Journal article
Glycomic Characterization of Prostate Specific Antigen and Prostatic Acid Phosphatase in Prostate Cancer and Benign Disease Seminal Plasma Fluids
Journal of proteome research, v 8(2), pp 620-630
06 Feb 2009
PMID: 19128049
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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. Using 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.
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Details
- Title
- Glycomic Characterization of Prostate Specific Antigen and Prostatic Acid Phosphatase in Prostate Cancer and Benign Disease Seminal Plasma Fluids
- Creators
- Krista Y White - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Lucy Rodemich - Department of Microbiology and Immunology, Drexel Institute for Biotechnology and Virology Research, Doylestown, PA 18902Julius O Nyalwidhe - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Mary Ann Comunale - Department of Microbiology and Immunology, Drexel Institute for Biotechnology and Virology Research, Doylestown, PA 18902Mary Ann Clements - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Raymond S Lance - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Paul F Schellhammer - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Anand Mehta - Department of Microbiology and Immunology, Drexel Institute for Biotechnology and Virology Research, Doylestown, PA 18902O. John Semmes - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507Richard R Drake - Department of Microbiology and Molecular Cell Biology, Center for Biomedical Proteomics, Eastern Virginia Medical School, Norfolk, Virginia 23507
- Publication Details
- Journal of proteome research, v 8(2), pp 620-630
- Publisher
- American Chemical Society; Washington, DC
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000263193300022
- Scopus ID
- 2-s2.0-61849113322
- Other Identifier
- 991014878059904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemical Research Methods