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Calsenilin enhances apoptosis by altering endoplasmic reticulum calcium signaling

C Lilliehook1, S Chan, E K Choi

  • 1Laboratory of Molecular Neuropsychiatry, Department of Psychiatry, Mount Sinai School of Medicine, New York, New York 10029, USA.

Insights

Calsenilin (also known as DREAM and KChIP3) increases susceptibility to apoptosis. This neuronal calcium sensor protein enhances cell death by altering calcium dynamics, particularly in response to stress.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Calsenilin (DREAM/KChIP3) is a neuronal calcium sensor protein.
  • It interacts with presenilin proteins at the endoplasmic reticulum and Golgi apparatus.

Purpose of the Study:

  • To investigate the role of calsenilin in apoptosis.
  • To determine if calsenilin influences cellular calcium dynamics during apoptosis.

Main Methods:

  • Stable neuroglioma cell lines overexpressing calsenilin were used.
  • Apoptosis was induced by serum withdrawal or thapsigargin.
  • Caspase and calpain activities were measured.
  • Calcium imaging was employed to assess intracellular calcium release.

Main Results:

  • Calsenilin overexpression enhanced apoptosis induced by serum withdrawal and thapsigargin.
  • Caspase and calpain activities were elevated in calsenilin-overexpressing cells undergoing apoptosis.
  • Cells overexpressing calsenilin showed increased intracellular calcium release upon thapsigargin treatment.

Conclusions:

  • Calsenilin promotes apoptosis, making cells more vulnerable to apoptotic stimuli.
  • Altered calcium dynamics, specifically increased intracellular calcium release, may mediate calsenilin's pro-apoptotic effect.

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