Clusterin prevents aggregation of neuropeptide 106-126 in vitro.
The prion/amyloid neuropeptide 106-126 spontaneously aggregates to form fibrillar structures in vitro. The aggregation in vitro could be prevented in a dose-related manner by clusterin, and the specificity of this action was confirmed by reversal with antibody to clusterin. The relevance of these observations is discussed in relation to previous observations that clusterin and PrPBSE colocalise in naturally occurring cases of BSE.
McHattie
S
S
Royal Veterinary College, Royal College Street, London, NW1 OTU, United Kingdom.
Edington
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D051152:Clusterin; D016643:Encephalopathy, Bovine Spongiform / Q000378:metabolism; D006023:Glycoproteins / Q000276:immunology / Q000494:pharmacology*; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D011328:Prions / Q000138:chemical synthesis / Q000737:chemistry*
D000906:Antibodies; D051152:Clusterin; D006023:Glycoproteins; D018832:Molecular Chaperones; D009479:Neuropeptides; D010446:Peptide Fragments; D011328:Prions; C082632:prion protein (106-126)