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J. Biol. Chem., Vol. 278, Issue 11, 8877-8880, March 14, 2003

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Ghrelin Can Bind to a Species of High Density Lipoprotein Associated with Paraoxonase^*

Nicholas J. Beaumont^§, Vernon O. Skinner, Tricia M.-M. Tan^¶, Bala S. Ramesh, Dominic J. Byrne, Gavin S. MacColl^**, Jeff N. Keen, Pierre M. Bouloux^¶**, Dimitri P. Mikhailidis, K. Richard Bruckdorfer, Mark P. Vanderpump^¶, and Kaila S. Srai

From the Departments of  Biochemistry and Molecular Biology and ^** Medicine, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, United Kingdom, the Departments of ^¶ Endocrinology and  Clinical Biochemistry, Royal Free Hospital NHS Trust, Pond Street, London NW3 2QG, United Kingdom, and the  School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom

Ghrelin is a 28-residue peptide hormone that is principally released from the stomach during fasting and prior to eating. Two forms are present in human plasma: the unmodified peptide and a less abundant acylated version, in which octanoic acid is attached to the third residue, a serine, via an ester linkage. The acylated form of ghrelin acts as a ligand for the growth hormone secretagogue receptor and can stimulate the release of growth hormone from the pituitary gland. It also initiates behavioral and metabolic adaptations to fasting. Here we show that an immobilized form of ghrelin specifically binds a species of high density lipoprotein associated with the plasma esterase, paraoxonase, and clusterin. Both free ghrelin and paraoxon, a substrate for paraoxonase, can inhibit this interaction. An endogenous species of ghrelin is found to co-purify with high density lipoprotein during density gradient centrifugation and subsequent gel filtration. This interaction links the orexigenic peptide hormone ghrelin to lipid transport and metabolism. Furthermore, the interaction of the esterified hormone ghrelin with a species of HDL containing an esterase suggests a possible mechanism for the conversion of ghrelin to des-acyl ghrelin.

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