Evidence map›Paper›PMID 27190383›Full record

ArticleNephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association2017

Matrix metalloproteinase 9 is associated with peritoneal membrane solute transport and induces angiogenesis through β-catenin signaling.

Manreet Padwal, Imad Siddique, Lili Wu, Katelynn Tang, Felix Boivin, Limin Liu, Jennifer Robertson, Darren Bridgewater, Judith West-Mays, Azim Gangji and 2 more

Abstract read
In one paragraph

Article in Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

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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

12 authors.

Manreet PadwalDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Imad SiddiqueDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Lili WuInstitute of Traditional Chinese Medicine, Beijing, China.
Katelynn TangDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Felix BoivinDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, ON, Canada.
Limin LiuDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Jennifer RobertsonDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, ON, Canada.
Darren BridgewaterDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, ON, Canada.
Judith West-MaysDepartment of Pathology and Molecular Medicine, McMaster University, Hamilton, ON, Canada.
Azim GangjiDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Kenneth Scott BrimbleDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.
Peter J MargettsDivision of Nephrology, St. Joseph's Hospital, Department of Medicine, McMaster University, Hamilton, ON, Canada.

Funding

Role of MMPs in TGFbeta-induced Cataract FormationR01EY017146 · NEI · MCMASTER UNIVERSITY · PI WEST-MAYS, JUDITH A · 2006 to 2015
$2.2M
NEI NIH HHS R01 EY017146
6 · The paper itself

Abstract

Background: For patients using peritoneal dialysis (PD), the peritoneal membrane can develop fibrosis and angiogenesis, leading to ultrafiltration failure, chronic hypervolemia and increased risk of technique failure and mortality. Matrix metalloproteinases (MMPs), and specifically the gelatinases (MMP2 and MMP9), may be involved in peritoneal membrane injury. Methods: From stable PD patients, mesothelial cells were assayed for MMP gene expression. MMP9 was overexpressed in mouse peritoneum by adenovirus, and MMP9 -/- mice were subjected to transforming growth factor β (TGF-β)-induced peritoneal fibrosis. Results: MMP9 mRNA expression correlated with peritoneal membrane solute transport properties. Overexpression of MMP9 in the mouse peritoneum induced submesothelial thickening and angiogenesis. MMP9 induced mesothelial cell transition to a myofibroblast phenotype measured by increased alpha smooth muscle actin and decreased E-cadherin expression. Angiogenesis was markedly reduced in MMP9 -/- mice treated with an adenovirus expressing active TGF-β compared with wild-type mice. TGF-β-mediated E-cadherin cleavage was MMP9 dependent, and E-cadherin cleavage led to β-catenin-mediated signaling. A β-catenin inhibitor blocked the angiogenic response induced by AdMMP9. Conclusions: Our data suggest that MMP9 is involved in peritoneal membrane injury possibly through cleavage of E-cadherin and induction of β-catenin signaling. MMP9 is a potential biomarker for peritoneal membrane injury and is a therapeutic target to protect the peritoneal membrane in PD patients.

Indexed as

Animalsbeta CateninBiological TransportCadherinsHemodialysis SolutionsHumansMatrix Metalloproteinase 9MiceMice, Inbred C57BLNeovascularization, PathologicPeritoneal DialysisPeritoneal FibrosisSignal TransductionTransforming Growth Factor betabeta CateninCadherinsHemodialysis SolutionsMatrix Metalloproteinase 9Transforming Growth Factor betaangiogenesisfibrosismatrix metalloproteinaseperitoneal membranetransforming growth factor-ββ-catenin

Identifiers

PMID27190383
PMCPMC6251592

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Registered trials

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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.