Abstract
Background:
Several serum biomarkers such as antigens, soluble proteins, metabolites, and genes have been identified for the diagnosis of cancers and for monitoring the recurrence after cancer treatment.
Methods:
In the present study, a protein kinase C (PKC) α-specific peptide substrate was phosphorylated with serum samples collected from cancer-bearing mice (U87, A431, HepG2, and A549) and the phosphorylation ratio was detected by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS).
Results:
The phosphorylation ratio for peptide substrates significantly increased in the serum of cancer-bearing mice compared with the ratio found in control mice. The addition of a PKCα inhibitor induced a concentration-dependent decrease in phosphorylation ratios, but the non-PKCα inhibitors, rottlerin and H-89, did not significantly effect phosphorylation ratios.
Conclusions:
These results suggest that serum activated PKCα is a good biomarker applicable to cancer diagnosis.
Keywords: Diagnosis, protein kinase, serum, peptide substrate, phosphorylation
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