Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells

Katsumi Shigemura, Shian Ying Sung, Hiroyuki Kubo, Rebecca S. Arnold, Masato Fujisawa, Akinobu Gotoh, Haiyen E. Zhau, Leland W K Chung

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

BACKGROUND: The A Disintegrin And Metalloprotease (ADAM) family is a group of transmembrane proteins containing cell adhesive and proteolytic functional domains. ADAM9 expression was shown to be mediated by androgen receptor (AR) and stress conditions. This study determined a common mediator responsible for ADAM9 protein regulation which supports human prostate cancer (PCa) cell growth and survival, METHODS: ADAM9 protein expression was measured under androgen, anti-androgen, hydrogen peroxide, and/or serum starvation conditions in PCa cells. The roles of reactive oxygen species (ROS) were assessed in the presence or absence of recombinant catalase, or in cells stably transfected with either catalase- or a control neo-cDNA expression vector. ROS was assayed by dihydroethidiurn (DHE) followed by FACS analysis. RESULTS: ADAM9 protein expression was upregulated by androgen in AR-positive but not in AR-negative PCa cells. The anti-androgen bicalutamide effectively blocked this induction. While serum starvation enhanced ADAM9 expression in AR-positive PCa cells, this stress condition did not alter ADAM9 expression in AR-negative PCa cells. Parallel results also showed that androgen treatment or serum starvation enhanced ROS only in AR-positive but not in AR-negative PCa cells. ROS appears to be a common downstream mediator of androgen- or serum starvation-induced ADAM9 expression since addition of hydrogen peroxide or introduction of catalase, either enhanced or abolished respectively ADAM9 protein expression by both AR-positive and -negative PCa cells. CONCLUSIONS: These findings suggest that ROS is: a common mediator responsible for ADAM9 protein induction in human PCa cells, downstream from AR, and stress response signaling.

Original languageEnglish
Pages (from-to)722-731
Number of pages10
JournalProstate
Volume67
Issue number7
DOIs
Publication statusPublished - May 15 2007
Externally publishedYes

Fingerprint

Androgen Receptors
Starvation
Reactive Oxygen Species
Prostatic Neoplasms
Androgens
Serum
Catalase
Proteins
Hydrogen Peroxide
Disintegrins
Metalloproteases
Adhesives
Cell Survival
Complementary DNA
Growth

Keywords

  • ADAM9
  • Androgen receptor
  • Androgen-independent progression
  • Prostate cancer
  • Reactive oxygen species (ROS)
  • Serum deprivation
  • Signal transduction

ASJC Scopus subject areas

  • Urology

Cite this

Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells. / Shigemura, Katsumi; Sung, Shian Ying; Kubo, Hiroyuki; Arnold, Rebecca S.; Fujisawa, Masato; Gotoh, Akinobu; Zhau, Haiyen E.; Chung, Leland W K.

In: Prostate, Vol. 67, No. 7, 15.05.2007, p. 722-731.

Research output: Contribution to journalArticle

Shigemura, Katsumi ; Sung, Shian Ying ; Kubo, Hiroyuki ; Arnold, Rebecca S. ; Fujisawa, Masato ; Gotoh, Akinobu ; Zhau, Haiyen E. ; Chung, Leland W K. / Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells. In: Prostate. 2007 ; Vol. 67, No. 7. pp. 722-731.
@article{78f830621a4e44408cf4474ba831bb2e,
title = "Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells",
abstract = "BACKGROUND: The A Disintegrin And Metalloprotease (ADAM) family is a group of transmembrane proteins containing cell adhesive and proteolytic functional domains. ADAM9 expression was shown to be mediated by androgen receptor (AR) and stress conditions. This study determined a common mediator responsible for ADAM9 protein regulation which supports human prostate cancer (PCa) cell growth and survival, METHODS: ADAM9 protein expression was measured under androgen, anti-androgen, hydrogen peroxide, and/or serum starvation conditions in PCa cells. The roles of reactive oxygen species (ROS) were assessed in the presence or absence of recombinant catalase, or in cells stably transfected with either catalase- or a control neo-cDNA expression vector. ROS was assayed by dihydroethidiurn (DHE) followed by FACS analysis. RESULTS: ADAM9 protein expression was upregulated by androgen in AR-positive but not in AR-negative PCa cells. The anti-androgen bicalutamide effectively blocked this induction. While serum starvation enhanced ADAM9 expression in AR-positive PCa cells, this stress condition did not alter ADAM9 expression in AR-negative PCa cells. Parallel results also showed that androgen treatment or serum starvation enhanced ROS only in AR-positive but not in AR-negative PCa cells. ROS appears to be a common downstream mediator of androgen- or serum starvation-induced ADAM9 expression since addition of hydrogen peroxide or introduction of catalase, either enhanced or abolished respectively ADAM9 protein expression by both AR-positive and -negative PCa cells. CONCLUSIONS: These findings suggest that ROS is: a common mediator responsible for ADAM9 protein induction in human PCa cells, downstream from AR, and stress response signaling.",
keywords = "ADAM9, Androgen receptor, Androgen-independent progression, Prostate cancer, Reactive oxygen species (ROS), Serum deprivation, Signal transduction",
author = "Katsumi Shigemura and Sung, {Shian Ying} and Hiroyuki Kubo and Arnold, {Rebecca S.} and Masato Fujisawa and Akinobu Gotoh and Zhau, {Haiyen E.} and Chung, {Leland W K}",
year = "2007",
month = "5",
day = "15",
doi = "10.1002/pros.20565",
language = "English",
volume = "67",
pages = "722--731",
journal = "Prostate",
issn = "0270-4137",
publisher = "Wiley-Liss Inc.",
number = "7",

