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Effect of poly-L-arginine in inhibiting scrapie prion protein of cultured cells

Title
Effect of poly-L-arginine in inhibiting scrapie prion protein of cultured cells
Author
김진기
Keywords
Poly-L-arginine;; Prion;; PrPC;; PrPSc;; Inhibition; BRANCHED POLYAMINES; POLYARGININE; POLYLYSINE; CONFORMATION; PLASMINOGEN; PROPAGATION; CONVERSION; AGGREGATE; COFACTOR; DISEASE
Issue Date
2017-04
Publisher
SPRINGER
Citation
MOLECULAR AND CELLULAR BIOCHEMISTRY, v. 428, No. 1-2, Page. 57-66
Abstract
Biological 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.
URI
https://link.springer.com/article/10.1007/s11010-016-2916-6http://repository.hanyang.ac.kr/handle/20.500.11754/72020
ISSN
0300-8177; 1573-4919
DOI
10.1007/s11010-016-2916-6
Appears in Collections:
COLLEGE OF PHARMACY[E](약학대학) > PHARMACY(약학과) > Articles
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