engleski

HEAT SHOCK PROTEINS IN BABESIOSIS OF DOGS

Heat shock proteins (HSPs) have the role of cellular shaperones, responsible for the proper conformation, translocation and degradation of other proteins. Recent discoveries suggest that HSPs have a much wider role outside the cells. Changes in the HSPs expression as well as their location (intra / extracellular) are now associated with the pathogenesis of a wide range of diseases in humans and animals. Serum concentrations of HSP40, HSP60 and TNFα in dogs with babesiosis (n = 18) were measured using ELISA tests and compared to the values in healthy dogs (n = 18). Mann-Whitney test and Spearman's correlation were tested, with significance p <0.05. In babesiosis, HSP60 was increased. A strong correlation show TNFα and HSP40 (r = 0.78) and TNFα and HSP60 (r = 0.82). It is known that increase of HSP60 can be induced by elevation of temperature, oxidative stress and acute inflammatory reaction. All of mentioned occur in babesiosis of dogs and have in common that they disturb the tertiary structure of proteins. Consequently, increased HSP in babesiosis may have a protective role against protein denaturation. While parasites express HSPs when they invade their host, host cells express the same proteins as a defensive mechanism. It seems that the parasite hijacks the host HSPs, because host chaperones have been found in association with proteins of parasitic origin at the erythrocyte membrane, which suggests that host HSPs may facilitate trafficking of proteins of parasitic origin to the erythrocyte surface. Recent studies have shown that HSP60 induce TNF release from macrophages and monocytes. Strong correlation between HSPs and TNFα as inflammatory marker indicate the role of chapperons in acute inflammation in babesiosis. Molecular chapperons have the potential to deliver a clinically relevant diagnostic and therapeutic approaches. The current challenge is to fully understand these networks and establish their clinical potential.

heat shock proteins, babesiosis, canine

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