Mouse Prnp ( Major prion protein) ELISA Kit

Alpha-synucleinopathies are a group of progressive neurodegenerative disorders, characterized by intracellular deposits of aggregated alpha-synuclein (alpha S). The clinical heterogeneity of these diseases is thought to be attributed to conformers (or strains) of alpha S but the contribution of inclusions in various cell types is unclear. The aim of the present work was to study alpha S conformers among different transgenic (TG) mouse models of alpha-synucleinopathies. To this end, four different TG mouse models were studied (Prnp-h[A53T]alpha S; Thy1-h[A53T]alpha S; Thy1-h[A30P]alpha S; Thy1-m alpha S) that overexpress human or murine alpha S and differed in their age-of-symptom onset and subsequent disease progression. Postmortem analysis of end-stage brains revealed robust neuronal alpha S pathology as evidenced by accumulation of alpha S serine 129 (p-alpha S) phosphorylation in the brainstem of all four TG mouse lines. Overall appearance of the pathology was similar and only modest differences were observed among additionally affected brain regions. To study alpha S conformers in these mice, we used pentameric formyl thiophene acetic acid (pFTAA), a fluorescent dye with amyloid conformation-dependent spectral properties. Unexpectedly, besides the neuronal alpha S pathology, we also found abundant pFTAA-positive inclusions in microglia of all four TG mouse lines. These microglial inclusions were also positive for Thioflavin S and showed immunoreactivity with antibodies recognizing the N-terminus of alpha S, but were largely p-alpha S-negative. In all four lines, spectral pFTAA analysis revealed conformational differences between microglia and neuronal inclusions but not among the different mouse models. Concomitant with neuronal lesions, microglial inclusions were already present at presymptomatic stages and could also be induced by seeded alpha S aggregation. Although nature and significance of microglial inclusions for human alpha-synucleinopathies remain to be clarified, the previously overlooked abundance of microglial inclusions in TG mouse models of alpha-synucleinopathy bears importance for mechanistic and preclinical-translational studies.

Bovine spongiform encephalopathy (BSE) of the cattle is the outstanding disease among other transmissible spongiform encephalopathy (TSEs). It can be transmitted from the cattle to a human and causes a new variant of the Creutzfeldt-Jakob disease (CJD). It is known that prion protein coding gene (PRNP) plays a major role in the TSE susceptibility or resistance in some species. Recent researches demonstrated that the insertion (in) and deletion (del) polymorphisms within promoter and intron 1 region of the PRNP related to BSE susceptibility in cattle. In contrast to cattle, BSE has never been reported in water buffalo; hence, PRNP polymorphisms may be an explanation for buffalo resistance to BSE. The aim of this study was to evaluate allele, genotype, and haplotype frequencies of the PRNP promoter and intron 1 insertion/deletion (indel) polymorphism in healthy Anatolian, Murrah, and Murrah x Anatolian crossbred buffaloes. According to our findings, there were no deletion alleles at two mentioned loci. All studied buffaloes were monomorphic and have carried in/in haplotypes which are considered as the most resistant genotype to BSE.