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Updated: Oct 16, 2025

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
Published on: August 2, 2018
Multifunctionality of prostatic acid phosphatase in prostate cancer pathogenesis
Evgenia Alpert1, Armin Akhavan1, Arie Gruzman1
1Bioconformatics Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A.
A novel proteomics method revealed three distinct forms of human prostatic acid phosphatase (PAcP). One form, PLPAcP, is linked to early prostate cancer, suggesting new therapeutic targets.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Prostatic acid phosphatase (PAcP) is a key protein in prostate biology.
- Understanding PAcP's diverse roles is crucial for prostate cancer research.
- Existing methods struggle to differentiate functional PAcP variants.
Purpose of the Study:
- To investigate the functional roles of PAcP in prostate cancer using a novel proteomics technique.
- To identify specific PAcP variants associated with early-stage prostate cancer.
- To explore potential new therapeutic strategies targeting PAcP.
Main Methods:
- Utilized signal sequence swapping, a proteomics tool to alter protein trafficking pathways.
- Redirected PAcP to different endoplasmic reticulum (ER) biogenesis pathways.
- Analyzed distinct PAcP forms based on function, location, and biochemical properties.
Main Results:
- Identified three PAcP forms with identical amino acid sequences but different physiological functions and subcellular locations.
- Discovered that one specific form, PLPAcP, correlates with early prostate cancer.
- Demonstrated the presence of these forms alongside wildtype PAcP.
Conclusions:
- The signal sequence swapping technique effectively distinguishes functional protein subsets.
- PLPAcP is implicated in the pathogenesis of prostate cancer.
- Findings suggest novel therapeutic avenues targeting specific PAcP forms in cancer treatment.
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