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Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin.
- Source :
- European Journal of Biochemistry; Jun2002, Vol. 269 Issue 11, p2789-2794, 6p
- Publication Year :
- 2002
-
Abstract
- The effect of the extracellular chaperone, clusterin, on amyloid fibril formation by lipid-free human apolipoprotein C-II (apoC-II) was investigated. Sub-stoichiometric levels of clusterin, derived from either plasma or semen, potently inhibit amyloid formation by apoC-II. Inhibition is dependent on apoC-II concentration, with more effective inhibition by clusterin observed at lower concentrations of apoC-II. The average sedimentation coefficient of apoC-II fibrils formed from apoC-II (0.3 mg·mL<superscript>-1</superscript> ) is reduced by coincubation with clusterin (10 µg·mL<superscript>-1</superscript> ). In contrast, addition of clusterin (0.1 mg·mL<superscript>-1</superscript> ) to preformed apoC-II amyloid fibrils (0.3 mg·mL<superscript>-1</superscript> ) does not affect the size distribution after 2 days. This sedimentation velocity data suggests that clusterin inhibits fibril growth but does not promote fibril dissociation. Electron micrographs indicate similar morphologies for amyloid fibrils formed in the presence or absence of clusterin. The substoichiometric nature of the inhibition suggests that clusterin interacts with transient amyloid nuclei leading to dissociation of the monomeric subunits. We propose a general role for clusterin in suppressing the growth of extracellular amyloid. [ABSTRACT FROM AUTHOR]
- Subjects :
- CLUSTERIN
APOLIPOPROTEINS
AMYLOID
PROTEIN folding
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 269
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6755520
- Full Text :
- https://doi.org/10.1046/j.1432-1033.2002.02957.x