Evidence map›Paper›PMID 34338144›Full record

ArticleBioengineered2021

Fermitin family homolog 2 (Kindlin-2) affects vascularization during the wound healing process by regulating the Wnt/β-catenin signaling pathway in vascular endothelial cells.

Jianghui Ying, Qiang Wang, Lu Lu, Jiaqi Liu, Rong Guo, Hao Hu, Hua Jiang, Fazhi Qi

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioengineered, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

5 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
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  4. Therapeutic effects ofBioengineered · 2022
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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

8 authors at 3 institutions in 1 country.

Jianghui YingDepartment of Plastic Surgery, Shanghai East Hospital, School of Medicine, Tongji University, Shanghai, China.
Qiang WangDepartment of Plastic Surgery, Zhongshan Hospital, Fudan University, Shanghai, China.
Lu LuDepartment of Plastic Surgery, Shanghai East Hospital, School of Medicine, Tongji University, Shanghai, China.
Jiaqi LiuDepartment of Plastic Surgery, Zhongshan Hospital, Fudan University, Shanghai, China.
Rong GuoDepartment of Plastic Surgery, Shanghai East Hospital, School of Medicine, Tongji University, Shanghai, China.
Hao HuDepartment of Plastic Surgery, Shanghai East Hospital, School of Medicine, Tongji University, Shanghai, China.
Hua JiangDepartment of Plastic Surgery, Shanghai East Hospital, School of Medicine, Tongji University, Shanghai, China.
Fazhi QiDepartment of Plastic Surgery, Zhongshan Hospital, Fudan University, Shanghai, China.
Shanghai East Hospital · CNFudan University · CNZhongshan Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kindlin-2 is a member of the FERM-containing cytoskeletal protein family that regulates cell-matrix interactions. Previous studies have shown that Kindlin-2 recruits focal adhesion proteins and regulates integration by binding to the focal adhesion region of the integrin β-segment. Although Kindlin-2 has been reported to be involved in various skin diseases and many kinds of tumors, its role in the skin wound healing process remains unclear. The aim of the present study was to investigate the role of Kindlin-2 in the regulation of wound healing. The effects of Kindlin-2 on wound healing were studied by a wound healing model, kindlin-2 (±) mice. The effects of Kindlin-2 on cell migration, cellular tube formation, and cell adhesion and spreading were evaluated in human umbilical vein endothelial cells (HUVECs) with downregulated Kindlin-2 expression. We found that the expression of kindlin-2 was elevated in wound healing tissues and that interfering with the expression of Kindlin-2 delayed the wound healing process and reduced neovascularization. We found that the wound healing of kindlin-2 (±) mice was delayed, with a decreased number of new blood vessels. Furthermore, depletion of Kindlin-2 impaired HUVEC spreading, migration and tube formation. Intriguingly, we found that kindlin-2 binds to β-catenin in the Wnt/β-catenin signaling pathway and cooperates with β-catenin to enter the nucleus from the cytoplasm, activating the downstream Wnt/β-catenin signaling pathway. Taken together, these results help to elucidate the mechanism of Kindlin-2 in the regulation of the wound healing process and provide a theoretical basis for further study of wound healing and abnormal healing.

Indexed as

Cytoskeletal ProteinsMuscle ProteinsAnimalsCell LineHumansHuman Umbilical Vein Endothelial CellsMembrane ProteinsMiceNeoplasm ProteinsNeovascularization, PhysiologicWnt Signaling PathwayWound HealingCytoskeletal ProteinsFERMT3 protein, humankindlin-2 protein, mouseMembrane ProteinsMuscle ProteinsNeoplasm ProteinsKindlin-2vascularizationWnt/β-catenin pathwaywound healing

Identifiers

PMID34338144
PMCPMC8806626
OpenAlexW3187375698

What OpenQuestion holds

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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.