Isolation and Characterization of Novel Presenilin Binding Protein

J Neurochem. 2000 Jul;75(1):109-16. doi: 10.1046/j.1471-4159.2000.0750109.x.

Abstract

Approximately 50% of familial Alzheimer's disease (AD) cases are linked to the presenilin (PS) gene. This suggests that an altered function of mutated PSs accounts for a fundamental process leading to AD. Here we identify a new PS binding protein, PBP, which is highly expressed in cerebral cortex and hippocampus. immunohistochemical studies and cell fractionation analysis show that PBP redistributes from cytoplasm to membranes in the presence of PS. In addition, PBP is deficient in the soluble fraction of sporadic AD brains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism
  • Amino Acid Sequence
  • Animals
  • Blotting, Northern
  • Blotting, Western
  • COS Cells
  • Carrier Proteins / analysis*
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Cell Fractionation
  • Cell Line
  • Cell Membrane / chemistry
  • Cerebral Cortex / chemistry
  • Cerebral Cortex / ultrastructure
  • Cytoplasm / chemistry
  • DNA, Complementary
  • Guanine Nucleotide Exchange Factors*
  • Hippocampus / chemistry
  • Hippocampus / ultrastructure
  • Humans
  • Immunohistochemistry
  • In Situ Hybridization
  • Kidney
  • Membrane Proteins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins*
  • Peptide Fragments / chemistry
  • Presenilin-1
  • Saccharomyces cerevisiae
  • Transfection

Substances

  • Carrier Proteins
  • DNA, Complementary
  • DOCK3 protein, human
  • Dock3 protein, mouse
  • Guanine Nucleotide Exchange Factors
  • Membrane Proteins
  • Nerve Tissue Proteins
  • PSEN1 protein, human
  • Peptide Fragments
  • Presenilin-1