ArticleMethods in molecular biology (Clifton, N.J.)2013
Proteomic analysis of the left ventricle post-myocardial infarction to identify in vivo candidate matrix metalloproteinase substrates.
Article in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
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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.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Phenotyping patients with ischaemic heart disease at risk of developing heart failure: an analysis of the HOMAGE trial.ESC heart failure · 2024Article
- Understanding cardiac extracellular matrix remodeling to develop biomarkers of myocardial infarction outcomes.Matrix biology : journal of the International Society for Matrix Biology · 2019Review
- Regulation and involvement of matrix metalloproteinases in vascular diseases.Frontiers in bioscience (Landmark edition) · 2016Review
- Using plasma matrix metalloproteinase-9 and monocyte chemoattractant protein-1 to predict future cardiovascular events in subjects with carotid atherosclerosis.Atherosclerosis · 2014Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Left ventricular remodeling post-myocardial infarction (MI) involves a multitude of mechanisms that regulate the repair response. Matrix metalloproteinases (MMPs) are a major family of proteolytic enzymes that coordinate extracellular matrix turnover. MMP-7 or MMP-9 deletion attenuate adverse remodeling post-MI, but the mechanisms have not been fully clarified. Both MMP-7 and MMP-9 have a large number of known in vitro substrates, but in vivo substrates for these two MMPs in the myocardial infarction setting are incompletely identified. Advances in proteomic techniques have enabled comprehensive profiling of protein expression in cells and tissue. In this chapter, we describe a protocol for the proteomic analysis of in vivo candidate MMP substrates in the post-MI left ventricle using two-dimensional electrophoresis, liquid chromatography coupled with tandem mass spectrometry, and immunoblotting.
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Registered trials
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