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Human PRNP Protein expressed in Human Cells - ABIN2005013
Wang, Tian, Fan, Chen, Lv, Sun, Zhao, Zhang, Wang, Shi, Gao, Chen, Shao, Dong: Polo-like kinase 3 (PLK3) mediates the clearance of the accumulated PrP mutants transiently expressed in cultured cells and pathogenic PrP(Sc) in prion infected cell line via protein interaction. in The international journal of biochemistry & cell biology 2015
This study is the first to demonstrate that tauroursodeoxycholic acid protects MSCs against ER stress via Akt (show AKT1 Proteins)-dependent PrP(C) and Akt (show AKT1 Proteins)-MnSOD (show SOD2 Proteins) pathway.
The stabilization mechanism of specific binding compounds can be summarized as stabilizing both the flexible C-terminal of alpha2 and the hydrophobic core, or only the hydrophobic core, or the overall structure of PrP(C) by high binding affinity. N159 and Q160 play an major role in the specific binding of the studied compounds, all of which interact similarly with L130, P158, N159, Q160,H187, T190, T191.
disease-associated mutations provide valuable insights into possible key structural determinants underlying misfolding of PrPC (review)
This study reports a novel p.S17G mutation in a clinically diagnosed LOAD patient, suggesting that the PRNP mutation is present in Chinese Alzheimer's disease patients, whereas, M129V polymorphism is not a risk factor for Alzheimer's disease or frontotemporal dementia in the Chinese Han population.
Those data indicate that the overexpression of PLK3 (show PLK3 Proteins)-mediated degradation of abnormal PrP (show C4BPA Proteins) is largely dependent on chaperone-mediated autophagy pathway.
biochemical characteristics of valine-to-isoleucine substitution at codon 180 (V180I) in PRNP gene from autopsied brains of patients with genetic Creutzfeldt-Jakob disease; findings indicate abnormal prion proteins in the neocortex are associated with toxicity resulting in severe spongiosis and that V180I is not a polymorphism, but is an authentic pathogenic mutation associated with specific biochemical characteristics
mechanism of the unfolding of the human prion protein
Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages.
the coordination bonds between the Methionine-Lysine-Histidine (Ac-MKH-NHMe) tripeptide model associated with the fifth metal binding site, which triggers the beta-sheet formation of human prion protein and the divalent metal cations such as Mn(2+), Cu(2+) and Zn(2+) were studied.
Importantly, flies expressing human PrP (show C4BPA Proteins) showing a robust eye phenotype will allow performing genetic screens to uncover novel mechanisms mediating PrP (show C4BPA Proteins) neurotoxicity.
Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND (show PRND Proteins)) Variation in Domestic Cattle
Misfolded structures, with nonnative beta-strands formed in the flexible N-terminal domain of PRNP were found in acidic pH simulations.
Genetic characterization of PRNP promoter indel variations and the polymorphism of open reading frames (ORFs) of PRNP and bovine prion-like Shadoo (SPRN (show SPRN Proteins)) genes, are reported.
data showed a differential timing of PrPC expression during early bovine development; the cell-specific expression of PrPC in bovine embryos was revealed to included the developing brain and spinal cord, peripheral nervous system, liver, and mesonephros
The results indicate that certain negative feedback response elements are located in the 5' flanking region and intron1 of the PRNP gene, suggesting that regulation by transcription factors such as Sp1 (show SP1 Proteins) and RP58 (show ZNF238 Proteins) may contribute to the negative feedback mechanism of PRNP.
allele and haplotype segregation at the polymorphic sites within the promoter (23indel) and intron 1 (12indel) regions of the PRNP
PRNP gene variation in Pakistani cattle and buffaloes.
A significant relation between the investigated PRNP indel polymorphisms (23 and 12 bp indels), and susceptibility of Polish Holstein-Friesian cattle to classical bovine spongiform encephalopathy, is reported.
fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow
these results identify a novel PrP(C)-interacting protein KCTD1 (show KCTD1 Proteins) and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).
single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the open reading frame of the porcine PRNP gene were found
Data show the presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.
