Table 3B.
Gel Spots Differentially Phosphorylated after Spinal Cord Injury
Gel spot number and associated protein isoformsa | Vol. Ratio SCI | Vol. Ratio sham | Fold change | NCBI acces. no. | Seq. cov. (%)b | No. of peptides | Theoretical MW/pIe | Functions |
---|---|---|---|---|---|---|---|---|
29. Glyceraldehyde-3-phosphate dehydrogenase | ↑ 1.23 ± 0.34** | 0.56 ± 0.16 | 2.20 | P04797‡ | 54 | 33/– | 36/8.4 | Glycolytic enzyme |
34. Ubiquitin carboxyl-terminal hydrolase isozyme L1 | ↑ 1.50 ± 0.66** | 0.24 ± 0.14 | 6.25 | Q9R0P9‡ | 71 | 36/– | 25/5.1 | Deubiquitinating enzyme |
27. Cathepsin D precursor | ↓ 3.23 ± 1.24* | 7.41 ± 3.30 | −2.29 | P24268¶ | 6 | –/2 | 45/6.7 | Aspartyl protease |
28. Neurofilament light chain | ↓ 2.74 ± 0.81* | 6.77 ± 3.80 | −2.47 | P19527†¶ | 20 | 11/1 | 61/4.6 | Axonal cytoskeleton |
The volume ratio (Vol. Ratio) of the Pro-Q Diamond and SYPRO Ruby signals (calculated from VolPro-Q/VolSYPRO Ruby) was used to quantify the relative phosphorylation level of each gel spot; Mean Fold Change was calculated from the ratio of SCI/sham; fold decreases were calculated by dividing 1 by the ratio of the injured to sham samples; arefers to the spot numbers in Figure 1; brefers to the total percentage of the sequence covered by peptide mass fingerprinting (PMF); crefers to the number of peptides that match the sequence for PMF; drefers to the number of peptides used to identify a protein by tandem mass spectrometry (MS/MS) (CI% > 95%); erefers to the theoretical molecular weight (MW) and the theoretical isoelectric point (pI); *p < 0.05; **p < 0.01; †Protein Score CI% >95%, ‡Protein Score CI% > 99%; ¶Total Ion Score CI% >99%.