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      The Functional Role of Prion Protein (PrP C) on Autophagy

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          Abstract

          Cellular prion protein (PrP C) plays an important role in the cellular defense against oxidative stress. However, the exact protective mechanism of PrP C is unclear. Autophagy is essential for survival, differentiation, development, and homeostasis in several organisms. Although the role that autophagy plays in neurodegenerative disease has yet to be established, it is clear that autophagy-induced cell death is observed in neurodegenerative disorders that exhibit protein aggregations. Moreover, autophagy can promote cell survival and cell death under various conditions. In this review, we describe the involvement of autophagy in prion disease and the effects of PrP C.

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          Most cited references48

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          Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein.

          PrPC is a host protein anchored to the outer surface of neurons and to a lesser extent of lymphocytes and other cells. The transmissible agent (prion) responsible for scrapie is believed to be a modified form of PrPC. Mice homozygous for disrupted PrP genes have been generated. Surprisingly, they develop and behave normally for at least seven months, and no immunological defects are apparent. It is now feasible to determine whether mice devoid of PrPC can propagate prions and are susceptible to scrapie pathogenesis.
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            Molecular biology of prion diseases.

            Prions cause transmissible and genetic neurodegenerative diseases, including scrapie and bovine spongiform encephalopathy of animals and Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker diseases of humans. Infectious prion particles are composed largely, if not entirely, of an abnormal isoform of the prion protein, which is encoded by a chromosomal gene. A posttranslational process, as yet unidentified, converts the cellular prion protein into an abnormal isoform. Scrapie incubation times, neuropathology, and prion synthesis in transgenic mice are controlled by the prion protein gene. Point mutations in the prion protein genes of animals and humans are genetically linked to development of neuro-degeneration. Transgenic mice expressing mutant prion proteins spontaneously develop neurologic dysfunction and spongiform neuropathology. Understanding prion diseases may advance investigations of other neurodegenerative disorders and of the processes by which neurons differentiate, function for decades, and then grow senescent.
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              Autophagy: in sickness and in health.

              The degradation of intracellular components in lysosomes (autophagy) has recaptured the attention of cell biologists in recent years. The main reason for this renewed interest is the dissection of the molecular machinery that participates in this process, because the identification of new intracellular elements involved in autophagy has provided new tools to trace, quantify and manipulate autophagy in a growing number of organisms. As a result, a better understanding of the physiological roles of autophagy, the consequences of its malfunctioning and its participation in different pathological processes has emerged. This article reviews our current knowledge of the role of autophagy in disease and the efforts to reconcile its proposed dual function as both a cell protector and a cell killer.
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                Author and article information

                Journal
                Pathogens
                Pathogens
                pathogens
                Pathogens
                MDPI
                2076-0817
                26 June 2013
                September 2013
                : 2
                : 3
                : 436-445
                Affiliations
                [1 ]Ilsong Institute of Life Science, Hallym University, 1605-4 Gwanyang-dong, Dongan-gu, Anyang, Gyeonggi-do 431-060, Republic of Korea; E-Mails : shilysea@ 123456hallym.ac.kr (H.Y.S.); jmoh76@ 123456hallym.ac.kr (J.M.O.)
                [2 ]Department of Microbiology, College of Medicine, Hallym University, 1 Okcheon-dong, Chuncheon, Kangwon-do 200-702, Republic of Korea
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: yskim@ 123456hallym.ac.kr ; Tel.: +82-31-380-1986; Fax: +82-31-388-3427.
                Article
                pathogens-02-00436
                10.3390/pathogens2030436
                4235692
                25437200
                8af37c14-c674-43da-97e6-fd757257cd91
                © 2013 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 02 May 2013
                : 11 June 2013
                : 18 June 2013
                Categories
                Review

                prion,prnp-deficient,prion diseases,autophagy,autophagic flux,oxidative stress

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