Identification of tilapia ghrelin and its effects on growth hormone and prolactin release in the tilapia, Oreochromis mossambicus

Comp Biochem Physiol B Biochem Mol Biol. 2003 Jul;135(3):421-9. doi: 10.1016/s1096-4959(03)00109-x.

Abstract

We have identified ghrelin and cDNA encoding precursor protein from the stomach of a euryhaline tilapia, Oreochromis mossambicus. The sequence of 20-amino acid tilapia ghrelin is GSSFLSPSQKPQNKVKSSRI. The third serine residue was modified by n-decanoic acid. The carboxyl-terminal end of the peptide possessed an amide structure. RT-PCR analysis revealed high levels of gene expression in the stomach and low levels in the brain, kidney and gill. Tilapia ghrelin stimulated growth hormone (GH) and prolactin (PRL) release from the organ-cultured tilapia pituitary at a dose of 10 nM. Thus, a novel regulatory mechanism of GH secretion by gastric ghrelin seems to be conserved in the tilapia. Stimulation of PRL release by homologous ghrelin has been reported in human, bullfrog and eel, and suggests the presence of growth hormone secretagogue receptor not only on somatotrophs but also on PRL cells of the tilapia pituitary.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Gene Expression Profiling
  • Ghrelin
  • Growth Hormone / metabolism*
  • Humans
  • Molecular Sequence Data
  • Organ Specificity
  • Peptide Hormones / chemistry
  • Peptide Hormones / genetics
  • Peptide Hormones / isolation & purification
  • Peptide Hormones / metabolism*
  • Pituitary Gland / chemistry
  • Pituitary Gland / cytology
  • Pituitary Gland / metabolism
  • Prolactin / metabolism*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Sequence Homology
  • Stomach / chemistry
  • Tilapia / metabolism*

Substances

  • Ghrelin
  • Peptide Hormones
  • RNA, Messenger
  • Prolactin
  • Growth Hormone