Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines

Terry W. Moody, Craig A. Mayr, Terry J. Gillespie, Thomas P. Davis

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


The formation and processing of neurotensin (NT) by three prostate cancer cell lines was investigated. Neurotensin (NT) immunoreactivity was detected in conditioned media and extracts of LNCaP cells. Using HPLC techniques, the immunoreactivity extracted from LNCaP cells coeluted with synthetic NT standard. Metalloendopeptidase activity was detected in PC-3, DU-145 and LNCaP cells, whereas high levels of neutral endopeptidase activity was detected only in LNCaP cells. NT was relatively stable when incubated with PC-3 or D-145 cells but was rapidly degraded by LNCaP cells to NT1-11 and NT1-10. Phosphoramidon inhibited the metabolism of NT by LNCaP cells. These data suggest that NT is present in and metabolized by LNCaP cellular enzymes.

Original languageEnglish (US)
Pages (from-to)253-258
Number of pages6
Issue number2
StatePublished - Feb 1998


  • Neuroendocrine tumors
  • Neurotensin
  • Neutral endopeptidase
  • Prostate cancer
  • Proteases

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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