Plasminogen

Mays, Charles E.; Ryou, Chongsuk

doi:10.4161/pri.5.1.14460

Cited by 14 publications

(12 citation statements)

References 42 publications

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“…After infection with sheep PrPsc, both PrPc and PrPsc are released into the extracellular environment where they are associated with exosomes [49]. Plasminogen markedly stimulates propagation of the PrPsc format in a dose-dependent manner by increasing the rate of generation of this transmissible agent [50].…”

Section: Transport Of Prpsc From Infected To Uninfected Tissuesmentioning

confidence: 99%

Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?

Prasad¹,

Bondy

2019

CAS

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Prion diseases are a group of incurable infectious terminal neurodegenerative diseases caused by the aggregated misfolded PrPsc in selected mammals including humans. The complex physical interaction between normal prion protein PrPc and infectious PrPsc causes conformational change from the α- helix structure of PrPc to the β-sheet structure of PrPsc, and this process is repeated. Increased oxidative stress is one of the factors that facilitate the conversion of PrPc to PrPsc. This overview presents evidence to show that increased oxidative stress and inflammation are involved in the progression of this disease. Evidence is given for the participation of redoxsensitive metals Cu and Fe with PrPsc inducing oxidative stress by disturbing the homeostasis of these metals. The fact that some antioxidants block the toxicity of misfolded PrPc peptide supports the role of oxidative stress in prion disease. After exogenous infection in mice, PrPsc enters the follicular dendritic cells where PrPsc replicates before neuroinvasion where they continue to replicate and cause inflammation leading to neurodegeneration. Therefore, reducing levels of oxidative stress and inflammation may decrease the rate of the progression of this disease. It may be an important order to reduce oxidative stress and inflammation at the same time. This may be achieved by increasing the levels of antioxidant enzymes by activating the Nrf2 pathway together with simultaneous administration of dietary and endogenous antioxidants. It is proposed that a mixture of micronutrients could enable these concurrent events thereby reducing the progression of human prion disease.

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Section: Transport Of Prpsc From Infected To Uninfected Tissuesmentioning

confidence: 99%

Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?

Prasad¹,

Bondy

2019

CAS

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“…Importantly, PrPsc generated by PMCA is infectious when inoculated to wild type animals [39,41,42]. PMCA allows studies on genotypic and species barrier of prion transmission [44,45,46,47,48,49,50,51,52], the detection of PrPsc in various biological fluids (blood, urine, saliva, LCR) [53,54,55,56,57,58], de novo generation of prions [59,60,61], and the identification of cofactors involved in PrP conversion [59,61,62,63,64,65,66,67,68,69,70,71,72,73]. To overcome some of the above-mentioned issues specific to cellular models, and to assess whether strain tropism can be studied in an acellular system, we recently developed a region-specific PMCA (rsPMCA) [46].…”

Section: Acellular Models Of Prion Strain Tropismmentioning

confidence: 99%

In vitro Modeling of Prion Strain Tropism

Levavasseur

Privat

Haı̈k

2019

Viruses

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Prions are atypical infectious agents lacking genetic material. Yet, various strains have been isolated from animals and humans using experimental models. They are distinguished by the resulting pattern of disease, including the localization of PrPsc deposits and the spongiform changes they induce in the brain of affected individuals. In this paper, we discuss the emerging use of cellular and acellular models to decipher the mechanisms involved in the strain-specific targeting of distinct brain regions. Recent studies suggest that neuronal cultures, protein misfolding cyclic amplification, and combination of both approaches may be useful to explore this under-investigated but central domain of the prion field.

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“…Under physiological conditions, the presence of a cellular factor for prion formation in the host cannot be entirely ruled out. Because biological macromolecules, including sulfated glycosaminoglycan and specific nucleic acids, can not only interact with PrP C but can also lead to efficient proteinase-resistant PrP (PrP res ) formation in vitro , several molecules have been considered as candidate catalysts for PrP conversion in the host [ 7 , 8 , 9 , 10 , 11 ]. These possible interaction-partners of PrP C have been called protein X and, furthermore, PrP C contains discontinuous structure, the loop (residue 165–171) and carboxy-terminus of helix C, to which protein X could bind [ 12 ].…”

Section: Prion Diseasesmentioning

confidence: 99%

“…Potentially, components of ERVs may act as cofactors to enhance prion conversion, and this hypothesis is supported by the previous finding that retroviral sequences co-sediment with infectivity in scrapie. For example, small, highly structured RNAs were shown to have the capacity to participate in the conversion of human recombinant PrP Sen to PrP res [ 63 ], and RNA molecules were shown to stimulate prion protein conversion [ 11 , 64 ]. In addition, a recent study showed that co-infection of small-ruminant lentiviruses and PrP Sc significantly enhanced PrP Sc accumulation within cells [ 65 ].…”

Section: Endogenous Retroviruses In Prion Diseasesmentioning

confidence: 99%

Involvement of Endogenous Retroviruses in Prion Diseases

et al. 2013

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For millions of years, vertebrates have been continuously exposed to infection by retroviruses. Ancient retroviral infection of germline cells resulted in the formation and accumulation of inherited retrovirus sequences in host genomes. These inherited retroviruses are referred to as endogenous retroviruses (ERVs), and recent estimates have revealed that a significant portion of animal genomes is made up of ERVs. Although various host factors have suppressed ERV activation, both positive and negative functions have been reported for some ERVs in normal and abnormal physiological conditions, such as in disease states. Similar to other complex diseases, ERV activation has been observed in prion diseases, and this review will discuss the potential involvement of ERVs in prion diseases.

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Plasminogen

Cited by 14 publications

References 42 publications

Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?

Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?

In vitro Modeling of Prion Strain Tropism

Involvement of Endogenous Retroviruses in Prion Diseases

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