An altered left ventricle protein profile in human ischemic cardiomyopathy revealed in comparative quantitative

Xin Yi1,2,3, Ding-Sheng Jiang4,5,6, Gaoke Feng1,2,3

  • 1Department of Cardiology, Renmin Hospital of Wuhan University, Wuhan, People’s Republic of China

Kardiologia Polska
|August 23, 2019
PubMed

Insights

Researchers identified key proteins altered in ischemic cardiomyopathy (ICM). These differentially expressed proteins, including C1 inhibitor SERPING1, offer potential new diagnostic and therapeutic targets for heart failure patients.

Area of Science:

  • Cardiology
  • Proteomics
  • Biochemistry

Background:

  • Ischemic cardiomyopathy (ICM) is a primary cause of heart failure, stemming from coronary artery disease.
  • Identifying and quantifying protein expression changes in ICM patients is crucial for developing better diagnostic and treatment strategies.

Purpose of the Study:

  • To identify and quantify differentially expressed proteins in the left ventricles of patients with ICM.
  • To explore the molecular mechanisms underlying ICM through proteomic analysis.

Main Methods:

  • Quantitative proteomic analysis of left ventricular tissue from 6 ICM patients and 7 normal heart donors using liquid chromatography-tandem mass spectrometry.
  • Bioinformatic analyses including gene ontology, pathway mapping, and protein interaction analysis were performed on identified proteins.

Main Results:

  • 1723 proteins were quantified, with 104 upregulated and 63 downregulated in ICM patients.
  • Altered proteins were associated with extracellular matrix, metabolism, immune response, muscle contraction, cytoskeleton, transcription/translation, and signal transduction.
  • C1 inhibitor SERPING1 was found to inhibit complement activation in response to ischemic stimulus.

Conclusions:

  • The study identified differentially expressed proteins that are potential novel diagnostic and therapeutic targets for ICM.
  • These findings advance the understanding of molecular mechanisms in ICM and highlight SERPING1's role in complement regulation.
Abstract

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