Cited by 265Mitochondrial Function and PathologyCell death mechanisms and regulationCardiac Ischemia and Reperfusion

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Zn2+ Induces Permeability Transition Pore Opening and Release of Pro-apoptotic Peptides from Neuronal Mitochondria

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Jiang, Dongmei, Sullivan, Patrick G., Sensi, Stefano L., Steward, Oswald, Weiss, John H.·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m108834200

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Abstract

Rapid entry of Ca(2+) or Zn(2+) kills neurons. Mitochondria are major sites of Ca(2+)-dependent toxicity. This study examines Zn(2+)-initiated mitochondrial cell death signaling. 10 nm Zn(2+) induced acute swelling of isolated mitochondria, which was much greater than that induced by higher Ca(2+) levels. Zn(2+) entry into mitochondria was dependent upon the Ca(2+) uniporter, and the consequent swelling resulted from opening of the mitochondrial permeability transition pore. Confocal imaging of intact neurons revealed entry of Zn(2+) (with Ca(2+)) to cause pronounced mitochondrial swelling, which was far greater than that induced by Ca(2+) entry alone. Further experiments compared the abilities of Zn(2+) and Ca(2+) to induce mitochondrial release of cytochrome c (Cyt-c) or apoptosis-inducing factor. In isolated mitochondria, 10 nm Zn(2+) exposures induced Cyt-c release. Induction of Zn(2+) entry into cortical neurons resulted in distinct increases in cytosolic Cyt-c immunolabeling and in cytosolic and nuclear apoptosis-inducing factor labeling within 60 min. In comparison, higher absolute [Ca(2+)](i) rises were less effective in inducing release of these factors. Addition of the mitochondrial permeability transition pore inhibitors cyclosporin A and bongkrekic acid decreased Zn(2+)-dependent release of the factors and attenuated neuronal cell death as assessed by trypan blue staining 5-6 h after the exposures.

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Authors: Jiang, D., Sullivan, P. G., Sensi, S. L., Steward, O., & Weiss, J. H.
Affiliations: University of California, Irvine (US)
Corresponding author: Weiss, John H.
ORCID: Sullivan, Patrick G.
Sensi, Stefano L.
Steward, Oswald
Weiss, John H.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2001-12
Volume: 276
Issue: 50
Pages: 47524-47529
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m108834200
OpenAlex: W2057520074
Cited by: 265
References: 34
Citations by year: 2026: 5 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 4 · 2021: 11 · 2020: 11 · 2019: 11 · 2018: 11 · 2017: 9 · 2016: 6 · 2015: 14 · 2014: 5 · 2013: 9 · 2012: 19
FWCI: 4.42
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6878 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Alzheimer's Association
National Institutes of Health (5k02ag000836-05, 5r01ns032280-07, 5r01ns030884-11, NS30884)
National Institute on Aging (AG00836, AG 00919, 2T32 AG 00096, T32AG000096)
National Institute of Neurological Disorders and Stroke (NS 30884, NS-32280)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
Keywords: zinc, mitochondrial permeability transition pore, mitochondrial swelling, cytochrome c release, apoptosis-inducing factor, neuronal cell death, calcium uniporter, cyclosporine, bongkrekic acid, cortical neurons
MeSH terms: Animals, Anti-Bacterial Agents, Bongkrekic Acid, Brain, Calcium, Cations, Cytochrome c Group, Cytoplasm, Cytosol, Dose-Response Relationship, Drug, Enzyme Inhibitors, Flavoproteins, Humans, Immunohistochemistry, Male, Membrane Proteins, Mitochondria, Necrosis, Neurons, Time Factors, Trypan Blue, Zinc, Cyclosporine, Rats, Sprague-Dawley, Apoptosis, Microscopy, Confocal, Apoptosis Inducing Factor, Rats

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Zn2+ Induces Permeability Transition Pore Opening and Release of Pro-apoptotic Peptides from Neuronal Mitochondria

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