Proteolytic generation and aggregation of peptides from transmembrane regions:: lung surfactant protein C and amyloid β-peptide

被引:26
作者
Johansson, J
Weaver, TE
Tjernberg, LO
机构
[1] Swedish Univ Agr Sci, Ctr Biomed, Dept Mol Biosci, S-75123 Uppsala, Sweden
[2] Cincinnati Childrens Hosp Med Ctr, Div Pulm Biol, Cincinnati, OH 45229 USA
[3] Karolinska Inst, S-14157 Huddinge, Sweden
[4] Sumitomo Pharmaceut Co Ltd, Alzheimer Ctr, Neurotec, Novum, S-14157 Huddinge, Sweden
关键词
A beta; SP-C; amyloid disease; protein conformation; aggregation;
D O I
10.1007/s00018-003-3274-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The formation of amyloid fibrils is associated with several devastating diseases in humans and animals, including e.g. Alzheimer's disease (AD) and the spongiform encephalopathies. Here, we review and discuss the current knowledge on two amyloid peptides: lung surfactant protein C (SP-C) and the amyloid beta-peptide (Abeta), implicated in human lung disease and in AD, respectively. Both these hydrophobic peptides are derived from the transmembrane region of their precursor protein, and can transit from a monomeric alpha-helical state to a beta-sheet fibril. The alpha helices of SP-C and Abeta are composed of amino acid residues with inherently higher propensities for beta strand than helix conformation. Their helical states are stabilized by a membrane environment, and loss of membrane association thus promotes structural conversion and fibril formation. We speculate that the loss of structural context for sequences with a high propensity for formation of beta sheets may be a common feature of amyloid formation in general.
引用
收藏
页码:326 / 335
页数:10
相关论文
共 103 条
[11]   Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice [J].
Cherny, RA ;
Atwood, CS ;
Xilinas, ME ;
Gray, DN ;
Jones, WD ;
McLean, CA ;
Barnham, KJ ;
Volitakis, I ;
Fraser, FW ;
Kim, YS ;
Huang, XD ;
Goldstein, LE ;
Moir, RD ;
Lim, JT ;
Beyreuther, K ;
Zheng, H ;
Tanzi, RE ;
Masters, CL ;
Bush, AI .
NEURON, 2001, 30 (03) :665-676
[12]   Designing conditions for in vitro formation of amyloid protofilaments and fibrils [J].
Chiti, F ;
Webster, P ;
Taddei, N ;
Clark, A ;
Stefani, M ;
Ramponi, G ;
Dobson, CM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) :3590-3594
[13]   Overexpression of surfactant protein-C mature peptide causes neonatal lethality in transgenic mice [J].
Conkright, JJ ;
Na, CL ;
Weaver, TE .
AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY, 2002, 26 (01) :85-90
[14]   Secretion of surfactant protein C, an integral membrane protein, requires the N-terminal propeptide [J].
Conkright, JJ ;
Bridges, JP ;
Na, CL ;
Voorhout, WF ;
Trapnell, B ;
Glasser, SW ;
Weaver, TE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (18) :14658-14664
[15]   Systematic review: The relation between nutrition and nosocomial pneumonia: randomized trials in critically ill patients [J].
Deborah Cook ;
Bernard De Jonghe ;
Daren Heyland .
Critical Care, 1 (1)
[16]   Understanding the sequence determinants of conformational switching using protein design [J].
Dalal, S ;
Regan, L .
PROTEIN SCIENCE, 2000, 9 (09) :1651-1659
[17]  
Dodart JC, 2000, REV NEUROSCIENCE, V11, P75
[18]   Metal binding and oxidation of amyloid-β within isolated senile plaque cores:: Raman microscopic evidence [J].
Dong, J ;
Atwood, CS ;
Anderson, VE ;
Siedlak, SL ;
Smith, MA ;
Perry, G ;
Carey, PR .
BIOCHEMISTRY, 2003, 42 (10) :2768-2773
[19]   A RIP tide in neuronal signal transduction [J].
Ebinu, JO ;
Yankner, BA .
NEURON, 2002, 34 (04) :499-502
[20]   Reconstitution of γ-secretase activity [J].
Edbauer, D ;
Winkler, E ;
Regula, JT ;
Pesold, B ;
Steiner, H ;
Haass, C .
NATURE CELL BIOLOGY, 2003, 5 (05) :486-488