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Parkinson's disease is the second most common neurodegenerative disease which affects almost 1% of the population above the age of 60. It is is characterized by loss of dopaminergic neurons in the striatum and substantia nigra, coupled with the formation of intracellular Lewy bodies in degenerating neurons. Recent evidence suggests endoplasmic reticulum stress as a common and prominent occurrence in the progression of Parkinson's disease pathogenesis in the affected human brain. One of the cellular defense mechanism to combat endoplasmic reticulum stress due to excessive protein accumulation is through activation of the unfolded protein response pathway. In this review we focus on the impact and role of this unfolded protein response as a causative factor of Parkinson's disease leading to neurodegeneration.
Cell death is an essential event in normal life and development, as well as in the pathophysiological processes that lead to disease. It has become clear that each of the main cellular organelles can participate in cell death signalling pathways, and recent advances have highlighted the importance of the endoplasmic reticulum (ER) in cell death processes. In cells, the ER functions as the organelle where proteins mature, and as such, is very responsive to extracellular-intracellular changes of environment. This short overview focuses on the known pathways of programmed cell death triggering from or involving the ER.
The response of five positive acute phase proteins (APP) was evaluated in pigs after infection with Bordetella bronchiseptica (Bbr). Twelve piglets from a herd with high health status were used. Six of them were infected intranasally with Bbr (3.4 x 10⁸ cfu). The standard bacteriological methods and PCR were used for detection of Bbr in nasal swabs, lungs, and bronchoalveolar fluids. Serum APP concentrations were measured using commercial tests. Various kinetics of response was identified within the APP tested. C-reactive protein and serum amyloid A was characterised as a ven fast, transient responder, while haptoglobin as a fast and very prolonged responder. Pig major acute phase protein was characterised as a fast, protracted responder. Alfa-l-acid-glycoprotein did not respond significantly after inoculation. No correlations were found between levels of APP in serum and changes in the turbinates. On the basis of the investigation we cannot state that evaluation of APP concentrations in serum may provide useful information about severity of atrophic rhinitis. However, the concentration of most investigated APP increased after inoculation. Thus, APP measurement could be the primary screening test prior to specific disease diagnosis. "APP-high" animals may be chosen next for pathogen-specific diagnostics. Moreover, monitoring of serum APP concentrations may be useful for selecting clinically healthy pigs before integration into an uninfected herd.
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