PMID: 9422344Jan 9, 1998Paper

Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid beta-peptide

Journal of Neurochemistry
A J Bruce-KellerM P Mattson

Abstract

The bcl-2 protooncogene product possesses antiapoptotic properties in neuronal and nonneuronal cells. Recent data suggest that Bcl-2's potency as a survival factor hinges on its ability to suppress oxidative stress, but neither the subcellular site(s) nor the mechanism of its action is known. In this report electron paramagnetic resonance (EPR) spectroscopy analyses were used to investigate the local effects of Bcl-2 on membrane lipid peroxidation. Using hydrogen peroxide (H2O2) and amyloid beta-peptide (A beta) as lipoperoxidation initiators, we determined the loss of EPR-detectable paramagnetism of nitroxyl stearate (NS) spin labels 5-NS and 12-NS. In intact cell preparations and postnuclear membrane fractions, A beta and H2O2 induced significant loss of 5-NS and 12-NS signal amplitude in control PC12 cells, but not PC12 cells expressing Bcl-2. Cells were subjected to differential subcellular fractionation, yielding preparations of plasma membrane and mitochondria. In preparations derived from Bcl-2-expressing cells, both fractions contained Bcl-2 protein. 5-NS and 12-NS signals were significantly decreased following A beta and H2O2 exposure in control PC12 mitochondrial membranes, and Bcl-2 largely prevented these effects. P...Continue Reading

Citations

Feb 4, 1999·Journal of Neurochemistry·I I Kruman, M P Mattson
Jan 5, 2000·Physiological Reviews·D G Nicholls, S L Budd
May 20, 2000·Annals of the New York Academy of Sciences·J P BlassG E Gibson
Sep 14, 2001·The Journal of Biological Chemistry·A ChengM P Mattson
Aug 3, 2002·Cell Proliferation·Alexander M SapozhnikovWilliam G Telford
Jan 11, 2005·Neurotoxicity Research·Tomás PalomoRichard M Kostrzewa
Mar 13, 2009·Journal of Cutaneous Pathology·Daniela TavianMaria E Clementi
Dec 3, 2013·Canadian Journal of Physiology and Pharmacology·Jia LiLinna Pan
Jun 18, 2014·BMC Complementary and Alternative Medicine·Saeed SamarghandianMohadeseh Hosseini
Apr 19, 2016·Journal of Asian Natural Products Research·Huo-Yun ChengXin-Sheng Yao
Aug 29, 2020·Dalton Transactions : an International Journal of Inorganic Chemistry·Mingxiao ShaoZhe Liu
Mar 7, 2001·Antioxidants & Redox Signaling·J M Villalba, P Navas
Aug 4, 2004·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Maria D'AlessioLina Ghibelli
Mar 21, 2006·Apoptosis : an International Journal on Programmed Cell Death·J ChenP X Chen
Feb 3, 2012·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ying LiuLin Yang
Nov 3, 2012·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·An-Sheng ChengTsu-Liang Chang
Apr 27, 2000·American Journal of Respiratory Cell and Molecular Biology·N S WardJ A Elias
Sep 5, 2006·Apoptosis : an International Journal on Programmed Cell Death·Ozgur Kutuk, Huveyda Basaga
Mar 4, 2011·Journal of Veterinary Science·Mustafa Yavuz GulbaharUnal Parlak
Mar 19, 2003·Journal of Neurochemistry·Krishna Pada SarkerIkuro Maruyama
Sep 3, 2009·Annals of the New York Academy of Sciences·Min Kyung KangHyong Joo Lee
Apr 9, 2016·Chemical Communications : Chem Comm·Miaomiao KangBen Zhong Tang
Jul 9, 2011·Pharmacological Reviews·Grace E Stutzmann, Mark P Mattson
Oct 11, 2003·Journal of Neurochemistry·Daniel C LuEdward H Koo
Jan 23, 2008·Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology·Jee Eun YeoSoo Kyung Kang

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