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C200575200v1
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Papers In Press, published online ahead of print January 16, 2003
J. Biol. Chem, 10.1074/jbc.C200575200
Submitted on October 11, 2002
Revised on January 10, 2003
Accepted on January 16, 2003

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

Department of Biochemistry and Molecular Biology, Royal Free and University College Medical School, London NW3 2PF

Corresponding Author: n.beaumont{at}rfc.ucl.ac.uk

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. Only the acylated form of ghrelin acts as a ligand for the growth hormone secretagogue (GHS) receptor. It stimulates the release of growth hormone from the pituitary gland and initiates behavioural 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. Some endogenous ghrelin is found to co-purify with HDL during density gradient centrifugation. This interaction links the orexigenic peptide hormone ghrelin to lipid transport and a plasma enzyme that breaks down oxidised lipids in LDL. Furthermore, the interaction of the esterified hormone ghrelin with a species containing an esterase suggests a possible mechanism for the conversion of ghrelin to des-acyl ghrelin.


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