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

TitleProteomic identification of calcium-binding chaperone calreticulin as a potential mediator for the neuroprotective and neuritogenic activities of fruit-derived glycoside amygdalin
Authors
Issue Date2015
Citation
Journal of Nutritional Biochemistry, 2015 v. 26 n. 2, p. 146-154 How to Cite?
AbstractAmygdalin 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 eleven mostly regulated protein spots from 2-D SDS-PAGE gels for protein identification by matrix-assisted laser desorption/ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS). 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.
Persistent Identifierhttp://hdl.handle.net/10722/205933

 

DC FieldValueLanguage
dc.contributor.authorCHENG, Yen_US
dc.contributor.authorYANG, Cen_US
dc.contributor.authorZHAO, Jen_US
dc.contributor.authorTse, HFen_US
dc.contributor.authorRong, Jen_US
dc.date.accessioned2014-10-20T09:55:35Z-
dc.date.available2014-10-20T09:55:35Z-
dc.date.issued2015-
dc.identifier.citationJournal of Nutritional Biochemistry, 2015 v. 26 n. 2, p. 146-154en_US
dc.identifier.urihttp://hdl.handle.net/10722/205933-
dc.description.abstractAmygdalin 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 eleven mostly regulated protein spots from 2-D SDS-PAGE gels for protein identification by matrix-assisted laser desorption/ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS). 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.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Nutritional Biochemistryen_US
dc.titleProteomic identification of calcium-binding chaperone calreticulin as a potential mediator for the neuroprotective and neuritogenic activities of fruit-derived glycoside amygdalinen_US
dc.typeArticleen_US
dc.identifier.emailTse, HF: hftse@hkucc.hku.hken_US
dc.identifier.emailRong, J: jrong@hku.hken_US
dc.identifier.authorityTse, HF=rp00428en_US
dc.identifier.authorityRong, J=rp00515en_US
dc.identifier.doi10.1016/j.jnutbio.2014.09.012-
dc.identifier.hkuros241243en_US

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