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J Biol Chem, Vol. 273, Issue 48, 31829-31836, November 27, 1998
From the The question of whether and to what extent the
in vivo cytochrome c oxidase (COX) capacity in
mammalian cells exceeds that required to support respiration is still
unresolved. In the present work, to address this question, a newly
developed approach for measuring the rate of COX activity, either as an
isolated step or as a respiratory chain-integrated step, has been
applied to a variety of human cell types, including several
tumor-derived semidifferentiated cell lines, as well as specialized
cells removed from the organism. KCN titration assays, carried out on
intact uncoupled cells, have clearly shown that the COX capacity is in low excess (16-40%) with respect to that required to support the endogenous respiration rate. Furthermore, measurements of
O2 consumption rate supported by 0.4 mM
tetramethyl-p-phenylenediamine in antimycin-inhibited uncoupled intact cells have given results that are fully consistent with those obtained in the KCN titration experiments. Similarly, KCN
titration assays on digitonin-permeabilized cells have revealed a COX
capacity that is nearly limiting (7-22% excess) for ADP + glutamate/malate-dependent respiration. The present
observations, therefore, substantiate the conclusion that the in
vivo control of respiration by COX is much tighter than has been
generally assumed on the basis of experiments carried out on isolated
mitochondria. This conclusion has important implications for
understanding the role of physiological or pathological factors in
affecting the COX threshold.
Low Reserve of Cytochrome c Oxidase Capacity in
Vivo in the Respiratory Chain of a Variety of Human Cell
Types
,,
, and
Division of Biology, California Institute of
Technology, Pasadena, California 91125 and the Institute of
Medical Biochemistry and Chemistry, University of Bari, Italy
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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