HSP110 expression in canine mammary gland tumor and its correlation with histopathological classification and grade.

Abstract

Heat shock proteins (HSPs) play critical roles as molecular chaperones, thereby promoting cellular homeostasis. HSPs are overexpressed in many types of human tumors and their serum concentration is elevated in cancer patients. Recent studies have suggested that HSPs may promote tumorigenesis via interactions with tumor-related proteins. There are only a few studies that address the expression of HSPs in canine tumors. In our previous study, we identified elevated levels of HSP110 expression in canine mammary gland tumors (cMGTs). In this study, we examined both serum concentrations and tissue expression of HSP110 in dogs with cMGT. We found that serum HSP110 concentrations were not significantly different in a comparison between dogs with cMGT (3.44 &#xb1; 1.27 &#x3bc;g/mL) and healthy controls (3.23 &#xb1; 1.18 &#x3bc;g/mL). By contrast, significant differences in levels of HSP110 expression were identified in comparisons between simple carcinoma and benign mixed tumor (p = 0.001), simple carcinoma and non-neoplastic lesions (p < 0.001), complex carcinoma and benign mixed tumor (p = 0.015), complex carcinoma and non-neoplastic lesions (p < 0.001), simple adenoma and benign mixed tumor (p = 0.041), and simple adenoma and non-neoplastic lesions (p = 0.007). Similarly, significantly different levels of HSP110 expression were identified when comparing grade &#x2162; with non-neoplastic lesion (p = 0.026), grade &#x2161; with benign tumor (p = 0.015), grade &#x2161; with non-neoplastic lesion (p < 0.001), and grade &#x2160; with non-neoplastic lesion (p < 0.001). Taken together, our results indicate that expression of HSP110 correlates with the malignancy in this cohort of dogs diagnosed with cMGT. These findings also suggest that HSP110 is associated with tumorigenesis and the relative malignancy of cMGT.