Pregledni rad
https://doi.org/10.46419/cvj.57.3.6
Immunohistochemical detection and localisation of prion protein in brain tissue of cattle, sheep and goats
Ivana Kolačko
orcid.org/0009-0003-2209-1126
; Laboratory for Transmissible Spongiform Encephalopathies, Department of Pathological Morphology, Croatian Veterinary Institute, 10000 Zagreb, Croatia
Snježana Zrnčić
orcid.org/0000-0003-4084-5641
; Laboratory for Aquatic Animal Diseases, Department of Pathological Morphology, Croatian Veterinary Institute, 10000 Zagreb, Croatia
Šimun Naletilić
; Laboratory for Pathology, Department of Pathological Morphology, Croatian Veterinary Institute, 10000 Zagreb, Croatia
*
Barbara Iulini
; Veterinary Medical Research Institute for Piedmont, Liguria and the Aosta Valley, Laboratory of Neuropathology, 10154 Turin, Italy
Karmen Branović Čakanić
; Laboratory for Transmissible Spongiform Encephalopathies, Department of Pathological Morphology, Croatian Veterinary Institute, 10000 Zagreb, Croatia
* Dopisni autor.
Sažetak
The misfolding of the cellular prion protein into its pathogenic isoform prion—a proteinaceous infectious particle-causes fatal neurodegenerative diseases. These prion diseases are classified as transmissible spongiform encephalopathies, which may arise from genetic mutations, infectious transmission or sporadic occurrence. They are characterised by protein aggregation and progressive neurodegeneration. In humans, prion diseases include Kuru, Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker-Syndrome, and fatal familial insomnia. In animals, they include atypical and classical scrapie in sheep and goats, atypical and classical bovine spongiform encephalopathy, also known as “mad cow disease”, and chronic wasting disease in cervids. Although the mechanisms underlying neurodegeneration and the role of neuroinflammation in these disorders remain insufficiently understood, characteristic features include spongiform changes, neuronal loss, gliosis, and accumulation of the pathogenic isoform of the prion. To date, there is no reliable ante mortem diagnostic test for these encephalopathies. The diagnosis is confirmed postmortem, and immunohistochemistry is one of the key diagnostic techniques. This review article summarises the available research data about prion diseases, focusing on the detection and localisation of the pathogenic isoform of the prion protein in brain tissue of cattle, sheep, and goats using immunohistochemical analysis.
Ključne riječi
prion; transmissible spongiform encephalopathy; scrapie; bovine spongiform encephalopathy; immunohistochemistry
Hrčak ID:
345263
URI
Datum izdavanja:
15.5.2026.
Posjeta: 582 *