Purification and characterization of brain clusterin

Biochem Biophys Res Commun. 1994 Nov 15;204(3):1131-6. doi: 10.1006/bbrc.1994.2580.

Abstract

Clusterin, a 70-80 kDa sulfated glycoprotein found in numerous tissues, is also known as complement lysis inhibitor (CLI), apolipoprotein J, SP-40,40, TRPM-2, and SGP-2. In Alzheimer disease (AD), clusterin mRNA is increased, whereas clusterin protein is found in deposits of beta-amyloid (A beta). These studies characterized clusterin protein from human brain. In extracts from cortex and hippocampus, clusterin was about 40% higher in AD than in controls. Purified clusterin from human brain was slightly smaller than serum clusterin. Brain and serum clusterin were indistinguishable in the inhibition of complement-mediated hemolysis. Both serum and brain clusterin were indistinguishable in inhibiting the aggregation of A beta and promoting oxidative stress in rat pheochromocytoma PC12 cells (MTT assay). The inhibition of A beta aggregation and enhancement of A beta toxicity by clusterin suggest new mechanisms in AD.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alzheimer Disease / metabolism
  • Animals
  • Antibodies, Monoclonal
  • Brain / metabolism*
  • Cerebral Cortex / metabolism
  • Clusterin
  • Complement Inactivator Proteins / isolation & purification*
  • Complement Inactivator Proteins / pharmacology
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Erythrocytes / drug effects
  • Erythrocytes / physiology
  • Gene Expression
  • Glycoproteins / biosynthesis
  • Glycoproteins / isolation & purification*
  • Glycoproteins / pharmacology*
  • Guinea Pigs
  • Hemolysis / drug effects
  • Hippocampus / metabolism
  • Humans
  • Hybridomas
  • Immunoblotting
  • Molecular Chaperones*
  • Molecular Weight
  • RNA, Messenger / biosynthesis
  • Reference Values

Substances

  • Antibodies, Monoclonal
  • CLU protein, human
  • Clusterin
  • Complement Inactivator Proteins
  • Glycoproteins
  • Molecular Chaperones
  • RNA, Messenger