Journal of Pathology and Translational Medicine

Original Articles

p53, Heat Shock Protein 70 and Topoisomerase II Expression in Gallbladder Carcinoma.: Dae Cheol Kim, Mee Sook Roh, Jin Sook Jeong; Korean J Pathol. 2006;40(6):432-438.

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Abstract PDF: BACKGROUND
The present study was designed to investigate the expression of p53, Heat Shock Protein 70 (HSP70), and Topoisomerase (Topo) II alpha in the preneoplastic lesions and carcinomas of the gallbladder (GB) and to assess the correlation between the expression of these proteins and the clinicopathologic parameters by performing immunohistochemistry.
METHODS
The immunohistochemical expressions of p53, HSP70 and Topo II alpha were evaluated in 38 gallbladder carcinomas and 3 adenomas. Fifteen CIS(s) and 8 dysplasias that were located adjacent to invasive carcinomas were also studied.
RESULTS
A p53 expression was identified in 22 (57.9%) of the 38 GB carcinomas, in 9 (64.3%) of 14 CISs, and in none of the 8 dysplasias and 3 adenomas. A HSP70 expression was found in 11 (29%) of the 38 carcinomas, in 11 (78.6%) of 14 CIS(s), and in 4 (57.2%) of 7 dysplasias. A Topo II alpha expression was present in 36 (94.7%) of the 38 carcinomas, in 13 (92.9%) of 14 CIS(s), in 7 (100%) of 7 dysplasias and in 3 (100%) of 3 adenomas. p53 overexpression was related to the T stage of the primary tumor, while HSP70 and Topo II alpha were not related to any of the clinicopathologic parameters.
CONCLUSION
p53 may be involved in GB carcinogenesis and in the progression of cancer. p53 may be also helpful for making the differential diagnosis between dysplasia and CIS. A further large study is needed to better elucidate the roles of HSP70 and Topo II alpha in GB carcinogenesis.

Expression of Heat Shock Protein 27 and Apoptosis in Renal Cell Carcinomas.: Ghil Suk Yoon; Korean J Pathol. 2006;40(1):39-45.

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Abstract PDF: BACKGROUND
Heat shock protein 27 (HSP27) is induced by heat shock and other pathophysiologic stresses, including neoplastic transformation. We examined the relationship between the HSP27 expression and the clinical and histologic parameters to elucidate the biologic and prognostic significance of HSP27 in renal cell carcinomas (RCCs). Its regulation of apoptosis in RCC development was also observed.
METHODS
We performed immunohistochemical studies for HSP27, caspase 3 and TUNEL on paraffin-embedded tissue microarray specimens from 48 RCCs.
RESULTS
There was a tendency to higher expression of HSP27 in the RCC than in normal renal tubular cells. Of the 48 RCCs, the HSP27 expression was positive in 38 cases. An inverse relationship was found between the Fuhrman nuclear grade and HSP27 expression, but this was without statistical significance (r=-0.218, p=0.093). No relationship between the HSP27 expression and the other parameters was observed. Also, no statistically significant difference was observed between apoptosis and the HSP27 expression more (p=0.951).
CONCLUSIONS
Although HSP27 expression was increased in RCC than in normal renal tubular cell the HSP27 expression may not be a powerful and statistically significant prognostic indicator in patients with RCC.

Immunohistochemical Study of Heat Shock Protein(HSP) and Estrogen Receptor(ER) in the Normal Endometrium and in Adenocarcinoma of the Endometrium.: Hyuni Cho, Aeree Kim, Yung Suk Lee, Han Kyeom Kim, Insun Kim; Korean J Pathol. 1995;29(2):205-211.

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Abstract PDF: Heat shock protein(HSP), first found in the MCF-7 human breast tumor cell line is one of the estrogen-regulated proteins and its synthesis is stimulated by estradiol. In this study, immunohistochemical staining was done for estrogen receptor(ER) and HSP on formalin-fixed, paraffin-embedded tissue sections in twelve normal cyclic and twenty carcinomatous endometria. 1) During the proliferative and early secretary phases, the nuclei of surface and glandular epithelial cells and stromal cells had moderate to strong staining for ER, whereas during the mid and late secretary phases, the glandular epithelial and stromal cells had weak staining for ER. The surface epithelial cells had positive staining of variable intensity. 2) From the early proliferative to mid secretary phases, the glandular and surface epithelial cells showed a positive reaction of variable intensity for HSP. In the late secretary phase, the glandular and surface epithelial cells showed a weak positive or a negative reaction for HSP. During the menstrual cycle, the stromal cells remained negative for HSP. 3) In adenocarcinomas of the endometrium, 8 of 11 (72.7%) well differentiated carcinomas were positive for both ER and HSP, while only 3 of 9(33.3%) moderately and poorly differentiated carcinomas were positive for ER and HSP. In conclusion, ER and estrogen-regulated heat shock protein(HSP) were closely related in normal and carcinomatous endometria and the reactivity was decreased according to poor differentiation.

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