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Immunohistochemical Expression of Caspase 3 and Its Relationship with p53 Expression in Endometrial Cancers  

Lee, Kyung-Enn (Department of Clinical Laboratory Science, College of Health Sciences, Catholic University of Pusan)
Abstract
Apoptosis is an important significance in the pathogenesis of cancer. Caspase 3 and p53 have been identified as important members of the apoptosis related proteins. This study was performed to define roles of caspase 3 expression and its relationship with p53 expression in endometrial cancers by immunohistochemistry. Immunoreactivity for caspase 3 was found in 13 (65.0%) out of 20 endometrial hyperplasia cases and 8 (36.4%) out of 22 endometrial cancers. Seven (87.5%) of the 8 cases with a positive caspase 3 immunoreactivity showed a positive p53 expression in 22 endometrial cancers. There were no significant associations between caspase 3 and p53 expressions. These findings suggest that caspase 3 expression might be associated with carcinogenesis of endometrial cancers. Further studies are needed to define the relationship between caspase 3 and p53 and apoptosis for examining the mechanisms of tissue-specific apoptosis related protein.
Keywords
Caspase 3; p53; Endometrial cancer; Immunohistochemistry;
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1 Miraz A, McGuirk M, Hockenbery TN, Wu Q, Ashar H, Black S. Human surviving is negatively regulated by wild type p53 and participates in p53 dependant apoptotic pathway. Oncogene 2002. 21: 2613-2622.   DOI   ScienceOn
2 Janicke RU, Sprengart ML, Wati MR, Porter AG. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem. 1998. 273: 9357-9360.   DOI
3 Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997. 275: 1132-1136.   DOI   ScienceOn
4 Li YH, Wang C, Meng K, Chen LB, Zhou XJ. Influence of survivin and caspase-3 on cell apoptosis and prognosis in gastric carcinoma. World J Gastroenterol. 2004. 10: 1984-1988.
5 Cha JY, Cho TI, Park TY, So JS, Choi SK, Park ES. Analysis of expression of survivin, caspase 3, and p53 protein in cervical neoplasia comparing with ki-67 index. Korean J Gynecol Oncol. 2008.19: 17-25.   DOI   ScienceOn
6 Vakkala M, Paakko P, Soini Y. Expression of caspases 3, 6 and 8 is increased in parallel with apoptosis and histological aggressiveness of the breast lesion. Br J Cancer. 1999. 81: 592-599.   DOI
7 Sohn JH, Kim DH, Choi NG, Park YE, Ro JY. Caspase-3/CPP32 immunoreactivity and its correlation with frequency of apoptotic bodies in human prostatic carcinomas and benign nodular hyperplasias. Histopathology 2000. 37: 555-560.   DOI   ScienceOn
8 Steven GS, Ronald AD. Principles and practice of surgical pathology and cytopathology. 3rd ed. Baltimore: Churchill Livingstone 1997. 2492-2494.
9 Izban KF, Wrone-Smith T, Hsi ED, Schnitzer B, Quevedo ME, Alkan S. Characterization of the interleukin-1 beta-converting enzyme/ced-3-family protease, caspase-3/CPP32, in Hodgkin's disease: lack of caspase-3 expression in nodular lymphocyte predominance Hodgkin's disease. Am J Pathol. 1999 154: 1439-1447.   DOI
10 Montironi R, Galluzzi CM, Fabris G. Apoptotic bodies in prostate intra-epithelial neoplasia and prostatic adenocarcinoma following total androgen ablation. Pathol Res Pract. 1995. 191: 873-880.   DOI
11 Hsia JY, Chen CY, Chen JT, Hsu CP, Shai SE, Yang SS, Chuang CY, Wang PY, Miaw J. Prognostic significance of caspase-3 expression in primary resected esophageal squamous cell carcinoma. Eur J Surg Oncol. 2003. 29: 4448.
12 Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW, Yuan J. Human ICE/CED-3 protease nomenclature. Cell 1996. 87: 171.   DOI   ScienceOn
13 Hall PA, Lane DP. p53 in tumour pathology: can we trust immunohistochemistry? J Pathol. 1994. 172: 14.
14 Hoshi T, Sasano H, Kato K, Yabuki N, Ohara S, Konno R, Asaki S, Toyota T, Tateno H, Nagura H. Immunohistochemistry of Caspase3/CPP32 in human stomach and its correlation with cell proliferation and apoptosis. Am J Pathol. 1997. 151: 821-829.
15 Chang F, Syrjanen S, Kurvinen K, Sytjanen K. The p53 tumor suppressor gene as a common cellular target in human carcinogenesis. Am J Gastroenterol. 1993. 88: 174-186.
16 Haldar S, Negrini M, Monne M, Sabbioni S, Croce CM. Down-regulation of bcl-2 by p53 in breast cancer cells. Cancer Res. 1994. 54: 2095-2097.