- Peptide CRATEFAVRSG, corresponding to amino acid residues 197-207 of rat Ghrelin receptor (Accession O08725). 2nd extracellular loop.
- Rat pancreas lysate, human SH-SY5Y neuroblastoma and mouse MS1 endothelial cells line lysates (1:200).
- Western blot analysis of rat pancreas (lanes 1 and 4), human SH-SY5Y neuroblastoma (lanes 2 and 5) and mouse MS1 endothelial (lanes 3 and 6) cells line lysates:1-3. Anti-Ghrelin Receptor (GHSR) (extracellular) Antibody (#AGR-031), (1:200).
4-6. Anti-Ghrelin Receptor (GHSR) (extracellular) Antibody, preincubated with Ghrelin Receptor/GHSR (extracellular) Blocking Peptide (#BLP-GR031).
- Rat and mouse hypothalamus (1:800).
- Human live neuroblastoma (SH-SY5Y) cells (1:50).
Ghrelin is a 28 amino acid peptide, acylated on a serine residue which is essential for its biological activity1,2. In rodents, an additional form of the peptide could be purified. The peptide is released from the stomach and exerts its effect on the ghrelin receptor (GHS-R). GHS-R is a member of the G-protein coupled receptor (GPCR) superfamily. Like all members, the receptor has seven transmembrane spanning domains and upon activation it stimulates phospholipase C, thereby increasing IP3 and intracellular Ca2+ levels1,3.
GHS-R is expressed in the hypothalamus, pituitary and hippocampus1,3.
Some of the actions of ghrelin include the stimulation of growth hormone release, food intake, fat accumulation, regulation of memory and learning, activation of reward-related pathways and neuroprotection to name a few1,3.
GHS-R 1b is a truncated form of the full length receptor which is also expressed. Although its exact functions are unknown, it is believed that it may be involved in downregulating signaling from the full length receptor4. In addition, it is overexpressed in lung cancer where it dimerizes with neurotensin receptor4,5.