Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

The Rab27a-binding protein, JFC1, regulates androgen-dependent secretion of prostate-specific antigen and prostatic-specific acid phosphatase

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Johnson, J. L.
  • Ellis, B. A.
  • Noack, D.
  • Seabra, M. C.
  • Catz, Sergio

publication date

  • November 2005

journal

  • Biochemical Journal  Journal

abstract

  • Two of the major proteins secreted by the prostate epithelium secretory cells are PSA (prostate-specific antigen) and PSAP (prostatic-specific acid phosphatase). The molecules involved in the secretory machinery of PSA and PSAP, and the regulation of this machinery, remain unknown. In the present paper, we provide evidence that JFC1 [synaptotagmin-like protein (slp1)], a Rab27a- and PtdIns(3,4,5)P3-binding protein, regulates the androgen-dependent secretion of PSAP and PSA in human LNCaP prostate carcinoma cells. Androgen-dependent PSAP secretion was significantly inhibited in cells that expressed the C2A domain of JFC1 [PtdIns(3,4,5)P3-binding-domain], but was unaffected by JFC1 overexpression. Conversely, PSA secretion was not inhibited by the C2A domain of JFC1. We show, using immunofluorescence analysis, that JFC1 co-localizes with PSAP, but rarely with PSA, in prostate granules, suggesting that JFC1 is part of the PSAP secretory machinery. However, PSA secretion was significantly increased in LNCaP cells that overexpressed JFC1, indicating that the secretion of PSA is susceptible to variations in the intracellular concentration of JFC1. Both PSAP and PSA secretion was increased by overexpression of wild-type Rab27a or the constitutively active Rab27aQ78L. The secretion of PSA was partially inhibited in the presence of LY294002, while the secretion of PSAP was completely abolished by the PI3K (phosphoinositide 3-kinase) inhibitor. This supports the view that PI3K plays a differential role in the secretion of prostate secretory markers. In conclusion, we present evidence that JFC1 differentially regulates the secretion of PSAP and PSA, and that Rab27a and PI3K play a central role in the exocytosis of prostate-specific markers.

subject areas

  • Acid Phosphatase
  • Androgens
  • Cell Line, Tumor
  • Cytoplasmic Granules
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Male
  • Membrane Proteins
  • Phosphatidylinositol 3-Kinases
  • Prostate
  • Prostate-Specific Antigen
  • Protein Binding
  • Protein Transport
  • Protein Tyrosine Phosphatases
  • Testosterone
  • Up-Regulation
  • rab GTP-Binding Proteins
scroll to property group menus

Research

keywords

  • exocytosis
  • phosphoinositide 3-kinase (PI3K)
  • prostate-specific antigen (PSA)
  • prostatic-specific acid phosphatase (PSAP)
  • synaptotagmin-like protein
  • vesicular trafficking
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0264-6021

Digital Object Identifier (DOI)

  • 10.1042/bj20050380

PubMed ID

  • 16004602
scroll to property group menus

Additional Document Info

start page

  • 699

end page

  • 710

volume

  • 391

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support