Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (546 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A 28-amino acid, acylated, orexigenic peptide that is a ligand for growth hormone secretagogue receptors. Ghrelin is widely expressed but primarily in the stomach in the adults. Ghrelin acts centrally to stimulate growth hormone secretion and food intake, and peripherally to regulate energy homeostasis. Its large precursor protein, known as appetite-regulating hormone or motilin-related peptide, contains ghrelin and obestatin.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Appetite-Regulating Hormone; Appetite Regulating Hormone; Gastric MLTRP; Motilin-Related Peptide; Motilin Related Peptide; GHRL Protein; PpMTLRP; Ghrelin Precursor.
Where it fits in the MeSH classification
- Broader topics
- Peptide Hormones
Related concepts
- Growth Hormone Secretagogue Receptors
Research landscape
PubMed indexes 9,110 records tagged with the MeSH heading “Ghrelin” (counts retrieved 2026-10-31). 1,724 of them (18.9%) were published from 2020 onward, and the busiest period so far is 2010-2019 with 4,397 records.
Reviews account for 1,401 records (15.4%) and meta-analyses for 71. Randomized controlled trials number 780 (8.6%) as a share of all records on the topic. Randomized trials make up a comparatively large share of this literature, which means many treatment questions have been tested directly.
Show the data
| Period | Records |
|---|---|
| through 1999 | 0 |
| 2000-2009 | 3,148 |
| 2010-2019 | 4,397 |
| 2020 onward | 1,724 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 1,401 | 15.4% |
| Meta-analyses | 71 | 0.8% |
| Randomized controlled trials | 780 | 8.6% |
Method: PubMed query "Ghrelin"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Liver-expressed antimicrobial peptide 2 antagonizes the effect of ghrelin in rodents | 2020 | Research article Design not recorded in structured metadata | 95 | cc by PMID 31539874 · DOI · PMC6839046 |
| Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode | 2020 | Research article Design not recorded in structured metadata | 64 | cc by PMID 32814772 · DOI · PMC7438500 |
| LEAP2 reduces postprandial glucose excursions and ad libitum food intake in healthy men | 2022 | Randomized controlled trial Design not recorded in structured metadata | 61 | cc by PMID 35492241 · DOI · PMC9043997 |
| Obestatin: canonical and unexpected functions | 2026 | Review article Design not recorded in structured metadata | 0 | cc by PMID 41784884 · DOI · PMC13167870 |
Liver-expressed antimicrobial peptide 2 antagonizes the effect of ghrelin in rodents [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Ghrelin, a stomach-derived peptide, promotes feeding and growth hormone (GH) secretion.
- Closing excerpt
- Together, these results reveal that LEAP2 inhibits central ghrelin functions and crosstalk between liver and stomach.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (145 words)
Ghrelin, a stomach-derived peptide, promotes feeding and growth hormone (GH) secretion. A recent study identified liver-expressed antimicrobial peptide 2 (LEAP2) as an endogenous inhibitor of ghrelin-induced GH secretion, but the effect of LEAP2 in the brain remained unknown. In this study, we showed that intracerebroventricular (i.c.v.) administration of LEAP2 to rats suppressed central ghrelin functions including Fos expression in the hypothalamic nuclei, promotion of food intake, blood glucose elevation, and body temperature reduction. LEAP2 did not inhibit neuropeptide Y (NPY)-induced food intake or des-acyl ghrelin-induced reduction in body temperature, indicating that the inhibitory effects of LEAP2 were specific for GHSR. Plasma LEAP2 levels varied according to feeding status and seemed to be dependent on the hepatic Leap2 expression. Furthermore, ghrelin suppressed the expression of hepatic Leap2 via AMPK activation. Together, these results reveal that LEAP2 inhibits central ghrelin functions and crosstalk between liver and stomach.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 31539874 · DOI · PMC6839046
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Ghrelin is a gastric peptide hormone with important physiological functions.
- Closing excerpt
- Mutagenesis analyses suggest that the interaction between the gap structure and the acyl acid moiety of ghrelin may participate in transforming the ghrelin receptor into an active conformation.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (137 words)
Ghrelin is a gastric peptide hormone with important physiological functions. The unique feature of ghrelin is its Serine 3 acyl-modification, which is essential for ghrelin's activity. However, it remains to be elucidated why the acyl-modification of ghrelin is necessary for activity. To address these questions, we solved the crystal structure of the ghrelin receptor bound to antagonist. The ligand-binding pocket of the ghrelin receptor is bifurcated by a salt bridge between E124 and R283. A striking feature of the ligand-binding pocket of the ghrelin receptor is a wide gap (crevasse) between the TM6 and TM7 bundles that is rich in hydrophobic amino acids, including a cluster of phenylalanine residues. Mutagenesis analyses suggest that the interaction between the gap structure and the acyl acid moiety of ghrelin may participate in transforming the ghrelin receptor into an active conformation.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 32814772 · DOI · PMC7438500
LEAP2 reduces postprandial glucose excursions and ad libitum food intake in healthy men [3]
Abstract reading summary — source excerpts
- Opening excerpt
- The gastric hormone ghrelin stimulates food intake and increases plasma glucose through activation of the growth hormone secretagogue receptor (GHSR).
