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A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition.

Publication ,  Journal Article
Devinney, MJ; Malaiyandi, LM; Vergun, O; DeFranco, DB; Hastings, TG; Dineley, KE
Published in: Cell Calcium
May 2009

Intracellular Zn(2+) toxicity is associated with mitochondrial dysfunction. Zn(2+) depolarizes mitochondria in assays using isolated organelles as well as cultured cells. Some reports suggest that Zn(2+)-induced depolarization results from the opening of the mitochondrial permeability transition pore (mPTP). For a more detailed analysis of this relationship, we compared Zn(2+)-induced depolarization with the effects of Ca(2+) in single isolated rat liver mitochondria monitored with the potentiometric probe rhodamine 123. Consistent with previous work, we found that relatively low levels of Ca(2+) caused rapid, complete and irreversible loss of mitochondrial membrane potential, an effect that was diminished by classic inhibitors of mPT, including high Mg(2+), ADP and cyclosporine A. Zn(2+) also depolarized mitochondria, but only at relatively high concentrations. Furthermore Zn(2+)-induced depolarization was slower, partial and sometimes reversible, and was not affected by inhibitors of mPT. We also compared the effects of Ca(2+) and Zn(2+) in a calcein-retention assay. Consistent with the well-documented ability of Ca(2+) to induce mPT, we found that it caused rapid and substantial loss of matrix calcein. In contrast, calcein remained in Zn(2+)-treated mitochondria. Considered together, our results suggest that Ca(2+) and Zn(2+) depolarize mitochondria by considerably different mechanisms, that opening of the mPTP is not a direct consequence of Zn(2+)-induced depolarization, and that Zn(2+) is not a particularly potent mitochondrial inhibitor.

Duke Scholars

Published In

Cell Calcium

DOI

EISSN

1532-1991

Publication Date

May 2009

Volume

45

Issue

5

Start / End Page

447 / 455

Location

Netherlands

Related Subject Headings

  • Zinc
  • Ruthenium Red
  • Rhodamine 123
  • Rats, Sprague-Dawley
  • Rats
  • Permeability
  • Mitochondrial Permeability Transition Pore
  • Mitochondrial Membrane Transport Proteins
  • Mitochondria, Liver
  • Membrane Potential, Mitochondrial
 

Citation

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Devinney, M. J., Malaiyandi, L. M., Vergun, O., DeFranco, D. B., Hastings, T. G., & Dineley, K. E. (2009). A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition. Cell Calcium, 45(5), 447–455. https://doi.org/10.1016/j.ceca.2009.03.002
Devinney, Michael J., Latha M. Malaiyandi, Olga Vergun, Donald B. DeFranco, Teresa G. Hastings, and Kirk E. Dineley. “A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition.Cell Calcium 45, no. 5 (May 2009): 447–55. https://doi.org/10.1016/j.ceca.2009.03.002.
Devinney MJ, Malaiyandi LM, Vergun O, DeFranco DB, Hastings TG, Dineley KE. A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition. Cell Calcium. 2009 May;45(5):447–55.
Devinney, Michael J., et al. “A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition.Cell Calcium, vol. 45, no. 5, May 2009, pp. 447–55. Pubmed, doi:10.1016/j.ceca.2009.03.002.
Devinney MJ, Malaiyandi LM, Vergun O, DeFranco DB, Hastings TG, Dineley KE. A comparison of Zn2+- and Ca2+-triggered depolarization of liver mitochondria reveals no evidence of Zn2+-induced permeability transition. Cell Calcium. 2009 May;45(5):447–455.
Journal cover image

Published In

Cell Calcium

DOI

EISSN

1532-1991

Publication Date

May 2009

Volume

45

Issue

5

Start / End Page

447 / 455

Location

Netherlands

Related Subject Headings

  • Zinc
  • Ruthenium Red
  • Rhodamine 123
  • Rats, Sprague-Dawley
  • Rats
  • Permeability
  • Mitochondrial Permeability Transition Pore
  • Mitochondrial Membrane Transport Proteins
  • Mitochondria, Liver
  • Membrane Potential, Mitochondrial