Morphology and MMP-9, AR and IGFR-1 responses of the seminal vesicle in TRAMP mice model

Tissue Cell. 2016 Jun;48(3):217-23. doi: 10.1016/j.tice.2016.03.005. Epub 2016 Mar 18.

Abstract

Seminal vesicles are important hormone-dependent accessory sex glands. Transgenic adenocarcinoma of the mouse prostate (TRAMP) model has been used to evaluate malignant diseases in the prostate and in other sexual glands. The aim of this study was to characterize structural and molecular features of the seminal vesicle in different life periods of the TRAMP mice. Groups: Control Group (5 FVB/12 week old mice), TRAMP 12 and 22 Groups (10 TRAMP 12 and 22 week old mice, respectively). Seminal vesicles were evaluated by morphological and immunohistochemical parameters; androgenic receptor (AR), Insulin-like growth factor 1 (IGFR-1) and metalloproteinase 9 (MMP-9). The TRAMP mice showed frequent epithelial proliferation, including cellular stromal invasion, especially in the TRAMP 22 group. Intense AR reactivity was seen in both stroma and epithelial regions in the TRAMP 22 group. Intense IGFR-1 and MMP-9 stromal immunolabeling was identified in both TRAMP groups. Thus, there were structural and molecular changes in the seminal vesicle in TRAMP mice, compromising not only the structure but also the stromal signaling, damaging thus the function and leading to glandular lesions. TRAMP mice could be indicated as a good model to study alterations of the seminal vesicle in association to prostate cancer.

Keywords: AR; IGFR-1; MMP-9; Seminal vesicle; TRAMP.

MeSH terms

  • Animals
  • Disease Models, Animal
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Insulin-Like Growth Factor I / biosynthesis*
  • Male
  • Matrix Metalloproteinase 9 / biosynthesis*
  • Mice
  • Mice, Transgenic
  • Prostatic Neoplasms / genetics
  • Prostatic Neoplasms / pathology*
  • Receptors, Androgen / biosynthesis*
  • Seminal Vesicles / pathology

Substances

  • Receptors, Androgen
  • insulin-like growth factor-1, mouse
  • Insulin-Like Growth Factor I
  • Matrix Metalloproteinase 9