The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Dynamin‐related protein 1 (Drp1)‐mediated diastolic dysfunction in myocardial ischemia‐reperfusion injury: therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission
Open accessAbstract
Mitochondrial fission, regulated by dynamin‐related protein‐1 (Drp1), is a newly recognized determinant of mitochondrial function, but its contribution to left ventricular (LV) impairment following ischemia‐reperfusion (IR) injury is unknown. We report that Drp1 activation during IR results in LV dysfunction and that Drp1 inhibition is beneficial. In both isolated neonatal murine cardiomyocytes and adult rat hearts (Langendorff preparation) mitochondrial fragmentation and swelling occurred within 30 min of IR Drp1‐S637 (serine 637) dephosphorylation resulted in Drp1 mitochondrial translocation and increased mitochondrial fission. The Drp1 inhibitor Mdivi‐1 preserved mitochondrial morphology, reduced cytosolic calcium, and prevented cell death. Drp1 siRNA similarly preserved mitochondrial morphology. In Langendorff hearts, Mdivi‐1 reduced mitochondrial reactive oxygen species, improved LV developed pressure (92±5 vs. 28±10 mmHg, P <0.001), and lowered LV end diastolic pressure (10±1 vs. 86±13 mmHg, P <0.001) following IR Mdivi‐1 was protective if administered prior to or following ischemia. Because Drp1‐S637 dephosphorylation is calcineurin sensitive, we assessed the effects of a calcineurin inhibitor, FK506. FK506 treatment prior to IR prevented Drp1‐S637 dephosphorylation and preserved cardiac function. Likewise, therapeutic hypothermia (30°C) inhibited Drp1‐S637 dephosphorylation and preserved mitochondrial morphology and myocardial function. Drp1 inhibition is a novel strategy to improve myocardial function following IR.—Sharp, W. S., Fang, Y. H., Han, M., Zhang, H. J., Hong, Z., Banathy, A., Morrow, E., Ryan, J. J., Archer, S. L. Dynamin‐related protein 1 (Drp1)‐mediated diastolic dysfunction in myocardial ischemia‐reperfusion injury: therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission. FASEB J. 28, 316–326 (2014). www.fasebj.org
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Cites
Zipes, D. P., & Wellens, H. J. J. (1998) · Circulation · doi:10.1161/01.cir.98.21.2334 · Cited by 2,744
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 2×
“Mitochondrial fusion is regulated by a family of GTPases including optic atrophy protein and mitofusin 1 and 2 (Mfn1 and Mfn2), while fission is largely regulated by the GTPase dynamin-related protein 1 (Drp1) and the Drp1 targeting molecule fission 1 (Fis1) (10, 11).”
BackgroundWriting Group Members, Roger, V. L., Go, A. S., Lloyd-Jones, D. M., Benjamin, E. J., Berry, J. D., Borden, W. B., Bravata, D. M., Dai, S., Ford, E. S., et al. (2012) · Circulation · doi:10.1161/cir.0b013e3182456d46 · Cited by 1,512
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110
Inhibiting Mitochondrial Fission Protects the Heart Against Ischemia/Reperfusion Injury
Ong, S.-B., Subrayan, S., Lim, S. Y., Yellon, D. M., Davidson, S. M., & Hausenloy, D. J. (2010) · Circulation · doi:10.1161/circulationaha.109.906610 · Cited by 986
Zhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.198 · Cited by 370
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The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Mitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306
Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms
Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870
Distinct fission signatures predict mitochondrial degradation or biogenesis.
Kleele, T., Rey, T., Winter, J., Zaganelli, S., Mahecic, D., Perreten Lambert, H., Ruberto, F. P., Nemir, M., Wai, T., Pedrazzini, T., et al. (2021) · Nature · doi:10.1038/s41586-021-03510-6 · Cited by 794
How mitochondrial dynamism orchestrates mitophagy
Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311
Metadata
- Authors
- Sharp, W. W., Fang, Y. H., Han, M., Zhang, H. J., Hong, Z., Banathy, A., Morrow, E., Ryan, J. J., & Archer, S. L.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2013-09-27
- Volume
- 28
- Issue
- 1
- Pages
- 316-326
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1996739007
- Cited by
- 355
- References
- 9
- FWCI
- 8.47
- Type
- journal article
- Language
- en
- Open access
- green
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