Proteomic analysis of protein expression in prostate cancer.
OBJECTIVE
To investigate protein expression in prostate cancer using 2-dimensional gel electrophoresis (2-DE) and mass spectrometry.


METHODS
Cells were collected from 29 peripheral zone tumors and from benign tissue by scraping cut surfaces of radical prostatectomy specimens. Samples were suspended in a medium with protease inhibitors and prepared for 2-DE. Gels were analyzed, and protein spots that differed quantitatively between tumor and benign tissue were identified via mass spectrometric fingerprinting of tryptic fragments and tandem mass spectrometry sequence analysis.


RESULTS
In total, 63 spots differed between cancer and benign samples (p < 0.01); 56 were overexpressed (> 1.5 fold) in cancer and 7 underexpressed (< 0.6 fold). Among overexpressed proteins were transcription factors (nucleoside diphosphate kinase 1) and enzymes involved in gene silencing (chromobox protein), protein synthesis (39S ribosomal protein L12, BiP protein, protein disulfide isomerase), degradation (cytosol aminopeptidase, endopeptidase Clp, inorganic pyrophosphatase) and energy metabolism (acyl-CoA dehydrogenase, isocitrate dehydrogenase, NADH-ubiquinone oxidoreductase, pyruvate dehydrogenase), heat-shock proteins (60 and 70 kd), structural proteins (cytokeratins) and membrane proteins (stomatinlike protein 2).


CONCLUSIONS
The protein profile of prostate cancer differs from that of benign tissue. Several potential target proteins for detection or evaluation of prognosis in prostate cancer were identified.
Lexander
Helena
H
Department of Oncology and Pathology, Karolinska Institute, Stockholm, Sweden.
Palmberg
Carina
C
Auer
Gert
G
Hellström
Magnus
M
Franzén
Bo
B
Jörnvall
Hans
H
Egevad
Lars
L
D015180:Electrophoresis, Gel, Two-Dimensional; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D008297:Male; D011471:Prostatic Neoplasms / Q000378:metabolism* / Q000473:pathology; D040901:Proteomics; D021241:Spectrometry, Mass, Electrospray Ionization