Evidence map›Paper›PMID 26176332›Full record

ArticleCanadian journal of physiology and pharmacology2015

Osteopontin is proteolytically processed by matrix metalloproteinase 9.

Merry L Lindsey, Fouad A Zouein, Yuan Tian, Rugmani Padmanabhan Iyer, Lisandra E de Castro Brás

Open access · greenAbstract read
In one paragraph

Article in Canadian journal of physiology and pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Merry L Lindseya San Antonio Cardiovascular Proteomics Center.
Fouad A Zoueina San Antonio Cardiovascular Proteomics Center.
Yuan Tiana San Antonio Cardiovascular Proteomics Center.
Rugmani Padmanabhan Iyera San Antonio Cardiovascular Proteomics Center.
Lisandra E de Castro Brása San Antonio Cardiovascular Proteomics Center.
G.V. (Sonny) Montgomery VA Medical Center · US

Funding

STRUCTURAL VASCULAR ADAPTATION OF THE MICROCIRCULATIONP01HL051971 · NHLBI · UNIVERSITY OF MISSISSIPPI MEDICAL CENTER · PI ALEXANDER, BARBARA T · 1993 to 2018
$39.4M
The role of leptin in autoimmune-associated hypertensionP20GM104357 · NIGMS · UNIVERSITY OF MISSISSIPPI MED CTR · PI TAYLOR, ERIN BASSFORD · 2013 to 2022
$23.4M
The Role of Macrophage-derived MMPs in LV RemodelingR01HL075360 · NHLBI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LINDSEY, MERRY L. · 2004 to 2018
$5.4M
Biomechanical Mechanisms of Artery TortuosityR01HL095852 · NHLBI · UNIVERSITY OF TEXAS SAN ANTONIO · PI HAN, HAI-CHAO · 2010 to 2014
$1.8M
Neutrophil Polarization Following Myocardial InfarctionI01BX000505 · VA · VETERANS HEALTH ADMINISTRATION · PI LINDSEY, MERRY L. · 2009 to 2024
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BLRD VA I01 BX000505NHLBI NIH HHS HHSN268201000036CNHLBI NIH HHS HL051971NHLBI NIH HHS HL095852NHLBI NIH HHS N01-HV-00244NHLBI NIH HHS P01 HL051971NHLBI NIH HHS R01 HL075360NHLBI NIH HHS R01HL075360NHLBI NIH HHS R01 HL095852NIGMS NIH HHS P20 GM104357NIGMS NIH HHS P20GM104357PHS HHS 268201000036C
6 · The paper itself

Abstract

Osteopontin is robustly upregulated following myocardial infarction (MI), which suggests that it has an important role in post-MI remodeling of the left ventricle (LV). Osteopontin deletion results in increased LV dilation and worsened cardiac function. Thus, osteopontin exerts protective effects post-MI, but the mechanisms have yet to be defined. Matrix metalloproteinases (MMPs) regulate LV remodeling post-MI, and osteopontin is a known substrate for MMP-2, -3, -7, and -9, although the cleavage sites have not been mapped. Osteopontin-derived peptides can exert distinct biological functions that may depend on their cleavage sites. We mapped the MMP-9 cleavage sites via LC-MS/MS analysis using label-free and N-terminal labeling methods, and compared them with those of MMP-2, -3, and -7. Each MMP yielded a unique cleavage profile with few overlapping cleavage sites. Using synthetic peptides, we validated 3 sites for MMP-9 cleavage at amino acid positions 151-152, 193-194, and 195-196. Four peptides were synthesized based on the upstream- and downstream-generated fragments and were tested for biological activity in isolated cardiac fibroblasts. Two peptides increased cardiac fibroblast migration rates post-wounding (p < 0.05 compared with the negative control). Our study highlights the importance of osteopontin processing, and confirms that different cleavage sites generate osteopontin peptides with distinct biological functions.

Indexed as

ProteolysisAnimalsCell MovementCell ProliferationCells, CulturedChromatography, High Pressure LiquidFibroblastsMatrix Metalloproteinase 9MiceMyocardial InfarctionMyocytes, CardiacOsteopontinPeptide FragmentsRecombinant ProteinsSubstrate SpecificityTandem Mass SpectrometryMatrix Metalloproteinase 9Mmp9 protein, mouseOsteopontinPeptide FragmentsRecombinant Proteinscardiaccardiaquecleavage sitesfibroblastesfibroblastsinfarctus du myocardemass spectrometrymatrix metalloproteinasesmétalloprotéinases matriciellesMMP-9MPM-9myocardial infarctionosteopontinostéopontinepeptidesproteomicsprotéomiquesites de clivagespectométrie de masse

Identifiers

PMID26176332
PMCPMC4764993
OpenAlexW2042728399

What OpenQuestion holds

Textmetadata
LicenceTDM
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.