Analysis of the saliva from patients with oral cancer by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
Using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), this study analyzed the saliva obtained from patients with oral cancer and compared these mass spectra with those obtained from healthy controls. Saliva without pre-treatment was mixed directly with a sinapinic acid matrix. Alpha-amylase (57 kDa) dominated the high mass range in the MALDI mass spectra of the saliva from healthy subjects, but the peak was suppressed for patients with oral cancer and was replaced by a peak at m/z 66 k in the spectra of patients' samples (15 out of 20). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) with in-gel tryptic digestion combined with matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) was employed to characterize this 66-kDa protein, which was thus shown to be albumin. However, based on SDS-PAGE results, concentrations of both alpha-amylase and albumin in patients' saliva were significantly higher than those in healthy subjects. This discrepancy was shown to be due to MALDI suppression effects due to the albumin. MALDI-MS thus has potential as a possible rapid diagnostic screening tool for oral cancer.
Chen
Yu-Chie
YC
Department of Applied Chemistry, National Chiao Tung University, Hsinchu 300, Taiwan. yuchie@cc.nctu.edu.tw
Li
Tzu-Ying
TY
Tsai
Ming-Fei
MF
D000328:Adult; D000368:Aged; D000418:Albumins / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D006868:Hydrolysis; D007202:Indicators and Reagents; D008297:Male; D008875:Middle Aged; D009062:Mouth Neoplasms / Q000378:metabolism*; D012463:Saliva / Q000737:chemistry* / Q000201:enzymology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin; D000516:alpha-Amylases / Q000032:analysis
D000418:Albumins; D007202:Indicators and Reagents; D000516:alpha-Amylases; D014357:Trypsin