Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles.

Literature DB >> 19322639

Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles.

Abstract

We have studied the interaction of hen egg white lysozyme (HEWL) amyloid fibrils with human erythrocytes and lipid vesicles. The fibrils caused extensive aggregation of human erythrocytes and lipid vesicles without any significant lysis. The membrane activity of HEWL fibrils suggests that the interaction of lysozyme fibrils with cellular membranes could be a contributing factor under disease conditions.

Entities: Gene Species

Mesh：

Substances：

Year: 2009 PMID： 19322639 DOI： 10.1007/s11010-009-0091-8

Source DB: PubMed Journal: Mol Cell Biochem ISSN： 0300-8177 Impact factor: 3.396

43 in total

1. Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.

Authors: C M Yip; J McLaurin
Journal: Biophys J Date: 2001-03 Impact factor: 4.033

2. Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid.

Authors: Cyril C Curtain; Fedá E Ali; Danielle G Smith; Ashley I Bush; Colin L Masters; Kevin J Barnham
Journal: J Biol Chem Date: 2002-11-14 Impact factor: 5.157

3. Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.

Authors: Vladimir Zamotin; Anna Gharibyan; Natalia V Gibanova; Marika A Lavrikova; Dmitry A Dolgikh; Michail P Kirpichnikov; Irina A Kostanyan; Ludmilla A Morozova-Roche
Journal: FEBS Lett Date: 2006-04-07 Impact factor: 4.124

4. Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering.

Authors: Satoru Fujiwara; Fumiko Matsumoto; Yasushige Yonezawa
Journal: J Mol Biol Date: 2003-08-01 Impact factor: 5.469

5. Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.

Authors: Mireille Dumoulin; Janet R Kumita; Christopher M Dobson
Journal: Acc Chem Res Date: 2006-09 Impact factor: 22.384

6. Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes.

Authors: S Jonathan Singer; Nazneen N Dewji
Journal: Proc Natl Acad Sci U S A Date: 2006-01-23 Impact factor: 11.205

Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles.

1. Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.

2. Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid.

3. Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.

4. Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering.

5. Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.

6. Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes.

7. Small-volume extrusion apparatus for preparation of large, unilamellar vesicles.

8. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology.

9. Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association.

10. Lysozyme interactions with phospholipid vesicles: relationships with fusion and release of aqueous content.

1. Prolonged glycation of hen egg white lysozyme generates non amyloidal structures.

2. Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme.