Ghrelin gene products, receptors, and GOAT enzyme: biological and pathophysiological insight
- Manuel D Gahete,
- David Rincón-Fernández,
- Alicia Villa-Osaba,
- Daniel Hormaechea-Agulla,
- Alejandro Ibáñez-Costa,
- Antonio J Martínez-Fuentes,
- Francisco Gracia-Navarro,
- Justo P Castaño and
- Raúl M Luque
- Department of Cell Biology, Physiology and Immunology, Campus Universitario de Rabanales, Edificio Severo Ochoa (C6), Planta 3, University of Córdoba, 14014-Córdoba; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), University of Córdoba; Reina Sofia University Hospital, Córdoba; and CIBER Fisiopatología de la Obesidad y Nutrición (CIBERobn), Córdoba, Spain
- Correspondence should be addressed to R M Luque; Email: raul.luque{at}uco.es
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Figure 1
Overview of the human ghrelin gene structure and functionally relevant ghrelin gene derived variants (transcripts and putative peptides). Signal peptides are shown in green, ghrelin in grey, obestatin in blue and C-peptides in orange. In the case of the In1-ghrelin variant, the sequence that is shared with ghrelin (exon 1; 12-amino acids) is shown in grey and the unique sequence generated by the retention of intron 1 is shown in yellow.
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Figure 2
Overview of the post-transcriptional processing of native ghrelin and ghrelin gene derived peptides. During the post-translational modification of the native pre-pro-ghrelin, Ser3 can be acylated by GOAT. This modification of ghrelin is essential for binding to its only known receptor, GHSR1a, and to exert the majority of its biological functions. There is also a truncated orphan variant of the receptor, GHSR1b, with an unknown ligand and function. Additional ghrelin gene derived variants are likely to be similarly processed, generating a number of putative functional peptides, whose target receptors and biological actions are still to be elucidated.
- © 2013 Society for Endocrinology
