The role of human prostatic acid phosphatase (PAcP, P15309|PPAP_HUMAN) in prostate cancer was investigated using a new proteomic tool termed signal sequence swapping (replacement of domains from the native cleaved amino terminal signal sequence of secretory/membrane proteins with corresponding regions of functionally distinct signal sequence subtypes). This manipulation preferentially redirects proteins to different pathways of biogenesis at the endoplasmic reticulum, magnifying normally difficult to detect subsets of the protein of interest. For PAcP this technique reveals three forms identical in amino acid sequence but profoundly different in physiological functions, subcellular location, and biochemical properties. These three forms of PAcP can also occur with the wild-type PAcP signal sequence. Clinical specimens from patients with prostate cancer demonstrate that one form, termed PLPAcP, correlates with early prostate cancer. These findings confirm the analytical power of this method, implicate PLPAcP in prostate cancer pathogenesis, and suggest novel anticancer therapeutic strategies.
Multifunctionality of Prostatic Acid Phosphatase in Prostate Cancer Pathogenesis
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
Evgenia Alpert, Armin Akhavan, Arie Gruzman, William J Hansen, Joshua Lehrer- Graiwer, Steven C Hall, Eric Johansen, Sean McAllister, Mittul Gulati, Ming-Fong Lin, Vishwanath R Lingappa; Multifunctionality of Prostatic Acid Phosphatase in Prostate Cancer Pathogenesis. Biosci Rep 2021; BSR20211646. doi: https://doi.org/10.1042/BCJ20200944
Download citation file: