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HEAT SHOCK PROTEINS IN BABESIOSIS OF DOGS


Irena Artuković, Ljiljana Bedrica, Josipa Kuleš, Jelena Gotić, Renata Barić Rafaj
HEAT SHOCK PROTEINS IN BABESIOSIS OF DOGS // 8. Međunarodni kongres Veterinarska znanost i struka
Zagreb, Hrvatska, 2019. str. 143-143 (poster, međunarodna recenzija, sažetak, znanstveni)


Naslov
HEAT SHOCK PROTEINS IN BABESIOSIS OF DOGS

Autori
Irena Artuković, Ljiljana Bedrica, Josipa Kuleš, Jelena Gotić, Renata Barić Rafaj

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
8. Međunarodni kongres Veterinarska znanost i struka / - , 2019, 143-143

ISBN
9789538006241

Skup
8th International congress Veterinary science and profession

Mjesto i datum
Zagreb, Hrvatska, 10-12. listopada 2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Heat shock proteins, babesiosis, canine

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Veterinarska medicina



POVEZANOST RADA


Projekt / tema
MZOŠ potpora 2018.

Ustanove
Veterinarski fakultet, Zagreb,
Klinika za traumatologiju