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Volume 271, Number 45, Issue of November 8, 1996 pp. 27995-27998
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
The Signal Transduction Function for Oxidative Phosphorylation Is at Least Second Order in ADP

(Received for publication, August 20, 1996)

Jeroen A. L. Jeneson , Robert W. Wiseman , Hans V. Westerhoff ^¶ and Martin J. Kushmerick ^**

From the  NMR Research Laboratory, Department of Radiology, University of Washington School of Medicine, Seattle, Washington 98195, the ^¶ Department of Microbial Physiology, Faculty of Biology, Free University, NL-1081 HV Amsterdam, the Netherlands, the  E. C. Slater Institute, Biocenter, University of Amsterdam, NL-1018 TV Amsterdam, the Netherlands, the ^** Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195, and the   Center for Bioengineering, University of Washington School of Medicine, Seattle, Washington 98185

To maintain ATP constant in the cell, mitochondria must sense cellular ATP utilization and transduce this demand to F₀-F₁-ATPase. In spite of a considerable research effort over the past three decades, no combination of signal(s) and kinetic function has emerged with the power to explain ATP homeostasis in all mammalian cells. We studied this signal transduction problem in intact human muscle using ³¹P NMR spectroscopy. We find that the apparent kinetic order of the transduction function of the signal cytosolic ADP concentration ([ADP]) is at least second order and not first order as has been assumed. We show that amplified mitochondrial sensitivity to cytosolic [ADP] harmonizes with in vitro kinetics of [ADP] stimulation of respiration and explains ATP homeostasis also in mouse liver and canine heart. This result may well be generalizable to all mammalian cells.

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