Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines

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

doi:10.1016/S0196-9781(97)00306-9

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 journal › Article › peer-review

23 Scopus citations

Abstract

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 3.4.24.15 activity was detected in PC-3, DU-145 and LNCaP cells, whereas high levels of neutral endopeptidase 3.4.24.11 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 NT^1-11 and NT^1-1⁰. Phosphoramidon inhibited the metabolism of NT by LNCaP cells. These data suggest that NT is present in and metabolized by LNCaP cellular enzymes.

Original language	English (US)
Pages (from-to)	253-258
Number of pages	6
Journal	Peptides
Volume	19
Issue number	2
DOIs	https://doi.org/10.1016/S0196-9781(97)00306-9
State	Published - Feb 1998

Keywords

Neuroendocrine tumors
Neurotensin
Neutral endopeptidase
Prostate cancer
Proteases

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/S0196-9781(97)00306-9

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title = "Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines",

abstract = "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 3.4.24.15 activity was detected in PC-3, DU-145 and LNCaP cells, whereas high levels of neutral endopeptidase 3.4.24.11 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.",

keywords = "Neuroendocrine tumors, Neurotensin, Neutral endopeptidase, Prostate cancer, Proteases",

author = "Moody, {Terry W.} and Mayr, {Craig A.} and Gillespie, {Terry J.} and Davis, {Thomas P.}",

note = "Funding Information: The authors thank Drs. J. Taylor for helpful discussions, S. Bloom for the NT antisera and D. Brenner for the rNEP. This research was supported by a contract from the Arizona Disease Control Research Commission to T. P. D. ",

year = "1998",

month = feb,

doi = "10.1016/S0196-9781(97)00306-9",

language = "English (US)",

volume = "19",

pages = "253--258",

journal = "Peptides",

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T1 - Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines

AU - Moody, Terry W.

AU - Mayr, Craig A.

AU - Gillespie, Terry J.

AU - Davis, Thomas P.

N1 - Funding Information: The authors thank Drs. J. Taylor for helpful discussions, S. Bloom for the NT antisera and D. Brenner for the rNEP. This research was supported by a contract from the Arizona Disease Control Research Commission to T. P. D.

PY - 1998/2

Y1 - 1998/2

N2 - 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 3.4.24.15 activity was detected in PC-3, DU-145 and LNCaP cells, whereas high levels of neutral endopeptidase 3.4.24.11 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.

AB - 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 3.4.24.15 activity was detected in PC-3, DU-145 and LNCaP cells, whereas high levels of neutral endopeptidase 3.4.24.11 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.

KW - Neuroendocrine tumors

KW - Neurotensin

KW - Neutral endopeptidase

KW - Prostate cancer

KW - Proteases

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DO - 10.1016/S0196-9781(97)00306-9

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AN - SCOPUS:0032006924

SN - 0196-9781

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JO - Peptides

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ER -

Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines

Abstract

Keywords

ASJC Scopus subject areas

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