Evidence map›Paper›PMID 33732908›Full record

ArticleBiochemistry and biophysics reports2021

Irisin supports integrin-mediated cell adhesion of lymphocytes.

Phyoe Kyawe Myint, Atsushi Ito, Michael G Appiah, Gideon Obeng, Samuel Darkwah, Eiji Kawamoto, Arong Gaowa, Eun Jeong Park, Motomu Shimaoka

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
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

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Role and mechanism of Integrin α5β1 in bone formation and disease.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. 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

9 authors at 1 institution in 1 country.

Phyoe Kyawe MyintDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Atsushi ItoDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Michael G AppiahDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Gideon ObengDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Samuel DarkwahDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Eiji KawamotoDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Arong GaowaDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Eun Jeong ParkDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Motomu ShimaokaDepartment of Molecular Pathobiology and Cell Adhesion Biology, Mie University Graduate School of Medicine, Japan.
Mie University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Irisin, a myokine released from skeletal muscle, has recently been found to act as a ligand for the integrins αVβ5, αVβ1, and α5β1 expressed on mesenchymal cells, thereby playing an important role in the metabolic remodeling of the bone, skeletal muscle and adipose tissues. Although the immune-modulatory effects of irisin in chronic inflammation have been documented, its interactions with lymphocytic integrins have yet to be elucidated. Here, we show that irisin supports the cell adhesion of human and mouse lymphocytes. Cell adhesion assays using a panel of inhibitory antibodies to integrins have shown that irisin-mediated lymphocyte adhesion involves multiple integrins including not only α4β1 and α5β1, but also leukocyte-specific αLβ2 and α4β7. Importantly, mouse lymphocytic TK-1 cells that lack the expression of β1 integrins have exhibited αLβ2- and α4β7-mediated cell adhesion to irisin. Irisin has also been demonstrated to bind to purified recombinant integrin αLβ2 and α4β7 proteins. Thus, irisin represents a novel ligand for integrin αLβ2 and α4β7, capable of supporting lymphocyte cell adhesion independently of β1 integrins. These results suggest that irisin may play an important role in regulating lymphocyte adhesion and migration in the inflamed vasculature.

Indexed as

Cell adhesionECM, extracellular matrixFc, fragment crystallizableFibronectin type III domain-containing protein 5FNDC-5, fibronectin type III domain-containing protein 5ICAM-1, intercellular adhesion molecule-1IntegrinsIrisinLFA-1, lymphocyte function-associated antigen 1LPAM-1, lymphocyte Peyer's patch adhesion moleculesMAdCAM-1, mucosal addressin cell adhesion molecule-1PBMCs, peripheral blood mononuclear cellsSDS-PAGE, sodium dodecyl sulphate-polyacrylamide gel electrophoresis

Identifiers

PMID33732908
PMCPMC7944048
OpenAlexW3134306191

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.