» Articles » PMID: 27635058

Systems Biology-opportunities and Challenges: the Application of Proteomics to Study the Cardiovascular Extracellular Matrix

Overview
Journal Cardiovasc Res
Date 2016 Sep 17
PMID 27635058
Citations 14
Authors
Affiliations
Soon will be listed here.
Abstract

Systems biology approaches including proteomics are becoming more widely used in cardiovascular research. In this review article, we focus on the application of proteomics to the cardiac extracellular matrix (ECM). ECM remodelling is a hallmark of many cardiovascular diseases. Proteomic techniques using mass spectrometry (MS) provide a platform for the comprehensive analysis of ECM proteins without a priori assumptions. Proteomics overcomes various constraints inherent to conventional antibody detection. On the other hand, studies that use whole tissue lysates for proteomic analysis mask the identification of the less abundant ECM constituents. In this review, we first discuss decellularization-based methods that enrich for ECM proteins in cardiac tissue, and how targeted MS allows for accurate protein quantification. The second part of the review will focus on post-translational modifications including hydroxylation and glycosylation and on the release of matrix fragments with biological activity (matrikines), all of which can be interrogated by proteomic techniques.

Citing Articles

Orthogonal proteomics methods warrant the development of Duchenne muscular dystrophy biomarkers.

Johansson C, Hunt H, Signorelli M, Edfors F, Hober A, Svensson A Clin Proteomics. 2023; 20(1):23.

PMID: 37308827 PMC: 10258980. DOI: 10.1186/s12014-023-09412-1.


Ten Years of Extracellular Matrix Proteomics: Accomplishments, Challenges, and Future Perspectives.

Naba A Mol Cell Proteomics. 2023; 22(4):100528.

PMID: 36918099 PMC: 10152135. DOI: 10.1016/j.mcpro.2023.100528.


Extracellular Matrix in Heart Failure: Role of ADAMTS5 in Proteoglycan Remodeling.

Barallobre-Barreiro J, Radovits T, Fava M, Mayr U, Lin W, Ermolaeva E Circulation. 2021; 144(25):2021-2034.

PMID: 34806902 PMC: 8687617. DOI: 10.1161/CIRCULATIONAHA.121.055732.


Microgravity Effects on the Matrisome.

Buravkova L, Larina I, Andreeva E, Grigoriev A Cells. 2021; 10(9).

PMID: 34571874 PMC: 8471442. DOI: 10.3390/cells10092226.


Divide-and-Conquer Matrisome Protein (DC-MaP) Strategy: An MS-Friendly Approach to Proteomic Matrisome Characterization.

Ouni E, Pyr Dit Ruys S, Dolmans M, Herinckx G, Vertommen D, Amorim C Int J Mol Sci. 2020; 21(23).

PMID: 33266304 PMC: 7730167. DOI: 10.3390/ijms21239141.


References
1.
Patterson S, Aebersold R . Proteomics: the first decade and beyond. Nat Genet. 2003; 33 Suppl:311-23. DOI: 10.1038/ng1106. View

2.
Kim B, Jang I, Shin S, Kwon Y, Heo S, Choi E . Therapeutic angiogenesis in a murine model of limb ischemia by recombinant periostin and its fasciclin I domain. Biochim Biophys Acta. 2014; 1842(9):1324-32. DOI: 10.1016/j.bbadis.2014.05.004. View

3.
Tao G, Levay A, Peacock J, Huk D, Both S, Purcell N . Collagen XIV is important for growth and structural integrity of the myocardium. J Mol Cell Cardiol. 2012; 53(5):626-38. PMC: 3472103. DOI: 10.1016/j.yjmcc.2012.08.002. View

4.
Chen H, Wang J, Xiang M, Lin Y, He A, Jin C . Cathepsin S-mediated fibroblast trans-differentiation contributes to left ventricular remodelling after myocardial infarction. Cardiovasc Res. 2013; 100(1):84-94. PMC: 3778959. DOI: 10.1093/cvr/cvt158. View

5.
Spiro R . Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology. 2002; 12(4):43R-56R. DOI: 10.1093/glycob/12.4.43r. View