Immunohistochemical evaluation of expression of heat shock proteins HSP70 and HSP90 in mammary gland neoplasms in bitches

Abstract

Heat shock proteins have essential roles in a number of pathophysiologic conditions including carcinogenesis and represent a group of novel molecular markers in cancer management.The aim of this study was to investigate heat shock protein expression in correlation with other neoplasm traits such as: histological type, differentiation grade, proliferative activity, estrogenic receptor expression, and cyclooxygenase-2 and p53 proteins. Material for the investigation comprised 133 tumors of the mammary gland collected from bitches. In total 14 adenomas, 66 complex carcinomas, 47 simple carcinomas and 6 solid carcinomas were collected. Evaluations were conducted with histopathological and immunohistochemical methods using suitable antibodies. Expression of heat shock protein 70 was observed in all types of evaluated neoplasms. A higher average number of cells undergoing expression of heat shock protein 70, which was statistically insignificant, was established in complex and simple cancers and in cancers with the 1 st and the 2 nd degree of histological malignancy. Expression of heat shock protein 90 was observed in all studied neoplasms; it was very insignificant in adenomas, compared to cancers, and the highest expression was established in the solid cancers, as well as in cancers with the 2 nd degree of histological malignancy. This high expression of heat shock protein 90 was correlated with proliferative activity. The results suggest that heat shock protein 90 is involved in canine mammary gland carcinogenesis. The results also suggest that heat shock protein 90 may be a prognostic factor, but this requires detailed clinical confirmation.

Heat shock protein 70 and nitric oxide concentrations in non-tumorous and neoplastic canine mammary tissues: preliminary results – Short communication

“…Our results support the findings of Badowska-Kozakiewicz and Malicka (2012) who reported that the expression of Hsp70 was the lowest in grade III canine mammary carcinomas.…”

“…Moreover, the highest con- centration of these parameters was observed in malignant tumours. There are some reports that the level of Hsp70 expression is significantly elevated in canine mammary tumours (Kumaraguruparan et al, 2006;Romanucci et al, 2006;Badowska-Kozakiewicz and Malicka, 2012); however, there is no information on the concentration of Hsp70 in canine mammary tumours and non-tumorous mammary gland tissues. This fact makes it impossible to compare our results with those reported by other authors.…”

Reproductive System

“…Molecular targets have been investigated to elucidate prognosis or the pathways of tumorigenesis such as CA15.3 and LDH (Campos et al, 2012), Snail (Im et al, 2012), cyclooxygenase-2 (Millanta et al, 2006a), heat-shock proteins (Badowska-Kozakiewicz, 2012;Romanucci et al, 2006), VEGF (Millanta et al, 2006b), p53, BRCA1, c-erbB-2 (Singer et al, 2012, antiapoptotic and proapoptotic proteins (Lana et al, 2007), β-catenin, E-cadherin and adenomatous polyposis coli protein (APC) (Restucci et al, 2007), and connexin (Torres et al, 2005), as well as several proliferation markers such as proliferating cell nuclear antigen (PCNA) and Ki-67 (Lana et al, 2007). Immunocytochemical Ki-67 marker and erythropoietin receptor expression seem to be useful to identify malignant canine tumors and patient poor outcome (Zuccari et al, 2004;Sfacteria et al, 2005).…”

Heat‐shock protein 70 expression in the equine cornea

“…Limitations of the current study include the lack of availability of a species‐specific positive control and that normal equine tissue was obtained from cadaveric globes. Equine mammary tumors are exceedingly rare, limiting access to an established positive control tissue in the horse . One previous study used the primary antibody utilized in this study to evaluate HSP70 expression in equine small intestine; however, the positive control in their staining protocol included human mammary carcinoma .…”