TY - JOUR
T1 - Proteomic and phosphoproteomic analyses of the soluble fraction following acute spinal cord contusion in rats
AU - Chen, Anshu
AU - McEwen, Melanie L.
AU - Sun, Shixin
AU - Ravikumar, Rangaswamyrao
AU - Springer, Joe E.
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Traumatic spinal cord injury (SCI) causes marked neuropathological changes in the spinal cord, resulting in limited functional recovery. Currently, there are no effective treatments, and the mechanisms underlying these neuropathological changes are not completely understood. In this study, two-dimensional gel electrophoresis coupled with mass spectrometry was used to investigate injury-related changes in the abundance (SYPRO Ruby stain) and phosphorylation (Pro-Q Diamond stain) of proteins from the soluble fraction of the lesion epicenter at 24 h following SCI. Over 1500 SYPRO Ruby-stained spots and 100 Pro-Q Diamond-stained spots were examined. We identified 26 unique proteins within 38 gel spots that differentially changed in abundance, phosphorylation, or both in response to SCI. Protein redundancies among the gel spots were likely due to differences in proteolysis, post-translational modifications, and the existence of isoforms. The proteins affected were blood-related proteins, heat-shock proteins, glycolytic enzymes, antioxidants, and proteins that function in cell structure, cell signaling, DNA damage, and protein degradation. These protein changes post injury may suggest additional avenues of investigation into the underlying molecular mechanisms responsible for the pathophysiological consequences of SCI.
AB - Traumatic spinal cord injury (SCI) causes marked neuropathological changes in the spinal cord, resulting in limited functional recovery. Currently, there are no effective treatments, and the mechanisms underlying these neuropathological changes are not completely understood. In this study, two-dimensional gel electrophoresis coupled with mass spectrometry was used to investigate injury-related changes in the abundance (SYPRO Ruby stain) and phosphorylation (Pro-Q Diamond stain) of proteins from the soluble fraction of the lesion epicenter at 24 h following SCI. Over 1500 SYPRO Ruby-stained spots and 100 Pro-Q Diamond-stained spots were examined. We identified 26 unique proteins within 38 gel spots that differentially changed in abundance, phosphorylation, or both in response to SCI. Protein redundancies among the gel spots were likely due to differences in proteolysis, post-translational modifications, and the existence of isoforms. The proteins affected were blood-related proteins, heat-shock proteins, glycolytic enzymes, antioxidants, and proteins that function in cell structure, cell signaling, DNA damage, and protein degradation. These protein changes post injury may suggest additional avenues of investigation into the underlying molecular mechanisms responsible for the pathophysiological consequences of SCI.
KW - Contusion
KW - Phosphoproteome
KW - Proteome
KW - Spinal cord injury,2-DE
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U2 - 10.1089/neu.2009.1051
DO - 10.1089/neu.2009.1051
M3 - Article
C2 - 19691422
AN - SCOPUS:76349111840
SN - 0897-7151
VL - 27
SP - 263
EP - 274
JO - Journal of Neurotrauma
JF - Journal of Neurotrauma
IS - 1
ER -