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Submitted on July 26, 2004
Accepted on November 19, 2004
Department of Biochemistry and Nutrition, Faculty of Medicine, Université Libre de Bruxelles, Brussels, Belgium
* To whom correspondence should be addressed. E-mail: cdelport{at}ulb.ac.be.
Ghrelin, a ligand of the growth hormone secretagogue receptor (GHS-R 1a), is a 28 amino acid peptide with an unusual octanoyl group on Ser3, crucial for its biological activity. For the first time, ghrelin and GHS-R 1b, a truncated variant of the receptor resulting from alternative splicing, but not GHS-R 1a, mRNAs were detected in the human erythroleukemic cell line HEL. Two antibodies, used for RIA (RIA), were directed against octanoylated and total (octanoylated and desoctanoylated) ghrelin and the recognized epitopes characterized. Using RP-HPLC analysis followed by RIA, we demonstrated that octanoylated and desoctanoylated ghrelins were present in HEL cells and their culture medium, of which more than 90% was octanoylated. The ghrelin levels were not affected after 24 h treatment with sodium butyrate, phorbol 12-myristate 13-acetate (PMA), or forskolin, but a significant 3-fold increase of desoctanoylated ghrelin was detected into the culture medium after 48 h treatment with sodium butyrate. The anti-ghrelin SB801 and SB969 antisera inhibited by 24% and 39% HEL cell proliferation after 72 h, respectively.
Taken together, these data suggested that endogenous ghrelin stimulated HEL cell proliferation by an autocrine pathway involving an unidentified receptor, distinct from GHS-R1a, and that the HEL cell line represents a unique model to study the octanoylation of ghrelin.
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