Evidence map›Paper›PMID 39355613›Full record

ArticleFrontiers in endocrinology2024

MG53's non-physiologic interaction with insulin receptor: lack of effect on insulin-stimulated Akt phosphorylation in muscle, heart and liver tissues.

Kyung Eun Lee, Miyuki Nishi, Jongsoo Kim, Takashi Murayama, Zachary Dawson, Xiaoliang Wang, Xinyu Zhou, Tao Tan, Chuanxi Cai, Hiroshi Takeshima and 1 more

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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. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Kyung Eun LeeDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Miyuki NishiDepartment of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Jongsoo KimDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Takashi MurayamaDepartment of Cellular and Molecular Pharmacology, Graduate School of Medicine, Juntendo University, Tokyo, Japan.
Zachary DawsonDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Xiaoliang WangDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Xinyu ZhouDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Tao TanDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Chuanxi CaiDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.
Hiroshi TakeshimaDepartment of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Ki Ho ParkDivision of Surgical Sciences, Department of Surgery, University of Virginia, Charlottesville, VA, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rationale: MG53's known function in facilitating tissue repair and anti-inflammation has broad applications to regenerative medicine. There is controversy regarding MG53's role in the development of type 2 diabetes mellitus. Objective: This study aims to address this controversy - whether MG53's myokine function contributes to inhibition of insulin signaling in muscle, heart, and liver tissues. Study design: We determined the binding affinity of the recombinant human MG53 (rhMG53) to the insulin receptor extracellular domain (IR-ECD) and found low affinity of interaction with K Conclusion: Overall, our data suggest that rhMG53 can bind to the IR-ECD, however has a low likelihood of a physiologic role, as the K

Indexed as

InsulinLiverMice, Inbred C57BLProto-Oncogene Proteins c-aktReceptor, InsulinAnimalsCytokinesDiabetes Mellitus, Type 2Hep G2 CellsHumansMaleMembrane ProteinsMiceMuscle, SkeletalMyocardiumPhosphorylationCytokinesInsulinMembrane ProteinsMG53 protein, mouseProto-Oncogene Proteins c-aktReceptor, InsulinTRIM72 protein, humanTripartite Motif ProteinsAkt phosphorylationC2C12 cellsHepG2 cellsinsulin receptorMG53/TRIM72micemyokinestype 2 diabetes mellitus

Identifiers

PMID39355613
PMCPMC11442255

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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.