Glycomic Characterization of Prostate-Specific Antigen and Prostatic Acid Phosphatase in Prostate Cancer and Benign Disease Seminal Plasma Fluids

Prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) are glycoproteins secreted by prostate epithelial cells, and have a long clinical history of use as serum biomarkers of prostate cancers. These two proteins are present at significantly higher concentrations in seminal plasma, maki...

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Bibliographic Details
Published in:Journal of proteome research 2009-02, Vol.8 (2), p.620-630
Main Authors: White, Krista Y, Rodemich, Lucy, Nyalwidhe, Julius O, Comunale, Mary Ann, Clements, Mary Ann, Lance, Raymond S, Schellhammer, Paul F, Mehta, Anand S, Semmes, O. John, Drake, Richard R
Format: Article
Language:English
Subjects:
Acid Phosphatase
Biomarkers, Tumor - blood
Biomarkers, Tumor - chemistry
Carbohydrate Conformation
Carbohydrate Sequence
Glycomics - methods
Humans
Male
Molecular Sequence Data
Polysaccharides - analysis
Prostate-Specific Antigen - blood
Prostate-Specific Antigen - chemistry
Prostatic Neoplasms - blood
Prostatic Neoplasms - chemistry
Prostatic Neoplasms - enzymology
Protein Tyrosine Phosphatases - blood
Protein Tyrosine Phosphatases - chemistry
Semen - chemistry
Semen - enzymology
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary:Prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) are glycoproteins secreted by prostate epithelial cells, and have a long clinical history of use as serum biomarkers of prostate cancers. These two proteins are present at significantly higher concentrations in seminal plasma, making this proximal fluid of the prostate a good source for purifying enough protein for characterization of prostate disease associated changes in glycan structures. With the use of seminal fluid samples representative of normal control, benign prostatic disease and prostate cancers, PAP and PSA were enriched by thiophilic absorption chromatography. Released N-linked glycan constituents from both proteins were analyzed by a combination of normal phase HPLC and MALDI-TOF spectrometry. For PSA, 40 putative glycoforms were determined, and 21 glycoforms were determined for PAP. PAP glycans were further analyzed with a hybrid triple quadrupole/linear ion trap mass spectrometer to assign specific glycoform classes to each of the three N-linked sites. The glycans identified in these studies will allow for more defined targeting of prostate disease-specific changes for PAP, PSA and other secreted prostatic glycoproteins.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr8007545