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dc.contributor.author김진기-
dc.date.accessioned2018-06-12T00:43:26Z-
dc.date.available2018-06-12T00:43:26Z-
dc.date.issued2017-04-
dc.identifier.citationMOLECULAR AND CELLULAR BIOCHEMISTRY, v. 428, No. 1-2, Page. 57-66en_US
dc.identifier.issn0300-8177-
dc.identifier.issn1573-4919-
dc.identifier.urihttps://link.springer.com/article/10.1007/s11010-016-2916-6-
dc.identifier.urihttp://repository.hanyang.ac.kr/handle/20.500.11754/72020-
dc.description.abstractBiological effect of poly-L-arginine (PLR), the linear homopolymer comprised of L-arginine, was investigated to determine the activity of suppressing prions. PLR decreased the level of scrapie prion protein (PrPSc) in cultured cells permanently infected with prions in a concentration-dependent manner. The PrPSc inhibition efficacy of PLR was greater than that of another prion-suppressant poly-L-lysine (PLK) in a molecular mass-dependent fashion. The effective concentration of PLR to inhibit prions was achieved safely below the cytotoxic concentrations, and overall cytotoxicity of PLR was similar to that of PLK. PLR did not alter the cellular prion protein -(PrPC) level and was unable to change the states of preformed recombinant PrP aggregates and PrPSc from prion-infected cells. These data eliminate the possibility that the action mechanism of PLR is through removal of PrPC and pre-existing PrPSc. However, PLR formed complexes with plasminogen that stimulates prion propagation via conversion of PrPC to the misfolded isoform, PrPSc. The plasminogen-PLR complex demonstrated the greater positive surface charge values than the similar complex with PLK, raising the possibility that PLR interferes with the role of cofactor for PrPSc generation better than PLK.en_US
dc.description.sponsorshipThis research was supported by the grants of the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI) funded by the Ministry of Health and Welfare, Republic of Korea (HI16C1085, HI16C0965) and the National Research Foundation of Korea (2012R1A1A2043356).en_US
dc.language.isoen_USen_US
dc.publisherSPRINGERen_US
dc.subjectPoly-L-arginine;en_US
dc.subjectPrion;en_US
dc.subjectPrPC;en_US
dc.subjectPrPSc;en_US
dc.subjectInhibitionen_US
dc.subjectBRANCHED POLYAMINESen_US
dc.subjectPOLYARGININEen_US
dc.subjectPOLYLYSINEen_US
dc.subjectCONFORMATIONen_US
dc.subjectPLASMINOGENen_US
dc.subjectPROPAGATIONen_US
dc.subjectCONVERSIONen_US
dc.subjectAGGREGATEen_US
dc.subjectCOFACTORen_US
dc.subjectDISEASEen_US
dc.titleEffect of poly-L-arginine in inhibiting scrapie prion protein of cultured cellsen_US
dc.typeArticleen_US
dc.relation.no1-2-
dc.relation.volume428-
dc.identifier.doi10.1007/s11010-016-2916-6-
dc.relation.page57-66-
dc.relation.journalMOLECULAR AND CELLULAR BIOCHEMISTRY-
dc.contributor.googleauthorWaqas, Muhammad-
dc.contributor.googleauthorLee, Hye-Mi-
dc.contributor.googleauthorKim, Jeeyoung-
dc.contributor.googleauthorTelling, Glenn-
dc.contributor.googleauthorKim, Jin-Ki-
dc.contributor.googleauthorKim, Dae-Hwan-
dc.contributor.googleauthorRyou, Chongsuk-
dc.relation.code2017000412-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF PHARMACY[E]-
dc.sector.departmentDEPARTMENT OF PHARMACY-
dc.identifier.pidjinkikim-
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COLLEGE OF PHARMACY[E](약학대학) > PHARMACY(약학과) > Articles
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