Apoptosis induced by β-amyloid25-35 in acetylcholinesterase-overexpressing neuroblastoma cells

Hai Yan Zhang, William Stephen Brimijoin, Xi Can Tang

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

AIM: To examine the relationship between apoptosis induced by β-amyloid fragment 25-35 (Aβ25-35) and the activity of acetylcholinesterase (AChE) in AChE over-expresser-SC42 cells. METHODS: Cell survival was measured by microscopy and MTT reduction; DNA laddering was observed by electrophoresis; AChE activity was determined by spectrophotometry. RESULTS: Aβ25-35 1 μmol/L exposure for 24-48 h caused a significant decrease in cell viability, along with changes in morphology and DNA fragmentation. AChE activity was affected in an inverse manner, increasing gradually to a level that was 1.7-fold higher than control at the 48-h time point. No change in the cytotoxicity of Aβ25-35 was observed when the increased AChE activities were effectively inhibited by huperzine A throughout the 48-h exposure period. CONCLUSION: Although Aβ 25-35 can induce apoptosis in SC42 cells and simultaneously increase AChE activity, the capacity of AChE to hydrolyze acetylcholine is not involved in this apoptosis model.

Original languageEnglish (US)
Pages (from-to)853-958+948
JournalActa Pharmacologica Sinica
Volume24
Issue number9
StatePublished - Sep 1 2003

Fingerprint

Acetylcholinesterase
Neuroblastoma
Apoptosis
Amyloid
Cell Survival
Cells
Spectrophotometry
DNA
DNA Fragmentation
Cytotoxicity
Electrophoresis
Acetylcholine
Microscopy
Microscopic examination

Keywords

  • Acetylcholinesterase
  • Amyloid beta protein
  • Apoptosis
  • SC35 cells
  • SC42 cells

ASJC Scopus subject areas

  • Chemistry(all)
  • Pharmacology

Cite this

Apoptosis induced by β-amyloid25-35 in acetylcholinesterase-overexpressing neuroblastoma cells. / Zhang, Hai Yan; Brimijoin, William Stephen; Tang, Xi Can.

In: Acta Pharmacologica Sinica, Vol. 24, No. 9, 01.09.2003, p. 853-958+948.

Research output: Contribution to journalArticle

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AU - Brimijoin, William Stephen

AU - Tang, Xi Can

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Y1 - 2003/9/1

N2 - AIM: To examine the relationship between apoptosis induced by β-amyloid fragment 25-35 (Aβ25-35) and the activity of acetylcholinesterase (AChE) in AChE over-expresser-SC42 cells. METHODS: Cell survival was measured by microscopy and MTT reduction; DNA laddering was observed by electrophoresis; AChE activity was determined by spectrophotometry. RESULTS: Aβ25-35 1 μmol/L exposure for 24-48 h caused a significant decrease in cell viability, along with changes in morphology and DNA fragmentation. AChE activity was affected in an inverse manner, increasing gradually to a level that was 1.7-fold higher than control at the 48-h time point. No change in the cytotoxicity of Aβ25-35 was observed when the increased AChE activities were effectively inhibited by huperzine A throughout the 48-h exposure period. CONCLUSION: Although Aβ 25-35 can induce apoptosis in SC42 cells and simultaneously increase AChE activity, the capacity of AChE to hydrolyze acetylcholine is not involved in this apoptosis model.

AB - AIM: To examine the relationship between apoptosis induced by β-amyloid fragment 25-35 (Aβ25-35) and the activity of acetylcholinesterase (AChE) in AChE over-expresser-SC42 cells. METHODS: Cell survival was measured by microscopy and MTT reduction; DNA laddering was observed by electrophoresis; AChE activity was determined by spectrophotometry. RESULTS: Aβ25-35 1 μmol/L exposure for 24-48 h caused a significant decrease in cell viability, along with changes in morphology and DNA fragmentation. AChE activity was affected in an inverse manner, increasing gradually to a level that was 1.7-fold higher than control at the 48-h time point. No change in the cytotoxicity of Aβ25-35 was observed when the increased AChE activities were effectively inhibited by huperzine A throughout the 48-h exposure period. CONCLUSION: Although Aβ 25-35 can induce apoptosis in SC42 cells and simultaneously increase AChE activity, the capacity of AChE to hydrolyze acetylcholine is not involved in this apoptosis model.

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