The Thr183Ala Mutation, Not the Loss of the First Glycosylation Site, Alters the Physical Properties of the Prion Protein.
作者： Sabina Capellari , Syed IA Zaidi , Amy C Long , Eunice E Kwon , Robert B Petersen
关键词: Prion protein 、 Pathogenic mutation 、 Intracellular retention 、 Biochemistry 、 Residue (chemistry) 、 Phenotype 、 Glycosylation 、 Mutant protein 、 Chemistry 、 Glycan
摘要: The abnormal form of the prion protein has increased resistance to protease digestion and is insoluble in non-ionic detergents. normal modified by non-obligatory addition two N-linked glycans. One pathogenic mutation, Thr Ala at residue 183 human protein, blocks first glycan Asp 181. This mutation been reported result intracellular retention mutant its acquisition properties, presumably due lack glycan. We report that 181 not responsible for block transport or pathogen-like rather, itself probable cause phenotype.
elsevier.com
sci-hub.se 参考文章(14)
D. A. Kocisko, S. A. Priola, G. J. Raymond, B. Chesebro, P. T. Lansbury, B. Caughey, Species specificity in the cell-free conversion of prion protein to protease-resistant forms : A model for the scrapie species barrier Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 3923- 3927 ,(1995) , 10.1073/PNAS.92.9.3923
HANS A. KRETZSCHMAR, LINDA E. STOWRING, DAVID WESTAWAY, WILLIAM H. STUBBLEBINE, STANLEY B. PRUSINER, STEPHEN J. DEARMOND, Molecular cloning of a human prion protein cDNA. DNA (Mary Ann Liebert, Inc.). ,vol. 5, pp. 315- 324 ,(1986) , 10.1089/DNA.1986.5.315
Ricardo Nitrini, Sergio Rosemberg, Maria Rita Passos-Bueno, Lu�s S. Teixeira da Silva, Paula Iughetti, Maria Papadopoulos, Paulo M. Carrilho, Paulo Caramelli, Steffen Albrecht, Mayana Zatz, Andrea LeBlanc, Familial spongiform encephalopathy associated with a novel prion protein gene mutation Annals of Neurology. ,vol. 42, pp. 138- 146 ,(1997) , 10.1002/ANA.410420203
Susanne Liemann, Rudi Glockshuber, Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry. ,vol. 38, pp. 3258- 3267 ,(1999) , 10.1021/BI982714G
Mark Rogers, Albert Taraboulos, Michael Scott, Darlene Groth, Stanley B. Prusiner, Intracellular accumulation of the cellular prion protein after mutagenesis of its Asnlinked glycosylation sites Glycobiology. ,vol. 1, pp. 101- 109 ,(1990) , 10.1093/GLYCOB/1.1.101
Neil Stahl, Michael Baldwin, Rolf Hecker, Keh-Ming Pan, Alma Burlingame, Stanley Prusiner, Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry. ,vol. 31, pp. 5043- 5053 ,(1992) , 10.1021/BI00136A600
Tamao Endo, Darlene Groth, Stanley B. Prusiner, Akira Kobata, Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry. ,vol. 28, pp. 8380- 8388 ,(1989) , 10.1021/BI00447A017
Sylvain Lehmann, David A. Harris, Blockade of Glycosylation Promotes Acquistion of Scrapie-like Properties by the Prion Protein in Cultured Cells Journal of Biological Chemistry. ,vol. 272, pp. 21479- 21487 ,(1997) , 10.1074/JBC.272.34.21479
A. Taraboulos, M. Rogers, D. R. Borchelt, M. P. McKinley, M. Scott, D. Serban, S. B. Prusiner, Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 87, pp. 8262- 8266 ,(1990) , 10.1073/PNAS.87.21.8262
Neena Singh, Gianluigi Zanusso, Shu G. Chen, Hisashi Fujioka, Sandra Richardson, Pierluigi Gambetti, Robert B. Petersen, Prion Protein Aggregation Reverted by Low Temperature in Transfected Cells Carrying a Prion Protein Gene Mutation Journal of Biological Chemistry. ,vol. 272, pp. 28461- 28470 ,(1997) , 10.1074/JBC.272.45.28461