Heat shock proteins (HSPs) function as
molecular chaperones in the regulation of protein folding, conformation, and assembly; in addition, they also protect cells from
protein-
protein aggregation resulting from cellular stress. Recently, HSPs were shown to be overexpressed in several human
cancer cells compared with normal cells. HSPs are considered to be related to apoptosis-associated
proteins, and inhibition of apoptosis promotes
tumor growth. Canine mammary gland
tumors have received a great deal of attention from researchers due to the many common
biological and histological characteristics that they share with human
tumors. We previously confirmed that HSP110 is a canine mammary gland
tumor antigen and reported that HSP110
mRNA expression significantly increased in
tumor tissue. We have now created a functional recombinant canine HSP110
protein and a rabbit anti-HSP110 polyclonal antibody. This
recombinant protein can refold heat-denatured
firefly luciferase at 42°C. Immunohistochemical analysis showed that HSP110 was mainly localized in the cytoplasm of epithelial and interstitial cells in canine mammary gland
tumors. Extensive genomic research has revealed genetic similarities between humans and dogs; comparative oncological studies between these species have made remarkable progress. The results reported here contribute valuable oncological knowledge for the development of novel therapeutic methods in both veterinary science and human medicine.