Evidence map›Paper›PMID 41272451›Full record

ArticleMolecular medicine (Cambridge, Mass.)2025

Deletion of fibro-adipogenic progenitors-specific follistatin impairs muscle function and accelerates skeletal muscle atrophy in obese mice.

Muhammad Rahil Aslam, Muhammad Bilal, Allah Nawaz, Tomonobu Kado, Shinya Abe, Nguyen Quynh Phuong, Memoona, Sana Khalid, Le Duc Anh, Ayumi Nishimura and 17 more

Abstract read
In one paragraph

Article in Molecular medicine (Cambridge, Mass.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

27 authors.

Muhammad Rahil Aslam *First Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Muhammad Bilal *First Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan. drbilal@med.u-toyama.ac.jp.
Allah NawazFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Tomonobu KadoFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Shinya AbeLaboratory of Immune Regulation, Department of Virus Research, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Nguyen Quynh PhuongFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
MemoonaFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Sana KhalidDepartment of Molecular Neuroscience, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Le Duc AnhFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Ayumi NishimuraFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Yoshiyuki WatanabeFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Yoshiko IgarashiFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Naeem IqbalRawalpindi Medical University, Rawalpindi, 46000, Pakistan.
Maki YokoyamaFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Yasuhiro OnogiResearch Center for Pre-Disease Science, Faculty of Education and Research Promotion, University of Toyama, Toyama, 930-0194, Japan.
Kennichi HirabayashiDepartment of Diagnostic Pathology, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Hiroyuki MiwaDepartment of Allergy and Immunology, Faculty of Medicine, Saitama Medical University, Saitama, 350-0495, Japan.
Takumi EraDepartment of Cell Modulation, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Chuo-Ku, Kumamoto, 860-0811, Japan.
Martin M MatzukDepartment of Pathology and Immunology, Baylor College of Medicine, Houston, TX, 77030-3411, USA.
Seiji YamamotoDepartment of Pathology, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Koichi IkutaLaboratory of Immune Regulation, Department of Virus Research, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Isao UsuiDepartment of Endocrinology and Metabolism, Dokkyo Medical University, Tochigi, Japan.
Kohta KobayashiDepartment of Plastic, Reconstructive and Aesthetic Surgery, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Toshihiko SatakeDepartment of Plastic, Reconstructive and Aesthetic Surgery, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Masaru KatoFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Shiho FujisakaFirst Department of Internal Medicine, Faculty of Medicine, University of Toyama, Toyama, 930-0194, Japan.
Kazuyuki TobeResearch Center for Pre-Disease Science, Faculty of Education and Research Promotion, University of Toyama, Toyama, 930-0194, Japan. tobe@med.u-toyama.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFollistatin is a potent regulator of various TGF-β superfamily members, including myostatin (MSTN) and activin A. Previous studies have shown that follistatin is crucial in enhancing myogenesis during acute muscle injury. The mechanism by which fibro-adipogenic progenitors (FAPs)-specific follistatin influences muscle homeostasis in obese mice remains unknown. Therefore, we investigated the physiological role of follistatin in PDGFRα-positive FAPs in the regulation of muscle homeostasis and exercise in obese mice.

methodsA PDGFRα-specific follistatin knockout (follistatin KO) mouse model was generated using PDGFRα-GFP-CreER

resultsWe showed that follistatin KO mice had reduced expression of Fst in skeletal muscle and white adipose tissue. We also showed that follistatin KO mice exhibited decreased exercise performance and altered skeletal homeostasis during obesity. Deletion of follistatin in FAPs activated the MSTN: Activin A/SMADs signaling pathways, which negatively impacted muscle homeostasis. Furthermore, follistatin KO mice showed reduced muscle mass, increased muscle degradation, and atrophic myofibers. Mitochondrial biogenesis, oxidative phosphorylation, and fatty acid oxidation were also altered in the skeletal muscles of follistatin KO mice.

conclusionFollistatin plays a protective role in mice by maintaining the metabolic health of skeletal muscles; it restores muscle function during HFD challenge, thereby reducing diet-induced obesity-related complications.

Indexed as

FollistatinMuscle, SkeletalMuscular AtrophyObesityAdipogenesisAnimalsDiet, High-FatDisease Models, AnimalGene DeletionMaleMiceMice, Inbred C57BLMice, KnockoutMice, ObesePhysical Conditioning, AnimalFollistatinExercise capacityFibro-adipogenic progenitors (FAPs)FollistatinMuscle massObesity

Identifiers

PMID41272451
PMCPMC12752164

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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.