- Closing excerpt
- In wild-type mice, plasma glucose and food intake are reduced by LEAP2 dosing, but not in GHSR-null mice, pointing to GHSR as a potential mediator of LEAP2's glucoregulatory and appetite-suppressing effects in mice.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (123 words)
The gastric hormone ghrelin stimulates food intake and increases plasma glucose through activation of the growth hormone secretagogue receptor (GHSR). Liver-expressed antimicrobial peptide 2 (LEAP2) has been proposed to inhibit actions of ghrelin through inverse effects on GHSR activity. Here, we investigate the effects of exogenous LEAP2 on postprandial glucose metabolism and ad libitum food intake in a randomized, double-blind, placebo-controlled, crossover trial of 20 healthy men. We report that LEAP2 infusion lowers postprandial plasma glucose and growth hormone concentrations and decreases food intake during an ad libitum meal test. In wild-type mice, plasma glucose and food intake are reduced by LEAP2 dosing, but not in GHSR-null mice, pointing to GHSR as a potential mediator of LEAP2's glucoregulatory and appetite-suppressing effects in mice.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 35492241 · DOI · PMC9043997
Obestatin: canonical and unexpected functions [4]
Abstract reading summary — source excerpts
- Opening excerpt
- The functions of appetite-regulating hormones have been studied for decades with the aim of finding a solution to the problem of obesity.
- Closing excerpt
- This review describes the main mechanisms and signaling pathways regulated by the obestatin peptide in muscle pathology.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (141 words)
The functions of appetite-regulating hormones have been studied for decades with the aim of finding a solution to the problem of obesity. Among these molecules, a small peptide called obestatin has emerged as an anorexigenic hormone, with an antagonistic effect to the hunger hormone ghrelin. After years of controversy regarding its function in food intake and the establishment of its receptor, GPR39, obestatin is currently being proposed as a powerful therapeutic candidate for pathologies associated with skeletal muscle. Several studies have demonstrated its key role as a regulatory peptide in myogenesis, thereby increasing regeneration in acute muscle damage. Obestatin promotes vascularization and reduces fibrosis in regenerated tissue, while also increasing muscle strength in muscle atrophy pathologies associated with glucocorticoid treatment and Duchenne muscular dystrophy. This review describes the main mechanisms and signaling pathways regulated by the obestatin peptide in muscle pathology.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41784884 · DOI · PMC13167870
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Ghrelin, CCK, GLP-1, and PYY(3-36): Secretory Controls and Physiological Roles in Eating and Glycemia in Health, Obesity, and After RYGB [5]
- Research article The cellular and molecular bases of leptin and ghrelin resistance in obesity [6]
- Research article The Homeostatic Force of Ghrelin [7]
- Research article The effects of ghrelin on inflammation and the immune system [8]
- Research article Influence of adipokines and ghrelin on bone mineral density and fracture risk: a systematic review and meta-analysis [9]
- Research article Acute and Chronic Effects of Exercise on Appetite, Energy Intake, and Appetite-Related Hormones: The Modulating Effect of Adiposity, Sex, and Habitual Physical Activity [10]
References
- Islam MN, Mita Y, Maruyama K, Tanida R, Zhang W, Sakoda H, et al.. Liver-expressed antimicrobial peptide 2 antagonizes the effect of ghrelin in rodents. . 2020. PMID 31539874 · DOI · PMC6839046
- Shiimura Y, Horita S, Hamamoto A, Asada H, Hirata K, Tanaka M, et al.. Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode. . 2020. PMID 32814772 · DOI · PMC7438500
- Hagemann CA, Jensen MS, Holm S, Gasbjerg LS, Byberg S, Skov-Jeppesen K, et al.. LEAP2 reduces postprandial glucose excursions and ad libitum food intake in healthy men. . 2022. PMID 35492241 · DOI · PMC9043997
- Santos-Zas I, Gurriaran-Rodriguez U, Cid-Diaz T, Leal-Lopez S, Casanueva FF, Pazos-Randulfe Y, et al.. Obestatin: canonical and unexpected functions. . 2026. PMID 41784884 · DOI · PMC13167870
- Steinert RE, Feinle-Bisset C, Asarian L, Horowitz M, Beglinger C, Geary N. Ghrelin, CCK, GLP-1, and PYY(3-36): Secretory Controls and Physiological Roles in Eating and Glycemia in Health, Obesity, and After RYGB. Physiol Rev. 2017. PMID 28003328 · DOI · PMC6151490
- Cui H, López M, Rahmouni K. The cellular and molecular bases of leptin and ghrelin resistance in obesity. Nat Rev Endocrinol. 2017. PMID 28232667 · DOI · PMC8904083
- Yanagi S, Sato T, Kangawa K, Nakazato M. The Homeostatic Force of Ghrelin. Cell Metab. 2018. PMID 29576534 · DOI
- Baatar D, Patel K, Taub DD. The effects of ghrelin on inflammation and the immune system. Mol Cell Endocrinol. 2011. PMID 21565248 · DOI
- Biver E, Salliot C, Combescure C, Gossec L, Hardouin P, Legroux-Gerot I, et al.. Influence of adipokines and ghrelin on bone mineral density and fracture risk: a systematic review and meta-analysis. J Clin Endocrinol Metab. 2011. PMID 21778223 · DOI
- Dorling J, Broom DR, Burns SF, Clayton DJ, Deighton K, James LJ, et al.. Acute and Chronic Effects of Exercise on Appetite, Energy Intake, and Appetite-Related Hormones: The Modulating Effect of Adiposity, Sex, and Habitual Physical Activity. Nutrients. 2018. PMID 30131457 · DOI · PMC6164815
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.