Inhibition of TRPM2 function by PARP inhibitors protects cells from oxidative stress-induced death

Research output: Contribution to journalReview article

21 Citations (Scopus)

Abstract

TRPM2 is a member of the transient receptor potential (TRP) protein superfamily of calcium-permeable, voltage-independent ion channels expressed in nonexcitable cells. Activation of TRPM2 by oxidative stress results in calcium influx and susceptibility to cell death, whereas inhibition of TRPM2 function enhances cell survival. In the present edition of this journal, Fonfria et al. demonstrate a role for poly(ADP ribose) polymerase (PARP) as a mediator between oxidative stress and TRPM2 activation. They present evidence that inhibition of either PARP or TRPM2 protects cells from plasma membrane damage and cell death. The therapeutic implications of this important observation are discussed.

Original languageEnglish (US)
Pages (from-to)515-516
Number of pages2
JournalBritish Journal of Pharmacology
Volume143
Issue number5
DOIs
StatePublished - Nov 1 2004

Fingerprint

Poly(ADP-ribose) Polymerases
Oxidative Stress
Cell Death
Cell Membrane
Calcium
Plasma Cells
Ion Channels
Cell Survival
Observation
Proteins
Poly(ADP-ribose) Polymerase Inhibitors
Therapeutics

All Science Journal Classification (ASJC) codes

  • Pharmacology

Cite this

@article{5260c2d418ba464781d0fd0b3750d83e,
title = "Inhibition of TRPM2 function by PARP inhibitors protects cells from oxidative stress-induced death",
abstract = "TRPM2 is a member of the transient receptor potential (TRP) protein superfamily of calcium-permeable, voltage-independent ion channels expressed in nonexcitable cells. Activation of TRPM2 by oxidative stress results in calcium influx and susceptibility to cell death, whereas inhibition of TRPM2 function enhances cell survival. In the present edition of this journal, Fonfria et al. demonstrate a role for poly(ADP ribose) polymerase (PARP) as a mediator between oxidative stress and TRPM2 activation. They present evidence that inhibition of either PARP or TRPM2 protects cells from plasma membrane damage and cell death. The therapeutic implications of this important observation are discussed.",
author = "Barbara Miller",
year = "2004",
month = "11",
day = "1",
doi = "10.1038/sj.bjp.0705923",
language = "English (US)",
volume = "143",
pages = "515--516",
journal = "British Journal of Pharmacology",
issn = "0007-1188",
publisher = "Wiley-Blackwell",
number = "5",

}

Inhibition of TRPM2 function by PARP inhibitors protects cells from oxidative stress-induced death. / Miller, Barbara.

In: British Journal of Pharmacology, Vol. 143, No. 5, 01.11.2004, p. 515-516.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Inhibition of TRPM2 function by PARP inhibitors protects cells from oxidative stress-induced death

AU - Miller, Barbara

PY - 2004/11/1

Y1 - 2004/11/1

N2 - TRPM2 is a member of the transient receptor potential (TRP) protein superfamily of calcium-permeable, voltage-independent ion channels expressed in nonexcitable cells. Activation of TRPM2 by oxidative stress results in calcium influx and susceptibility to cell death, whereas inhibition of TRPM2 function enhances cell survival. In the present edition of this journal, Fonfria et al. demonstrate a role for poly(ADP ribose) polymerase (PARP) as a mediator between oxidative stress and TRPM2 activation. They present evidence that inhibition of either PARP or TRPM2 protects cells from plasma membrane damage and cell death. The therapeutic implications of this important observation are discussed.

AB - TRPM2 is a member of the transient receptor potential (TRP) protein superfamily of calcium-permeable, voltage-independent ion channels expressed in nonexcitable cells. Activation of TRPM2 by oxidative stress results in calcium influx and susceptibility to cell death, whereas inhibition of TRPM2 function enhances cell survival. In the present edition of this journal, Fonfria et al. demonstrate a role for poly(ADP ribose) polymerase (PARP) as a mediator between oxidative stress and TRPM2 activation. They present evidence that inhibition of either PARP or TRPM2 protects cells from plasma membrane damage and cell death. The therapeutic implications of this important observation are discussed.

UR - http://www.scopus.com/inward/record.url?scp=8744277793&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=8744277793&partnerID=8YFLogxK

U2 - 10.1038/sj.bjp.0705923

DO - 10.1038/sj.bjp.0705923

M3 - Review article

C2 - 15514246

AN - SCOPUS:8744277793

VL - 143

SP - 515

EP - 516

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 5

ER -