Alzheimer's disease amyloid precursor protein is present in senile plaques and cerebrospinal fluid: Immunohistochemical and biochemical characterization

Jorge Ghiso, Fabrizio Tagliavini, Willem Frederik Timmers, Blas Frangione

Research output: Contribution to journalArticle

Abstract

The amyloid fibrils deposited in cerebral vessel walls and senile plaques in Alzheimer's disease are polymeric forms of a 4 kDa fragment produced by proteolysis of a putative precursor protein (APP). Using antibodies to several fragments of the deduced precursor, we were able to demonstrate the presence of APP in senile plaques, brain extracts and cerebrospinal fluid. Membrane-associated APP is detected as a group of 105-135 kDa proteins while soluble APP is predominantly 105 kDa, does not react with an anti C-terminal antibody, and is 10 kDa shorter than the membrane-bound APP. Amino terminal sequence of the tissue 105 kDa protein indicates that APP begins at residue 18 of the cDNA sequence. These findings imply that i) two forms of APP are detected: membrane-bound and secreted, and ii) APP can be processed in situ.

Original languageEnglish
Pages (from-to)430-437
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume163
Issue number1
DOIs
Publication statusPublished - Aug 30 1989

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Cerebrospinal fluid
Protein Precursors
Amyloid beta-Protein Precursor
Amyloid Plaques
Cerebrospinal Fluid
Alzheimer Disease
Proteolysis
Membranes
Antibodies
Amyloid
Brain
Membrane Proteins
Proteins
Complementary DNA
Tissue

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Alzheimer's disease amyloid precursor protein is present in senile plaques and cerebrospinal fluid : Immunohistochemical and biochemical characterization. / Ghiso, Jorge; Tagliavini, Fabrizio; Timmers, Willem Frederik; Frangione, Blas.

In: Biochemical and Biophysical Research Communications, Vol. 163, No. 1, 30.08.1989, p. 430-437.

Research output: Contribution to journalArticle

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