamashiro CT, Chui B., Extraction and amplification of DNA from formalin-fixed, paraffin-embedded tissues. Appl Immunohistochem Mol Morphol. ;10, 269–274. 2002. [PubMed]

20.Faulkner SW, Leigh DA., Universal amplification of DNA isolated from small regions of paraffin-embedded, formalin-fixed tissue. BioTechniques., 24, 47–50, 1998.

21.Wittwer CT, Reed GH, Gundry CN, Vandersteen JG, Pryor RJ., High-resolution genotyping by amplicon melting analysis using LCGreen. Clin Chem. ;49, 853–860, 2003. [PubMed]

22. Wang, Z. B., Liu, Y. Q., Cui, Y. F., Pathways to caspase activation. Cell Biol. Int., 29, 489–96, 2005. [PubMed]

23. Ho LH, Read SH, Dorstyn L, Lambrusco L, Kumar S. Caspase-2 is required for cell death induced by cytoskeletal disruption. Oncogene 27: 3393–3404, 2008. [PubMed]

24. Zhang, Y., Padalecki, S. S., Chaudhuri, A. R., De Waal, E., Goins, B. A., Grubbs, B., Ikeno, Y., Richardson, A., Mundy, G. R., Herman, B., Caspase-2 deficiency enhances aging-related traits in mice. Mech. Ageing Dev., 128, 213–21, 2007. [PubMed]

25. Tinel, A., Tschopp, J., The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science, 304, 843–6, 2004. [PubMed]

26. Fushimi, K. et al. , Up-regulation of the proapoptotic caspase 2 splicing isoform by a candidate tumor suppressor, RBM5. Proc. Natl. Acad. Sci. U.S.A., 105, 15708–15713, 2008. [PubMed]

27. Guo, Y.; Srinivasula, S.M.; Druilhe, A.; Fernandes-Alnemri, T.; Alnemri, E.S. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J. Biol. Chem., 277, 13430–13437, 2002. [PubMed]

28. Stennicke, H. R., Salvesen, G. S., Catalytic properties of the caspases. Cell Death Differ., 6, 1054–9, 1999. [PubMed]

29. Bonzon, C., Bouchier-Hayes, L., Pagliari, L. J. et al., Caspase-2- induced apoptosis requires bid cleavage: a physiological role for bid in heat shockinduced death. Mol. Biol. Cell., 17, 2150–7, 2006.
CITATION
DOI: 10.17511/ijmrr.2015.i1.06
Published: 2015-02-28
How to Cite
1.
İŞLER O, TURAÇLAR N, VURAL HC. Apoptosis and Cancer: Mutations Relationship within Caspase 2 Genes in Turk Male Patients. Int J Med Res Rev [Internet]. 2015Feb.28 [cited 2024Nov.8];3(1):27-4. Available from: https://ijmrr.medresearch.in/index.php/ijmrr/article/view/181
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Original Article