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Amendment history:
  • Correction (August 1993)
  • Correction (May 1993)

Research Article Free access | 10.1172/JCI116243

Influence of the high-affinity growth hormone (GH)-binding protein on plasma profiles of free and bound GH and on the apparent half-life of GH. Modeling analysis and clinical applications.

J D Veldhuis, M L Johnson, L M Faunt, M Mercado, and G Baumann

Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville.

Find articles by Veldhuis, J. in: JCI | PubMed | Google Scholar

Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville.

Find articles by Johnson, M. in: JCI | PubMed | Google Scholar

Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville.

Find articles by Faunt, L. in: JCI | PubMed | Google Scholar

Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville.

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Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville.

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Published February 1, 1993 - More info

Published in Volume 91, Issue 2 on February 1, 1993
J Clin Invest. 1993;91(2):629–641. https://doi.org/10.1172/JCI116243.
© 1993 The American Society for Clinical Investigation
Published February 1, 1993 - Version history
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Abstract

The discovery of a specific high-affinity growth hormone (GH) binding protein (GH-BP) in plasma adds complexity to the dynamics of GH secretion and clearance. Intuitive predictions are that such a protein would damp sharp oscillations in GH concentrations otherwise caused by bursts of GH secretion into the blood volume, prolong the apparent half-life of circulating GH, and contribute a reservoir function. To test these implicit considerations, we formulated an explicit mathematical model of pulsatile GH secretion and clearance in the presence of absence of a specific high-affinity GH-BP. Simulation experiments revealed that the pulsatile mode of physiological GH secretion creates a highly dynamic (nonequilibrium) system, in which the half-life of free GH, its instantaneous secretion rate, and the GH-BP affinity and capacity all contribute to defining momentary levels of free, bound, and total GH, the percentage of GH bound to protein, and the percentage occupancy of GH-BP [corrected]. In contrast, the amount of free GH at equilibrium is specified only by the GH distribution volume and secretion rate and the half-life of free hormone. We conclude that the in vivo dynamics of GH secretion, trapping, and clearance from the circulation offer a variety of regulatory loci at which the time structure of free, bound, and total GH delivery to target tissues can be controlled physiologically.

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