지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 1 - 9 (9page)
이용수
초록· 키워드
오류제보하기
Cellular prion protein, a membrane protein, is expressed in all mammals. Prion protein is also found in human blood as an anchorless protein, and this protein form is one of the many potential sources of misfolded prion protein replication during transmission. Many studies have suggested that b-amyloid1–42 oligomer causes neurotoxicity associated with Alzheimer’s disease, which is mediated by the prion protein that acts as a receptor and regulates the hippocampal potentiation. The prevention of the binding of these proteins has been proposed as a possible preventative treatment for Alzheimer’s disease;therefore, a greater understanding of the binding hot-spots between the two molecules is necessary. In this study, the epitope mapping immunoassay was employed to characterize binding epitopes within the prion protein and complementary epitopes in b-amyloid. Residues 23–39 and 93–119 in the prion protein were involved in binding to b-amyloid1–40 and 1–42, and monomers of this protein interacted with prion protein residues 93–113 and 123–166. Furthermore, b-amyloid antibodies against the C-terminus detected bound b-amyloid1–42 at residues 23–40, 104–122 and 159–175. b-Amyloid epitopes necessary for the interaction with prion protein were not determined. In conclusion, charged clusters and hydrophobic regions of the prion protein were involved in binding to b-amyloid1–40 and 1–42. The 3D structure appears to be necessary for b-amyloid to interact with prion protein. In the future, these binding sites may be utilized for 3D structure modeling, as well as for the pharmaceutical intervention of Alzheimer’s disease.
목차
등록된 정보가 없습니다.
참고문헌 (27)
참고문헌 신청
Ahmed M / 2010 / Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils / Nat Struct Mol Biol 17 : 561 ~ 567
Bounhar Y / 2001 / Prion protein protects human neurons against Bax-mediated apoptosis / J Biol Chem 276 : 39145 ~ 39149
Brown DR / 1997 / Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity / Exp Neurol 146 : 104 ~ 112
Brown DR / 2002 / Lack of prion protein expression results in a neuronal phenotype sensitive to stress / J Neurosci Res 67 : 211 ~ 224
Bueler H / 1992 / Normal development and behaviour of mice lacking the neuronal cellsurface PrP protein / Nature 356 : 577 ~ 582
Bounhar Y / 2001 / Prion protein protects human neurons against Bax-mediated apoptosis / J Biol Chem 276 : 39145 ~ 39149
Brown DR / 1997 / Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity / Exp Neurol 146 : 104 ~ 112
Brown DR / 2002 / Lack of prion protein expression results in a neuronal phenotype sensitive to stress / J Neurosci Res 67 : 211 ~ 224
Bueler H / 1992 / Normal development and behaviour of mice lacking the neuronal cellsurface PrP protein / Nature 356 : 577 ~ 582
이 논문의 저자 정보
최근 본 자료
댓글(0)
0