NR AIEP
AU McHattie,S.; Edington,N.
TI Clusterin prevents aggregation of neuropeptide 106-126 in vitro
QU Biochemical and Biophysical Research Communications 1999 Jun 7; 259(2): 336-40
PT journal article
AB 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.
MH Amino Acid Sequence; Animal; Antibodies/immunology; Encephalopathy, Bovine Spongiform/metabolism; Glycoproteins/immunology/*pharmacology; In Vitro; Microscopy, Electron; Molecular Sequence Data; Neuropeptides/chemical synthesis/*chemistry; Peptide Fragments/chemical synthesis/*chemistry; Prions/chemical synthesis/*chemistry; Support, Non-U.S. Gov't
AD Royal Veterinary College, Royal College Street, London, NW1 OTU, United Kingdom.
SP englisch
PO USA