Evidence map›Paper›PMID 36852525›Full record

ArticleAging cell2023

Glycation-mediated tissue-level remodeling of brain meningeal membrane by aging.

Hyo Min Kim, Shinheun Kim, Jueun Sim, Boo Soo Ma, Insung Yong, Youngmin Jo, Taek-Soo Kim, Jae-Byum Chang, Sung-Hye Park, Yong Jeong and 1 more

Open access · goldAbstract read
In one paragraph

Article in Aging cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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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

11 authors at 2 institutions in 2 countries.

Hyo Min KimDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Shinheun KimProgram of Brain and Cognitive Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Jueun SimDepartment of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Boo Soo MaDepartment of Mechanical Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Insung YongDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Youngmin JoDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Taek-Soo KimDepartment of Mechanical Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Jae-Byum ChangDepartment of Materials Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Sung-Hye ParkNeuroscience Research Institute, Department of Pathology, Seoul National University College of Medicine, Seoul, Korea.
Yong JeongDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Pilnam KimDepartment of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.ORCID 0000-0002-5592-4599
Korea Advanced Institute of Science and Technology · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen is a prominent target of nonenzymatic glycation, which is a hallmark of aging and causes functional alteration of the matrix. Here, we uncover glycation-mediated structural and functional changes in the collagen-enriched meningeal membrane of the human and mouse brain. Using an in vitro culture platform mimicking the meningeal membrane composed of fibrillar collagen, we showed that the accumulation of advanced glycation end products (AGEs) in the collagen membrane is responsible for glycation-mediated matrix remodeling. These changes influence fibroblast-matrix interactions, inducing cell-mediated ECM remodeling. The adherence of meningeal fibroblasts to the glycated collagen membrane was mediated by the discoidin domain-containing receptor 2 (DDR2), whereas integrin-mediated adhesion was inhibited. A-kinase anchoring protein 12 (AKAP12)-positive meningeal fibroblasts in the meningeal membrane of aged mice exhibited substantially increased expression of DDR2 and depletion of integrin beta-1 (ITGB1). In the glycated collagen membrane, meningeal fibroblasts increased the expression of matrix metalloproteinase 14 (MMP14) and less tissue inhibitor of metalloproteinase-1 (TIMP1). In contrast, the cells exhibited decreased expression of type I collagen (COL1A1). These results suggest that glycation modification by meningeal fibroblasts is intimately linked to aging-related structural and functional alterations in the meningeal membrane.

Indexed as

Maillard ReactionTissue Inhibitor of Metalloproteinase-1A Kinase Anchor ProteinsAnimalsBrainCell Cycle ProteinsCollagenFibroblastsGlycation End Products, AdvancedHumansIntegrinsMiceAkap12 protein, mouseA Kinase Anchor ProteinsCell Cycle ProteinsCollagenGlycation End Products, AdvancedIntegrinsTissue Inhibitor of Metalloproteinase-1brain meningeal membranediscoidin domain-containing receptor 2extracellular matrix remodelingglycationtype-I collagen

Identifiers

PMID36852525
PMCPMC10186607
OpenAlexW4322616483

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.