Multifunctionality of prostatic acid phosphatase in prostate cancer pathogenesis.

Autor:	Alpert E; Bioconformatics Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A., Akhavan A; Bioconformatics Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A., Gruzman A; Bioconformatics Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A., Hansen WJ; Prosetta Corporation, 670 5th St, SF, CA 94107, U.S.A., Lehrer-Graiwer J; Prosetta Corporation, 670 5th St, SF, CA 94107, U.S.A., Hall SC; Cell and Tissue Biology, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A.; Biomolecular Resource Center Mass Spectrometry Facility, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A., Johansen E; Biomolecular Resource Center Mass Spectrometry Facility, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A.; Cancer Center, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A., McAllister S; Cancer Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A., Gulati M; Department of Physiology, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A., Lin MF; Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198, U.S.A., Lingappa VR; Bioconformatics Laboratory of the California Pacific Medical Center (CPMC) Research Institute, 475 Brannan St, SF, CA 94107, U.S.A.; Prosetta Corporation, 670 5th St, SF, CA 94107, U.S.A.; Department of Physiology, UCSF, 513 Parnassus Ave, SF, CA 94143, U.S.A.
Jazyk:	angličtina
Zdroj:	Bioscience reports [Biosci Rep] 2021 Oct 29; Vol. 41 (10).
DOI:	10.1042/BSR20211646
Abstrakt:	The role of human prostatic acid phosphatase (PAcP, P15309|PPAP_HUMAN) in prostate cancer was investigated using a new proteomics 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 (ER), 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 wildtype 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. (© 2021 The Author(s).)
Databáze:	MEDLINE
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