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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
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.
Homozygous state of position 129 in the PRNP is not a risk factor for MSA (show TPO Proteins). No other variants in the PRNP gene were associated with increased risk for MSA (show TPO Proteins)
Transgenic Creutzfeldt-Jakob disease (CJD) mice, expressing the mouse PrP (show C4BPA Proteins) (moPrP) homolog of human PrP (show C4BPA Proteins) 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.
Identified are several nuclear PrP(c) partners, which comprise gamma-catenin (show JUP Proteins), one of its desmosomal partners, beta-catenin (show CTNNB1 Proteins) and TCF7L2 (show TCF7L2 Proteins), the main effectors of the canonical Wnt (show WNT2 Proteins) pathway, and YAP (show YAP1 Proteins), one effector of the Hippo pathway.
Rare mutation in PRNP leading to an exchange of amino acid from glutamic acid (E) to alanine (A) at codon 196 (E196A) is associated with Creutzfeldt-Jacob (show NELF Proteins) disease.
This article discusses a framework for investigating the extended hypothesis that PrPC may be involved in major depression associated with neurodegenerative conditions, with focus on the Transmissible Spongiform Encephalopathies (TSEs, or Prion Diseases) and Alzheimer's Disease (AlzD).
Expert commentary: Computational approaches provide novel insights into prion-like protein functions, their regulation and their role in disease.
The serine/threonine kinase (show TLK2 Proteins) ULK2 (show ULK2 Proteins) binds to and phosphorylates CARMA2sh.
We suggest that reduction of PFN-1 (show PFN1 Proteins) expression by elevated levels of PrP(c) may contribute to protective effects PrP(c)-overexpressing SH-SY5Y cells confer against STS (show STS Proteins)-induced apoptosis
Copper(II) interaction with the Human Prion 103-112 fragment and its mutants has been studied with various techniques. The studied human prion fragment contains both histidine and methionine residues, while methionine residues are systematically replaced or displaced in the studied mutants
these data indicate that the disruption of the PrP(C)-HOP (show STIP1 Proteins) complex could be a potential therapeutic target for modulating the migratory and invasive cellular properties that lead to metastatic Colorectal cancer (CRC (show CALR Proteins)).
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).
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.
Association of human and mouse P-tau with amyloid PrPSc did not diminish survival time following prion infection in these mice. By analogy, human P-tau may not affect prion disease progression in humans.
results suggest that PrP(C) recognizes structural features common to both Abeta (show APP Proteins) oligomers and fibril ends and that this interaction could contribute to the neurotoxic effect of Abeta (show APP Proteins) aggregates.
a simple purification strategy for single tryptophan, single cysteine-containing mutant variants of the mouse prion protein is presented, with yields comparable to that of the wild type protein.
The study presented here further elucidates our understanding of the soluble oligomeric amyloid-beta-Abetao-binding cellular prion protein (PrP(C)) signaling pathway in a familial form of Alzheimer's disease (AD) by implicating PrP(C) as a potential therapeutic target for AD.
The retention of prion protein in the endoplasmic reticulum prevents neuroblastoma (show ARHGEF16 Proteins) cells from proteasome inhibition-induced cytotoxicity.
Data, including data from studies using knockout/transgenic mice, suggest that PrPC is involved in development of insulin (show INS Proteins) resistance and obesity; PrPC knockout mice fed high-fat diet present all the symptoms associated with insulin (show INS Proteins) resistance (hyperglycemia, hyperinsulinemia, and obesity); transgenic mice overexpressing PrPC fed high-fat diet exhibit normal insulin (show INS Proteins) sensitivity and reduced weight gain.
PrP aggresomes are cytosolic overflow deposition centers for the endoplasmic reticulum quality control mechanisms.
recombinant PrP functions as a signaling molecule, and its homophilic interaction with membrane-anchored PrP(C) might promote neurite outgrowth and facilitate growth cone guidance.
single nucleotide polymorphisms (G11A, G615C, G684A, T726G) in the open reading frame of the porcine PRNP gene were found
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
The comparison of the structural stability of prion proteins from the three species rabbit, human and mouse showed that the human and mouse prion protein structures were not affected by the removing the two salt bridges
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.
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.
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 protein (p27-30) (Creutzfeldt-Jakob disease, Gerstmann-Strausler-Scheinker syndrome, fatal familial insomnia)
, prion protein PrP
, Major prion protein
, CARD-containing MAGUK protein 2
, bcl10-interacting maguk protein 2
, card-maguk protein 2
, carma 2
, caspase recruitment domain-containing protein 14
, CD230 antigen
, prion-related protein
, major scrapie-associated fibril protein 1
, prion protein precursor PrP
, prion protein variant a
, prion protein variant b
, prion protein, PrP
, prion protein, structural
, 65-21 protein
, acetylcholine receptor-inducing activity
, major prion protein homolog
, prion-like protein
, glutathione synthetase
, major prion protein preproprotein
, infectious amyloid
, PrP 27-30