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Giant mitochondria do not fuse and exchange their contents with normal mitochondria
Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN, United States.
Linköping University, Faculty of Health Sciences. Linköping University, Department of Clinical and Experimental Medicine, Geriatric .
Department of Chemistry, University of Minnesota, 207 Pleasant St. SE, Minneapolis, MN, United States.
2008 (English)In: Experimental Cell Research, ISSN 0014-4827, Vol. 314, no 1, 164-172 p.Article in journal (Refereed) Published
Abstract [en]

Giant mitochondria accumulate within aged or diseased postmitotic cells as a consequence of insufficient autophagy, which is normally responsible for mitochondrial degradation. We report that giant mitochondria accumulating in cultured rat myoblasts due to inhibition of autophagy have low inner membrane potential and do not fuse with each other or with normal mitochondria. In addition to the low inner mitochondrial membrane potential in giant mitochondria, the quantity of the OPA1 mitochondrial fusion protein in these mitochondria was low, but the abundance of mitofusin-2 (Mfn2) remained unchanged. The combination of these factors may explain the lack of mitochondrial fusion in giant mitochondria and imply that the dysfunctional giant mitochondria cannot restore their function by fusing and exchanging their contents with fully functional mitochondria. These findings have important implications for understanding the mechanisms of accumulation of age-related mitochondrial damage in postmitotic cells. © 2007 Elsevier Inc. All rights reserved.

Place, publisher, year, edition, pages
2008. Vol. 314, no 1, 164-172 p.
Keyword [en]
Giant mitochondria, L6 rat myoblasts, Mitochondrial fusion proteins, Mitochondrial membrane potential, Mitofusin-2, OPA1
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-47266DOI: 10.1016/j.yexcr.2007.09.013OAI: diva2:268162
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2011-01-11

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