PrP(c) is expressed in all digestive regions of the rat, monkey, and cow; PrP(c) expressing cells appeared scattered throughout the epithelium of fundic and pyloric glands as well as in intestinal villi and crypts.
study found 8 amino acid residues in rec-PrP that are probably involved in its low susceptibility to misfolding into a protease-resistant isoform; 3 of those residues (S107, M108, and I202) appear to have a stronger influence
fibrils formed by the rabbit protein contain less beta-sheet structure and more alpha-helix structure than those formed by the proteins from human and cow; strong inhibition of fibrillization of the rabbit PrP by the crowded physiological environment and the absence of such a protease-resistant fragment for the rabbit protein could be why rabbits are resistant to prion diseases
Different overall sensitivities of prion protein toward urea denaturation occurs with stabilities in the following species order: hamster = mouse < rabbit < bovine prion protein
amyloid and oxidative stress-related disease proteins like prion protein are increased in expression and form localized accumulations in diabetic muscle in this rabbit model of diabetes.
The salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.
Results describe a single amino acid exchange within the loop, D167S, between mouse and horse prion protein (PrP) which is unique to the PrP sequences of equine species.
The continuous ultrasonication significantly accelerates the nucleations of mPrP and lysozyme (show LYZ Proteins) aggregates by the interaction between monomer and cavitation bubble.
results suggest a plausible theory explaining the apparently contradictory results in the role of the threonine string in PrP conversion and provide novel insights into the complicated relationship among PrP stability, seeded conformational change, and prion structure, which is critical for understanding the molecular basis of prion infectivity.
Findings provide new mechanistic insight into the neuroprotective role for cellular prion protein in adult olfactory sensory epithelium neurogenesis, whereby more mature neurons are stably maintained in animals expressing cellular prion protein.
Furthermore, our finding that a relatively short beta-sheet core of PrP23-144 fibrils (residues approximately 112-139) with a parallel in-register organization of beta-strands is capable of seeding the conversion of full-length prion protein to the infectious form has important implications for the ongoing debate regarding structural aspects of prion protein conversion and molecular architecture of mammalian prions.
NMR spectroscopy experiments demonstrate intramolecular docking between N- and C-terminal domains of Prnp, revealing a novel auto-inhibitory mechanism that regulates its functional activity.
PrP(C) takes part in the cell apparatus controlling Ca(2 (show CA2 Proteins)+) homeostasis, and that PrP(C) is involved in protecting neurons from toxic Ca(2 (show CA2 Proteins)+) overloads.
both gain-of-function and loss-of-function pathogenic mechanisms may be associated with N-terminal domains and may therefore contribute to neurotoxicity in prion disease.
PrP(C) controls the expression of the epidermal growth factor receptor (EGFR (show EGFR Proteins)) downstream from Notch (show NOTCH1 Proteins).
the PRNP octapeptide repeat domain was necessary to promote exosome secretion and to impair the formation of the CAV1-dependent ATG12-ATG5 cytoplasmic complex that drives autophagosome formation.
Transgenic Creutzfeldt-Jakob disease (CJD) mice, expressing the mouse PrP (moPrP) homolog of human PrP D178N/V129 (moPrP D177N/V128), closely reproduce essential features of CJD. The mutant PrPs (show MSMB Proteins) expressed in these mice are misfolded but unable to self-replicate. They accumulate in different compartments of the neuronal secretory pathway, impairing the membrane delivery of ion channels essential for neuronal function.
Findings indicate the molecular mechanisms of prion pathogenesis and strain diversity.
Data indicate that prion protein PrP dimers were funneled into a thermodynamically stable misfolded state along a single pathway containing several intermediates.
Here, we report that the degree of PrP(Sc) protease resistance is highly dependent on the concentration of salt in the solution.
Localization of fully posttranslationally modified Syrian golden hamster glycosylated PrPC is confirmed in the plasma membrane together with the posttranslational glycosylation pattern.
The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that tends to aggregate into rod-like structures. The encoded protein contains a highly unstable region of five tandem octapeptide repeats. This gene is found on chromosome 20, approximately 20 kbp upstream of a gene which encodes a biochemically and structurally similar protein to the one encoded by this gene. Mutations in the repeat region as well as elsewhere in this gene have been associated with Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru. An overlapping open reading frame has been found for this gene that encodes a smaller, structurally unrelated protein, AltPrp. Alternative splicing results in multiple transcript variants.
, major prion protein
, prion-related protein
, prion protein, PrP
, prion protein, structural
, major scrapie-associated fibril protein 1
, prion protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
, prion protein PrP
, prion protein precursor PrP
, prion protein variant a
, prion protein variant b
, 65-21 protein
, acetylcholine receptor-inducing activity
, major prion protein homolog
, prion-like protein
, prion protein
, infectious amyloid
, Major prion protein
, major prion protein preproprotein
, PrP 27-30