Proteomic identification of calcium-binding chaperone calreticulin as a potential mediator for the neuroprotective and neuritogenic activities of fruit-derived glycoside amygdalin

Yuanyuan Cheng, Chuanbin YANG, Jia Zhao, Hung Fat Tse, Jianhui Rong*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

Amygdalin is a fruit-derived glycoside with the potential for treating neurodegenerative diseases. This study was designed to identify the neuroprotective and neuritogenic activities of amygdalin. We initially demonstrated that amygdalin enhanced nerve growth factor (NGF)-induced neuritogenesis and attenuated 6-hydroxydopamine (6-OHDA)-induced neurotoxicity in rat dopaminergic PC12 cells. To define protein targets for amygdalin, we selected a total of 11 mostly regulated protein spots from two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels for protein identification by matrix-assisted laser desorption/ionization-time-of-flight-mass spectrometry. We verified the effect of amygdalin on six representative proteins (i.e., calreticulin, Hsp90β, Grp94, 14-3-3η, 14-3-3ζ/δ and Rab GDI-α) for biological relevance to neuronal survival and differentiation. Calcium-binding chaperone calreticulin is of special interest for its activities to promote folding, oligomeric assembly and quality control of proteins that modulate cell survival and differentiation. We transiently knocked down calreticulin expression by specific siRNA and studied its effect on the neuroprotective and neuritogenic activities of amygdalin. We found that amygdalin failed to enhance NGF-induced neuritogenesis in calreticulin-siRNA transfected cells. On the other hand, amygdalin rescued 6-OHDA-induced loss of calreticulin expression. We also found that amygdalin increased the intracellular calcium concentration possibly via inducing calreticulin. Collectively, our results demonstrated the role of calreticulin in mediating the neuroprotective and neuritogenic activities of amygdalin.

Original languageEnglish
Pages (from-to)146-154
Number of pages9
JournalJournal of Nutritional Biochemistry
Volume26
Issue number2
DOIs
Publication statusPublished - 1 Feb 2015

Scopus Subject Areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Biology
  • Nutrition and Dietetics
  • Clinical Biochemistry

User-Defined Keywords

  • Amygdalin
  • Calreticulin
  • Neuritogenesis
  • Neuroprotection
  • Proteomics

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