Shallow Intracellular O2 Gradients and Absence of Perimitochondrial O2 “Wells” in Heavily Working Red Muscle

  • T. E. J. Gayeski
  • C. R. Honig
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 200)


It is generally believed that the principal site of resistance to O2 mass transport resides within the tissue cells.1,2 In this view the ΔPO2 from sarcolemma to cell interior greatly exceeds the ΔPO2 from red cell to interstitium. Precisely the reverse is suggested by recent mathematical models of O2 release from capillaries,3,4,5,6 and by measurements on suspensions of cardiac myocytes in vitro.7 This paper reports the first measurements with sufficient spatial resolution to map intracellular O2 gradients in vivo. We find that the large-scale O2 gradient from sarcolemma to cell interior is indeed shallow, and is not significantly perturbed by small-scale gradients around individual mitochondria.


Cell Interior Gracilis Muscle Fixed Site Sufficient Spatial Resolution Individual Mitochondrion 
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  1. 1.
    A. Krogh, The supply of 02 to the tissues and the regulation of the capillary circulation, J. Physiol. (Lond.), 52: 457 (1919).Google Scholar
  2. 2.
    J.A. Wittenberg, Myoglobin-facilitated oxygen diffusion: Role of myoglobin in oxygen entry into muscle, Physiol. Rev. 50: 559 (1970).Google Scholar
  3. 3.
    J.D. Hellums, The resistance of oxygen transport in the capillaries relative to that in the surrounding tissue, Microvasc. Res., 13: 131 (1977).Google Scholar
  4. 4.
    A. Clark Jr., W. Federspiel, P.A.A. Clark, and G.R. Cokelet, Oxygen delivery from red cells, Biophys. J., 47: 171 (1985).PubMedCrossRefGoogle Scholar
  5. 5.
    A. Clark Jr., and P.A.A. Clark, The end-points of the oxygen path: transport resistance in red cells and mitochondria, Adv. Exper. Med. Biol.Google Scholar
  6. 6.
    C.R. Honig, T.E.J. Gayeski, W. Federspiel, A. Clark Jr., and P. Clark, Muscle 02 gradients from hemoglobin to cytochrome; new concepts, new complexities, Adv. Exp. Med. Biol., 169: 23 (1984).PubMedGoogle Scholar
  7. 7.
    B.A. Wittenberg, and J.A. Witenberg, Oxygen pressure gradients in isolated cardiac myocytes, J. Biol. Chem.Google Scholar
  8. 8.
    T.E.J. Gayeski, R.J. Connett, and C.R. Honig, 02 transport in the rest-work transition illustrates new functions for myoglobin, Am. J. Physiol., 248: in press (1985).Google Scholar
  9. 9.
    A. Clark, and P.A.A. Clark, Capture of spatially homogenous chemical reactions in tissue by freezing, Biophys. J., 42: 25 (1983).PubMedCrossRefGoogle Scholar
  10. 10.
    T.E.J. Gayeski, A cryogenic microspectrophotometric method for measuring myoglobin saturation in subcellular volumes; Application to resting dog gracilis muscle, Ph.D. Dissertation, University of Rochester, Rochester, NY (1982).Google Scholar
  11. 11.
    R.J. Connett, T.E.J. Gayeski, and C.R. Honig, An upper bound on the minimum P02 for 02 consumption in red muscle, Adv. Exper. Med. Biol.Google Scholar
  12. 12.
    W.J. Federspiel, The effect of myoglobin concentration on muscle-cell P02 gradients, Adv. Exper. Med. Biol., 180: 539 (1984).Google Scholar
  13. 13.
    A. Clark Jr., and P.A.A. Clark, Local oxygen gradients produced by mitochondria in tissue, Biophys. J., accepted.Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • T. E. J. Gayeski
    • 1
  • C. R. Honig
    • 1
  1. 1.School of Medicine and DentistryThe University of RochesterRochesterUSA

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