Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398

Soichi Obara; Masanori Nakata; Hideo Takeshima; Hideki Katagiri; Tomoichiro Asano; Yoshitomo Oka; Ikuro Maruyama; Jun Ichi Kuratsu

doi:10.1016/j.canlet.2003.11.020

Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398

Soichi Obara, Masanori Nakata, Hideo Takeshima, Hideki Katagiri, Tomoichiro Asano, Yoshitomo Oka, Ikuro Maruyama, Jun Ichi Kuratsu

MED - Medical Sciences

Research output: Contribution to journal › Article › peer-review

33 Citations (Scopus)

Abstract

We report the increased activity and expression of the ILK protein in human glioblastomas and demonstrate that ILK activity is regulated by PTEN. The transfection of wild type-PTEN into the glioblastoma cell line U-251 MG altered the localization of ILK in the cell membrane; transfection with PTEN down-regulated PKB/Akt-Ser-473 phosphorylation via the inhibition of ILK-signaling. Our results suggest that ILK is critical for the PTEN-sensitive regulation of PKB/Akt-dependent cell survival. The selective COX-2 inhibitor NS-398 was found capable of down-regulating ILK and PKB/Akt phosphorylation. Our data indicate that inhibition of ILK signaling may be beneficial in the treatment of PTEN-deficient glioblastoma.

Original language	English
Pages (from-to)	115-122
Number of pages	8
Journal	Cancer Letters
Volume	208
Issue number	1
DOIs	https://doi.org/10.1016/j.canlet.2003.11.020
Publication status	Published - 2004 May 10

Keywords

Glioblastoma
ILK
NS-398
PKB/Akt-Serine 473
PTEN

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.canlet.2003.11.020

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title = "Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398",

abstract = "We report the increased activity and expression of the ILK protein in human glioblastomas and demonstrate that ILK activity is regulated by PTEN. The transfection of wild type-PTEN into the glioblastoma cell line U-251 MG altered the localization of ILK in the cell membrane; transfection with PTEN down-regulated PKB/Akt-Ser-473 phosphorylation via the inhibition of ILK-signaling. Our results suggest that ILK is critical for the PTEN-sensitive regulation of PKB/Akt-dependent cell survival. The selective COX-2 inhibitor NS-398 was found capable of down-regulating ILK and PKB/Akt phosphorylation. Our data indicate that inhibition of ILK signaling may be beneficial in the treatment of PTEN-deficient glioblastoma.",

keywords = "Glioblastoma, ILK, NS-398, PKB/Akt-Serine 473, PTEN",

author = "Soichi Obara and Masanori Nakata and Hideo Takeshima and Hideki Katagiri and Tomoichiro Asano and Yoshitomo Oka and Ikuro Maruyama and Kuratsu, {Jun Ichi}",

note = "Funding Information: This research was supported in part by grants from the Ministry of Education, Science and Culture of Japan (to Masanori Nakata, Ikuro Maruyama, Jun-ichi Kuratsu, Yoshitomo Oka,) and a Jichi Medical School Young Investigator Award (to Masanori Nakata).",

year = "2004",

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doi = "10.1016/j.canlet.2003.11.020",

language = "English",

volume = "208",

pages = "115--122",

journal = "Cancer Letters",

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T1 - Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398

AU - Obara, Soichi

AU - Nakata, Masanori

AU - Takeshima, Hideo

AU - Katagiri, Hideki

AU - Asano, Tomoichiro

AU - Oka, Yoshitomo

AU - Maruyama, Ikuro

AU - Kuratsu, Jun Ichi

N1 - Funding Information: This research was supported in part by grants from the Ministry of Education, Science and Culture of Japan (to Masanori Nakata, Ikuro Maruyama, Jun-ichi Kuratsu, Yoshitomo Oka,) and a Jichi Medical School Young Investigator Award (to Masanori Nakata).

PY - 2004/5/10

Y1 - 2004/5/10

N2 - We report the increased activity and expression of the ILK protein in human glioblastomas and demonstrate that ILK activity is regulated by PTEN. The transfection of wild type-PTEN into the glioblastoma cell line U-251 MG altered the localization of ILK in the cell membrane; transfection with PTEN down-regulated PKB/Akt-Ser-473 phosphorylation via the inhibition of ILK-signaling. Our results suggest that ILK is critical for the PTEN-sensitive regulation of PKB/Akt-dependent cell survival. The selective COX-2 inhibitor NS-398 was found capable of down-regulating ILK and PKB/Akt phosphorylation. Our data indicate that inhibition of ILK signaling may be beneficial in the treatment of PTEN-deficient glioblastoma.

AB - We report the increased activity and expression of the ILK protein in human glioblastomas and demonstrate that ILK activity is regulated by PTEN. The transfection of wild type-PTEN into the glioblastoma cell line U-251 MG altered the localization of ILK in the cell membrane; transfection with PTEN down-regulated PKB/Akt-Ser-473 phosphorylation via the inhibition of ILK-signaling. Our results suggest that ILK is critical for the PTEN-sensitive regulation of PKB/Akt-dependent cell survival. The selective COX-2 inhibitor NS-398 was found capable of down-regulating ILK and PKB/Akt phosphorylation. Our data indicate that inhibition of ILK signaling may be beneficial in the treatment of PTEN-deficient glioblastoma.

KW - Glioblastoma

KW - ILK

KW - NS-398

KW - PKB/Akt-Serine 473

KW - PTEN

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M3 - Article

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AN - SCOPUS:11144227278

SN - 0304-3835

VL - 208

SP - 115

EP - 122

JO - Cancer Letters

JF - Cancer Letters

IS - 1

ER -

Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398

Abstract

Keywords

UN SDGs

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