Evidence map›Paper›PMID 37728809›Full record

ArticleMolecular and cellular biochemistry2024

Remote ischemic preconditioning prevents sarcolemmal-associated proteolysis by MMP-2 inhibition.

Eliana P Bin, Tamara Zaobornyj, Mariana Garces, Verónica D'Annunzio, Bruno Buchholz, Timoteo Marchini, Pablo Evelson, Ricardo J Gelpi, Martín Donato

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In one paragraph

Article in Molecular and cellular biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Eliana P Bin *Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.
Tamara Zaobornyj *Universidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina.
Mariana GarcesUniversidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina.
Verónica D'AnnunzioUniversidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.
Bruno BuchholzUniversidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.
Timoteo MarchiniUniversidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina.
Pablo EvelsonUniversidad de Buenos Aires - CONICET, Instituto de Bioquímica y Medicina Molecular (IBIMOL), Buenos Aires, Argentina.
Ricardo J Gelpi *Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina.
Martín Donato *Universidad de Buenos Aires, Facultad de Ciencias Médicas, Instituto de Fisiopatología Cardiovascular, 950 J. E. Uriburu, 2nd floor, C1114AAD, Buenos Aires, Argentina. mdonato@fmed.uba.ar.ORCID http://orcid.org/0000-0003-4133-5280

Funding

National Agency for Scientific and Technological Promotion ANPCyT, PICT 2017-1447Universidad de Buenos Aires UBACyT 20020150100105BA
6 · The paper itself

Abstract

The death of myocytes occurs through different pathways, but the rupture of the plasma membrane is the key point in the transition from reversible to irreversible injury. In the myocytes, three major groups of structural proteins that link the extracellular and intracellular milieus and confer structural stability to the cell membrane: the dystrophin-associated protein complex, the vinculin-integrin link, and the spectrin-based submembranous cytoskeleton. The objective was to determine if remote ischemic preconditioning (rIPC) preserves membrane-associated cytoskeletal proteins (dystrophin and β-dystroglycan) through the inhibition of metalloproteinase type 2 (MMP-2) activity. A second objective was to describe some of the intracellular signals of the rIPC, that modify mitochondrial function at the early reperfusion. Isolated rat hearts were subjected to 30 min of global ischemia and 120 min of reperfusion (I/R). rIPC was performed by 3 cycles of ischemia/reperfusion in the lower limb (rIPC). rIPC significantly decreased the infarct size, induced Akt/GSK-3 β phosphorylation and inhibition of the MPTP opening. rIPC improved mitochondrial function, increasing membrane potential, ATP production and respiratory control. I/R increased ONOO

Indexed as

Matrix Metalloproteinase 2ProteolysisSarcolemmaAnimalsDystroglycansDystrophinIschemic PreconditioningMaleMatrix Metalloproteinase InhibitorsMyocardial Reperfusion InjuryMyocytes, CardiacRatsRats, WistarDystroglycansDystrophinMatrix Metalloproteinase 2Matrix Metalloproteinase InhibitorsMmp2 protein, ratCardioprotectionIschemiaMyocardial infarctionRemote preconditioningReperfusion

Identifiers

What OpenQuestion holds

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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.