Interaction between myoglobin and mitochondria in rat skeletal muscle

Tatsuya Yamada, Yasuro Furuichi, Hisashi Takakura, Takeshi Hashimoto, Yoshiteru Hanai, Thomas Jue, Kazumi Masuda

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


The mechanisms underlying subcellular oxygen transport mediated by myoglobin (Mb) remain unclear. Recent evidence suggests that, in the myocardium, transverse diffusion of Mb is too slow to effectively supply oxygen to meet the immediate mitochondrial oxygen demands at the onset of muscle contractions. The cell may accommodate the demand by maintaining the distribution of Mb to ensure a sufficient O2 supply in the immediate vicinity of the mitochondria. The present study has verified the co-localization of Mb with mitochondria by using biochemical histological and electron microscopy analyses. Immunohistochemical and electron microscopy analysis indicates a co-localization of Mb with mitochondria. Western blotting confirms the presence of Mb colocalizes with the mitochondrial fraction and appears more prominently in slow-twitch oxidative than in fast-twitch glycolytic muscle. In particular, Mb interacts with cytochrome c oxidase-subunit IV. These results suggest that a direct Mb-mediated O2 delivery to the mitochondria, which may play a potentially significant role for respiration.

Original languageEnglish (US)
Pages (from-to)490-497
Number of pages8
JournalJournal of Applied Physiology
Issue number4
StatePublished - Feb 15 2013


  • Cytochrome c oxidase-subunit IV
  • Mitochondrial respiration
  • Oxygen transport

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)


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