First Isolation of the Growth Hormone Secretagogue Receptor from Pituitary Tissue
The receptor responsible for GHRP-6, MK-677, and related GH secretagogues was solubilized and characterized for the first time, revealing a ~255 kDa G-protein-coupled complex.
Quick Facts
What This Study Found
The GH secretagogue receptor was solubilized as a ~255 kDa receptor-ligand-G-protein complex from porcine pituitary, confirming it is distinct from the GHRH receptor.
Key Numbers
How They Did This
Porcine anterior pituitary membranes were solubilized with digitonin detergent, and the GH secretagogue receptor complex was characterized by size and binding properties.
Why This Research Matters
Isolating the GH secretagogue receptor was essential for understanding how GHRPs and MK-677 work and for the eventual cloning of the ghrelin receptor (GHS-R).
The Bigger Picture
This biochemical characterization paved the way for the molecular cloning of the GHS receptor and the subsequent discovery of ghrelin as its natural ligand — transforming our understanding of growth hormone regulation.
What This Study Doesn't Tell Us
In vitro biochemistry using solubilized membranes. Molecular mass estimate may include detergent-associated artifacts. Porcine receptor may differ from human.
Questions This Raises
- ?What is the molecular identity of this receptor?
- ?Is this the same receptor through which the body naturally regulates GH secretion?
Trust & Context
- Key Stat:
- ~255 kDa receptor complex The GH secretagogue receptor was solubilized as a large complex including receptor, ligand, and G-protein
- Evidence Grade:
- Moderate biochemical evidence from a technically demanding receptor solubilization. Important milestone in receptor characterization.
- Study Age:
- Published in 1996, this was a key step toward the cloning of GHS-R1a and the discovery of ghrelin (1999).
- Original Title:
- Solubilization and characterization of a growth hormone secretagogue receptor from porcine anterior pituitary membranes.
- Published In:
- Biochemical and biophysical research communications, 225(3), 939-45 (1996)
- Authors:
- Pomés, A(2), Pong, S S(5), Schaeffer, J M(2)
- Database ID:
- RPEP-00379
Evidence Hierarchy
Frequently Asked Questions
What is the GH secretagogue receptor?
It's the receptor (now called GHS-R1a) that GHRP-6, hexarelin, MK-677, and the natural hormone ghrelin all bind to in order to stimulate growth hormone release. It's different from the GHRH receptor, which is why these compounds can be combined synergistically.
Why was isolating this receptor important?
Physically isolating the receptor proved it was a real, distinct protein — not just a variation of known receptors. This enabled its molecular cloning and led directly to the discovery of ghrelin, its natural ligand.
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Cite This Study
https://rethinkpeptides.com/research/RPEP-00379APA
Pomés, A; Pong, S S; Schaeffer, J M. (1996). Solubilization and characterization of a growth hormone secretagogue receptor from porcine anterior pituitary membranes.. Biochemical and biophysical research communications, 225(3), 939-45.
MLA
Pomés, A, et al. "Solubilization and characterization of a growth hormone secretagogue receptor from porcine anterior pituitary membranes.." Biochemical and biophysical research communications, 1996.
RethinkPeptides
RethinkPeptides Research Database. "Solubilization and characterization of a growth hormone secr..." RPEP-00379. Retrieved from https://rethinkpeptides.com/research/pomes-1996-solubilization-and-characterization-of
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Study data sourced from PubMed, a service of the U.S. National Library of Medicine, National Institutes of Health.
This study breakdown was produced by the RethinkPeptides research team. We analyze and report published research findings without making health recommendations. All interpretations are based solely on the published abstract and study data.