The stability of β-amyloid precursor protein in nine different cell types

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Abstract

Cell extracts from HeLa, macrophage, glial, C6, PC12, IMR-32, neuroblastoma, CHP-100 and P19 cells were examined for APP and its different derivatives by immunoblotting. When five antibodies (raised against different parts of APP) were used to stain western blots of nine cell extracts, three groups of immunoreactive proteins were observed: high molecular weight- (HMW 70-125 kDa), medium molecular weight- (MMW, 30-40 kDa) and low molecular weight (LMW, 4-16 kDa). The intensity of immunoreactivity among these three groups of proteins varied in each cell line. The strongest signal for HMW protein was observed in PC 12 cells, the strongest signal for MMW protein was observed in C6 astrocyte cells, and both HMW and MMW protein bands were detected in macrophages and P19 cell lines. LMW protein bands could be detected only by antibody against the carboxyl-terminal part of the APP molecule. These experiments suggest that APP is processed differently in the various cell types. The conversion of APP to β-peptide may be related to the stability of APP in cells and the understanding of these intermediate steps of APP processing is crucial to the elucidation of Alzheimer's disease.

Original languageEnglish
Pages (from-to)849-858
Number of pages10
JournalBiochemistry and Molecular Biology International
Volume29
Issue number5
StatePublished - 1993

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Amyloid beta-Protein Precursor
Proteins
Macrophages
Molecular Weight
Molecular weight
Cell Extracts
Cells
Cell Line
Antibodies
Neuroblastoma
Immunoblotting
Neuroglia
Astrocytes
Alzheimer Disease
Coloring Agents
Western Blotting
Derivatives
Peptides
Molecules
Processing

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

The stability of β-amyloid precursor protein in nine different cell types. / Lahiri, Debomoy.

In: Biochemistry and Molecular Biology International, Vol. 29, No. 5, 1993, p. 849-858.

Research output: Contribution to journalArticle

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