Two potentially specific but relevant patterns of proteomic change Response of SH-SY5Y cells to diff

来源 :Neural Regeneration Research | 被引量 : 0次 | 上传用户:wangxiao8910
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Dopamine (DA) exposure at a dose of 100 μmol/L for 24 hours causes oxidative stress in SH-SY5Y cells with induction of neuronal differentiation by retinoic acid (RA,10 μmol/L, 72 hours) followed by phorbol ester 12-O-tetradecanoyl-phorbol-13-acetate (TPA, 80 nmol/L, 72 hours). However, it remains unclear whether the alteration of phenotype observed in response to oxidative stress is associated with protein regulation in this cellular model for Parkinson’s disease. The present study detected protein regulation affected by oxidative stress at a proteomic level: selection of differentially altered proteins using two dimensional difference in-gel electrophoresis and identification of these proteins using matrix assisted laser desorption/ionization time-of-flight mass spectrometry. The results demonstrated significant alterations in expression of six proteins in SH-SY5Y cells following the differentiation and fourteen proteins in the differentiated cells following the exposure, exemplified by an increase of tubulin alpha1 in the former but a decrease of tubulin alpha-ubiquitous chain in the latter. These results suggest that two potentially specific but relevant patterns of proteomic change may be produced in SH-SY5Y cells with the induction of differentiation by RA followed by TPA, and in the differentiated cells after DA exposure. Dopamine (DA) exposure at a dose of 100 μmol / L for 24 hours causes oxidative stress in SH-SY5Y cells with induction of neuronal differentiation by retinoic acid (RA, 10 μmol / L, 72 hours) followed by phorbol ester 12-O -tetradecanoyl-phorbol-13-acetate (TPA, 80 nmol / L, 72 hours). However, it remains unclear whether the alteration of phenotype observed in response to oxidative stress is associated with protein regulation in this cellular model for Parkinson’s disease. present study detected protein regulation affected by oxidative stress at a proteomic level: selection of differentially altered proteins using two dimensional difference in-gel electrophoresis and identification of these proteins using matrix assisted laser desorption / ionization time-of-flight mass spectrometry. The disease significant alterations in expression of six proteins in SH-SY5Y cells following the differentiation and fourteen proteins in the differentiated cells following the exposure, exemplifie d by an increase of tubulin alpha1 in the former but a decrease of tubulin alpha-ubiquitous chain in the latter. These results suggest that two potentially specific but relevant patterns of proteomic change may be produced in SH-SY5Y cells with the induction of differentiation by RA followed by TPA, and in the differentiated cells after DA exposure.
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