Evidence map›Paper›PMID 38828411›Full record

ArticleFrontiers in endocrinology2024

Acyl modifications in bovine, porcine, and equine ghrelins.

Takanori Ida, Hatsumi Tominaga, Eri Iwamoto, Akito Kurogi, Ayaka Okura, Kengo Shimada, Johji Kato, Atsutoshi Kuwano, Hirotaka Ode, Sayaka Nagata and 8 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in endocrinology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors.

Takanori IdaDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Hatsumi TominagaMiyazaki Prefecture Industrial Technology Center, Miyazaki, Japan.
Eri IwamotoClinical Research Center, Kurume University Hospital, Fukuoka, Japan.
Akito KurogiDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Ayaka OkuraDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Kengo ShimadaDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Johji KatoDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Atsutoshi KuwanoEquine Research Institute, Japan Racing Association, Tochigi, Japan.
Hirotaka OdeRacehorse Clinic, Ritto Training Center, Japan Racing Association, Shiga, Japan.
Sayaka NagataDepartment of Food Science and Technology, Faculty of Health and Nutrition, Minami Kyushu University, Miyazaki, Japan.
Kazuo KitamuraDepartment of Projects Research, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Takashi YazawaDepartment of Biochemistry, Asahikawa Medical University, Hokkaido, Japan.
Miho Sato-HashimotoDepartment of Animal Pharmaceutical Science, School of Pharmaceutical Sciences, Kyusyu University of Medical Science, Miyazaki, Japan.
Masahiro YasudaLaboratory of Veterinary Anatomy, Faculty of Agriculture, University of Miyazaki, Miyazaki, Japan.
Mikiya MiyazatoDivision for Identification and Analysis of Bioactive Peptides, Department of Bioactive Peptides, Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan.
Yuki ShiimuraMolecular Genetics, Institute of Life Sciences, Kurume University, Fukuoka, Japan.
Takahiro SatoMolecular Genetics, Institute of Life Sciences, Kurume University, Fukuoka, Japan.
Masayasu KojimaMolecular Genetics, Institute of Life Sciences, Kurume University, Fukuoka, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ghrelin is a peptide hormone with various important physiological functions. The unique feature of ghrelin is its serine 3 acyl-modification, which is essential for ghrelin activity. The major form of ghrelin is modified with n-octanoic acid (C8:0) by ghrelin O-acyltransferase. Various acyl modifications have been reported in different species. However, the underlying mechanism by which ghrelin is modified with various fatty acids remains to be elucidated. Herein, we report the purification of bovine, porcine, and equine ghrelins. The major active form of bovine ghrelin was a 27-amino acid peptide with an n-octanoyl (C8:0) modification at Ser3. The major active form of porcine and equine ghrelin was a 28-amino acid peptide. However, porcine ghrelin was modified with n-octanol (C8:0), whereas equine ghrelin was modified with n-butanol (C4:0) at Ser3. This study indicates the existence of structural divergence in ghrelin and suggests that it is necessary to measure the minor and major forms of ghrelin to fully understand its physiology.

Indexed as

GhrelinAcylationAmino Acid SequenceAnimalsCaprylatesCattleHorsesSwineCaprylatesGhrelinoctanoic acidacyl-modificationghrelinGHS-Rn-butanoic acidn-octanoic acid

Identifiers

PMID38828411
PMCPMC11140078

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.