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Methods Mol Biol. 2013;1066:185-99. doi: 10.1007/978-1-62703-604-7_16.

Proteomic analysis of the left ventricle post-myocardial infarction to identify in vivo candidate matrix metalloproteinase substrates.

Author information

1
San Antonio Cardiovascular Proteomics Center, The University of Texas Health Science Center, San Antonio, TX, USA.

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.

PMID:
23955744
PMCID:
PMC3971009
DOI:
10.1007/978-1-62703-604-7_16
[Indexed for MEDLINE]
Free PMC Article

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