Prostate cancer is one of the most prevalent
cancers in men. It is critical to identify and characterize oncogenes that drive the pathogenesis of human
prostate cancer. The current study builds upon previous research showing that a
disintegrin and metallproteinase (ADAM)28 is involved in the pathogenesis of numerous
cancers. Our novel study used overexpression, pharmacological, and molecular approaches to investigate the
biological function of ADAM28 in human
prostate cancer cells, with a focus on cell proliferation and migration. The results of this study provide important insights into the role of
metalloproteinases in human
prostate cancer.The expression of ADAM28
protein levels was assessed within human prostate
tumors and normal adjacent tissue by immunohistochemistry. Immunocytochemistry and western blotting were used to assess ADAM28
protein expression in human
prostate cancer cell lines. Functional assays were conducted to assess proliferation and migration in human
prostate cancer cells in which ADAM28
protein expression or activity had been altered by overexpression, pharmacological inhibition, or by
siRNA gene knockdown.The membrane bound ADAM28 was increased in human
tumor biopsies and
prostate cancer cell lines. Pharmacological inhibition of ADAM28 activity and/or knockdown of ADAM28 significantly reduced proliferation and migration of human
prostate cancer cells, while overexpression of ADAM28 significantly increased proliferation and migration.ADAM28 is overexpressed in primary human prostate
tumor biopsies, and it promotes human
prostate cancer cell proliferation and migration. This study supports the notion that inhibition of ADAM28 may be a potential novel therapeutic strategy for human
prostate cancer.