}

TY - JOUR

T1 - Reactive oxygen species mediate androgen receptor- and serum starvation-elicited downstream signaling of ADAM9 expression in human prostate cancer cells

AU - Shigemura, Katsumi

AU - Sung, Shian Ying

AU - Kubo, Hiroyuki

AU - Arnold, Rebecca S.

AU - Fujisawa, Masato

AU - Gotoh, Akinobu

AU - Zhau, Haiyen E.

AU - Chung, Leland W K

PY - 2007/5/15

Y1 - 2007/5/15

N2 - BACKGROUND: The A Disintegrin And Metalloprotease (ADAM) family is a group of transmembrane proteins containing cell adhesive and proteolytic functional domains. ADAM9 expression was shown to be mediated by androgen receptor (AR) and stress conditions. This study determined a common mediator responsible for ADAM9 protein regulation which supports human prostate cancer (PCa) cell growth and survival, METHODS: ADAM9 protein expression was measured under androgen, anti-androgen, hydrogen peroxide, and/or serum starvation conditions in PCa cells. The roles of reactive oxygen species (ROS) were assessed in the presence or absence of recombinant catalase, or in cells stably transfected with either catalase- or a control neo-cDNA expression vector. ROS was assayed by dihydroethidiurn (DHE) followed by FACS analysis. RESULTS: ADAM9 protein expression was upregulated by androgen in AR-positive but not in AR-negative PCa cells. The anti-androgen bicalutamide effectively blocked this induction. While serum starvation enhanced ADAM9 expression in AR-positive PCa cells, this stress condition did not alter ADAM9 expression in AR-negative PCa cells. Parallel results also showed that androgen treatment or serum starvation enhanced ROS only in AR-positive but not in AR-negative PCa cells. ROS appears to be a common downstream mediator of androgen- or serum starvation-induced ADAM9 expression since addition of hydrogen peroxide or introduction of catalase, either enhanced or abolished respectively ADAM9 protein expression by both AR-positive and -negative PCa cells. CONCLUSIONS: These findings suggest that ROS is: a common mediator responsible for ADAM9 protein induction in human PCa cells, downstream from AR, and stress response signaling.

AB - BACKGROUND: The A Disintegrin And Metalloprotease (ADAM) family is a group of transmembrane proteins containing cell adhesive and proteolytic functional domains. ADAM9 expression was shown to be mediated by androgen receptor (AR) and stress conditions. This study determined a common mediator responsible for ADAM9 protein regulation which supports human prostate cancer (PCa) cell growth and survival, METHODS: ADAM9 protein expression was measured under androgen, anti-androgen, hydrogen peroxide, and/or serum starvation conditions in PCa cells. The roles of reactive oxygen species (ROS) were assessed in the presence or absence of recombinant catalase, or in cells stably transfected with either catalase- or a control neo-cDNA expression vector. ROS was assayed by dihydroethidiurn (DHE) followed by FACS analysis. RESULTS: ADAM9 protein expression was upregulated by androgen in AR-positive but not in AR-negative PCa cells. The anti-androgen bicalutamide effectively blocked this induction. While serum starvation enhanced ADAM9 expression in AR-positive PCa cells, this stress condition did not alter ADAM9 expression in AR-negative PCa cells. Parallel results also showed that androgen treatment or serum starvation enhanced ROS only in AR-positive but not in AR-negative PCa cells. ROS appears to be a common downstream mediator of androgen- or serum starvation-induced ADAM9 expression since addition of hydrogen peroxide or introduction of catalase, either enhanced or abolished respectively ADAM9 protein expression by both AR-positive and -negative PCa cells. CONCLUSIONS: These findings suggest that ROS is: a common mediator responsible for ADAM9 protein induction in human PCa cells, downstream from AR, and stress response signaling.

KW - ADAM9

KW - Androgen receptor

KW - Androgen-independent progression

KW - Prostate cancer

KW - Reactive oxygen species (ROS)

KW - Serum deprivation

KW - Signal transduction

UR - http://www.scopus.com/inward/record.url?scp=34248207325&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34248207325&partnerID=8YFLogxK

U2 - 10.1002/pros.20565

DO - 10.1002/pros.20565

M3 - Article

VL - 67

SP - 722

EP - 731

JO - Prostate

JF - Prostate

SN - 0270-4137

IS - 7

ER -