Ghrelin binding to serum albumin and its biological impact

Daniela Lufrano, Sebastián A. Trejo, Ramiro E. Llovera, Mariano Salgueiro, Gimena Fernandez, Valentina Martínez Damonte, F. Luis González Flecha, Jesica Raingo, Mario R. Ermácora, Mario Perelló

    Research output: Contribution to journalArticleResearchpeer-review

    11 Citations (Scopus)


    © 2016 Elsevier Ireland Ltd Ghrelin is an octanoylated peptide hormone that plays a key role in the regulation of the body weight and glucose homeostasis. In plasma, ghrelin circulates bound to larger proteins whose identities are partially established. Here, we used size exclusion chromatography, mass spectrometry and isothermal titration microcalorimetry to show that ghrelin interacts with serum albumin. Furthermore, we found that such interaction displays an estimated dissociation constant (KD) in the micromolar range and involves albumin fatty-acid binding sites as well as the octanoyl moiety of ghrelin. Notably, albumin-ghrelin interaction reduces the spontaneous deacylation of the hormone. Both in vitro experiments—assessing ghrelin ability to inhibit calcium channels—and in vivo studies—evaluating ghrelin orexigenic effects—indicate that the binding to albumin affects the bioactivity of the hormone. In conclusion, our results suggest that ghrelin binds to serum albumin and that this interaction impacts on the biological activity of the hormone.
    Original languageEnglish
    Pages (from-to)130-140
    JournalMolecular and Cellular Endocrinology
    Publication statusPublished - 15 Nov 2016


    • Ghrelin
    • Hormone
    • Protein-protein interaction
    • Serum albumin
    • Transport


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