Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1

A. Krongrad, Elena Nikolaevna Atochina, J. V V Ryan, B. A. Roos

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Human endopeptidase 24.11 (EP) occurs in greatest abundance on terminally differentiated prostate cells; thus, loss of EP could mark dedifferentiation of prostate epithelium. To identify laboratory models that would permit continuous work oil the biochemistry and hormonal regulation of EP, we examined the well differentiated LNCaP and poorly differentiated PPC-1 human prostate cancer cell lines. Ultrastructural analysis revealed that LNCaP secretes electron-dense material that resembles the particulate matter of seminal plasma, which is associated with endopeptidase activity. LNCaP medium contained EP activity while PPC-1 medium did not. Whether the apparent deletion of EP from the PPC-1 cell line is characteristic of poorly differentiated prostate adenocarcinoma is not yet clear. However, it may be relevant to the carcinogenic process that EP can limit growth of lung small carcinomas by inactivating cell growth-promoting bombesin-like peptides. Because bombesin has been identified in aggressive human prostate cancers, loss of EP in PPC-1 could represent a necessary step in transformation to aggressive phenotype. The combination of LNCaP and PPC-1, which offers well-differentiated and poorly differentiated cancer phenotypes, appears well suited to studying the relevance of EP in prostate cancer biology.

Original languageEnglish
Pages (from-to)113-116
Number of pages4
JournalUrological Research
Volume25
Issue number2
DOIs
Publication statusPublished - Apr 1997
Externally publishedYes

Fingerprint

Neprilysin
Human Activities
Prostatic Neoplasms
Cell Line
Prostate
Bombesin
Phenotype
Endopeptidases
Particulate Matter
Small Cell Lung Carcinoma
Growth
Semen
Biochemistry
Oils
Adenocarcinoma
Epithelium
Electrons
Peptides

Keywords

  • Endopeptidase 24.11
  • Growth
  • LNCaP
  • PPC-1
  • Prostate cancer

ASJC Scopus subject areas

  • Urology

Cite this

Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1. / Krongrad, A.; Atochina, Elena Nikolaevna; Ryan, J. V V; Roos, B. A.

In: Urological Research, Vol. 25, No. 2, 04.1997, p. 113-116.

Research output: Contribution to journalArticle

@article{3b3db2e0f03d4d88b23395713620e49a,
title = "Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1",
abstract = "Human endopeptidase 24.11 (EP) occurs in greatest abundance on terminally differentiated prostate cells; thus, loss of EP could mark dedifferentiation of prostate epithelium. To identify laboratory models that would permit continuous work oil the biochemistry and hormonal regulation of EP, we examined the well differentiated LNCaP and poorly differentiated PPC-1 human prostate cancer cell lines. Ultrastructural analysis revealed that LNCaP secretes electron-dense material that resembles the particulate matter of seminal plasma, which is associated with endopeptidase activity. LNCaP medium contained EP activity while PPC-1 medium did not. Whether the apparent deletion of EP from the PPC-1 cell line is characteristic of poorly differentiated prostate adenocarcinoma is not yet clear. However, it may be relevant to the carcinogenic process that EP can limit growth of lung small carcinomas by inactivating cell growth-promoting bombesin-like peptides. Because bombesin has been identified in aggressive human prostate cancers, loss of EP in PPC-1 could represent a necessary step in transformation to aggressive phenotype. The combination of LNCaP and PPC-1, which offers well-differentiated and poorly differentiated cancer phenotypes, appears well suited to studying the relevance of EP in prostate cancer biology.",
keywords = "Endopeptidase 24.11, Growth, LNCaP, PPC-1, Prostate cancer",
author = "A. Krongrad and Atochina, {Elena Nikolaevna} and Ryan, {J. V V} and Roos, {B. A.}",
year = "1997",
month = "4",
doi = "10.1007/BF01037925",
language = "English",
volume = "25",
pages = "113--116",
journal = "Urological Research",
issn = "0300-5623",
publisher = "Springer Verlag",
number = "2",

}

TY - JOUR

T1 - Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1

AU - Krongrad, A.

AU - Atochina, Elena Nikolaevna

AU - Ryan, J. V V

AU - Roos, B. A.

PY - 1997/4

Y1 - 1997/4

N2 - Human endopeptidase 24.11 (EP) occurs in greatest abundance on terminally differentiated prostate cells; thus, loss of EP could mark dedifferentiation of prostate epithelium. To identify laboratory models that would permit continuous work oil the biochemistry and hormonal regulation of EP, we examined the well differentiated LNCaP and poorly differentiated PPC-1 human prostate cancer cell lines. Ultrastructural analysis revealed that LNCaP secretes electron-dense material that resembles the particulate matter of seminal plasma, which is associated with endopeptidase activity. LNCaP medium contained EP activity while PPC-1 medium did not. Whether the apparent deletion of EP from the PPC-1 cell line is characteristic of poorly differentiated prostate adenocarcinoma is not yet clear. However, it may be relevant to the carcinogenic process that EP can limit growth of lung small carcinomas by inactivating cell growth-promoting bombesin-like peptides. Because bombesin has been identified in aggressive human prostate cancers, loss of EP in PPC-1 could represent a necessary step in transformation to aggressive phenotype. The combination of LNCaP and PPC-1, which offers well-differentiated and poorly differentiated cancer phenotypes, appears well suited to studying the relevance of EP in prostate cancer biology.

AB - Human endopeptidase 24.11 (EP) occurs in greatest abundance on terminally differentiated prostate cells; thus, loss of EP could mark dedifferentiation of prostate epithelium. To identify laboratory models that would permit continuous work oil the biochemistry and hormonal regulation of EP, we examined the well differentiated LNCaP and poorly differentiated PPC-1 human prostate cancer cell lines. Ultrastructural analysis revealed that LNCaP secretes electron-dense material that resembles the particulate matter of seminal plasma, which is associated with endopeptidase activity. LNCaP medium contained EP activity while PPC-1 medium did not. Whether the apparent deletion of EP from the PPC-1 cell line is characteristic of poorly differentiated prostate adenocarcinoma is not yet clear. However, it may be relevant to the carcinogenic process that EP can limit growth of lung small carcinomas by inactivating cell growth-promoting bombesin-like peptides. Because bombesin has been identified in aggressive human prostate cancers, loss of EP in PPC-1 could represent a necessary step in transformation to aggressive phenotype. The combination of LNCaP and PPC-1, which offers well-differentiated and poorly differentiated cancer phenotypes, appears well suited to studying the relevance of EP in prostate cancer biology.

KW - Endopeptidase 24.11

KW - Growth

KW - LNCaP

KW - PPC-1

KW - Prostate cancer

UR - http://www.scopus.com/inward/record.url?scp=0030904907&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030904907&partnerID=8YFLogxK

U2 - 10.1007/BF01037925

DO - 10.1007/BF01037925

M3 - Article

C2 - 9144877

AN - SCOPUS:0030904907

VL - 25

SP - 113

EP - 116

JO - Urological Research

JF - Urological Research

SN - 0300-5623

IS - 2

ER -