Galectin-3: A Modifiable Risk Factor in Heart Failure
Tóm tắt
Myocardial galectin-3 is upregulated upon cardiac stressors such as angiotensin II and pressure overload leading to cardiac remodeling and heart failure. The expression level of galectin-3 mirrors the progression and severity of heart failure and therefore, galectin-3 is being used as a biomarker for heart failure. However, as galectin-3 is causally involved in pathological myocardial fibrosis it has been suggested that galectin-3 also actively contributes to heart failure development. In this review we discuss how galectin-3 could be a target for therapy in heart failure. Currently, attempts are being made to target or inhibit galectin-3 using natural or pharmaceutical inhibitors with the aim to ameliorate heart failure. Available experimental evidence suggests that galectin-3 inhibition indeed may represent a novel tool to treat heart failure. A strong interaction with aldosterone, another strong pro-fibrotic factor, has been described. Clinical studies are needed to prove if galectin-3 may be used to install specific treatment regimens.
Tài liệu tham khảo
McMurray JJ, Adamopoulos S, Anker SD, et al. ESC guidelines for the diagnosis and treatment of acute and chronic heart failure 2012: The Task Force for the Diagnosis and Treatment of Acute and Chronic Heart Failure 2012 of the European Society of Cardiology. Developed in collaboration with the Heart Failure Association (HFA) of the ESC. Eur J Heart Fail. 2012;14:803–69.
Bui AL, Horwich TB, Fonarow GC. Epidemiology and risk profile of heart failure. Nat Rev Cardiol. 2011;8:30–41.
von Lueder TG, Krum H. RAAS inhibitors and cardiovascular protection in large scale trials. Cardiovasc Drugs Ther. 2013;27:171–9.
Parikh R, Kadowitz PJ. A review of current therapies used in the treatment of congestive heart failure. Expert Rev Cardiovasc Ther. 2013;11:1171–8.
Shah AM, Mann DL. In search of new therapeutic targets and strategies for heart failure: recent advances in basic science. Lancet. 2011;378:704–12.
Krum H, Tonkin A. Why do phase III trials of promising heart failure drugs often fail? The contribution of “regression to the truth”. J Card Fail. 2003;9:364–7.
Voors AA, van Veldhuisen DJ. Why do drugs for acute heart failure fail? Eur J Heart Fail. 2012;14:955–6.
Roubille F, Busseuil D, Merlet N, et al. Investigational drugs targeting cardiac fibrosis. Expert Rev Cardiovasc Ther. 2014;12:111–25.
van Kimmenade RR, Januzzi Jr JL, Ellinor PT, et al. Utility of amino-terminal pro-brain natriuretic peptide, galectin-3, and apelin for the evaluation of patients with acute heart failure. J Am Coll Cardiol. 2006;48:1217–24.
Lok DJ, Lok SI, Bruggink-Andre de la Porte PW, et al. Galectin-3 is an independent marker for ventricular remodeling and mortality in patients with chronic heart failure. Clin Res Cardiol. 2013;102:103–10.
de Boer RA, Edelmann F, Cohen-Solal A, et al. Galectin-3 in heart failure with preserved ejection fraction. Eur J Heart Fail. 2013;15:1095–101.
Carrasco-Sanchez FJ, Aramburu-Bodas O, Salamanca-Bautista P, et al. Predictive value of serum galectin-3 levels in patients with acute heart failure with preserved ejection fraction. Int J Cardiol. 2013;169:177–82.
de Boer RA, Lok DJ, Jaarsma T, et al. Predictive value of plasma galectin-3 levels in heart failure with reduced and preserved ejection fraction. Ann Med. 2011;43:60–8.
Shah RV, Chen-Tournoux AA, Picard MH, et al. Galectin-3, cardiac structure and function, and long-term mortality in patients with acutely decompensated heart failure. Eur J Heart Fail. 2010;12:826–32.
Ho MK, Springer TA. Mac-2, a novel 32,000 Mr mouse macrophage subpopulation-specific antigen defined by monoclonal antibodies. J Immunol. 1982;128:1221–8.
Raz A, Carmi P, Raz T, et al. Molecular cloning and chromosomal mapping of a human galactoside-binding protein. Cancer Res. 1991;51:2173–8.
de Boer RA, Voors AA, Muntendam P, et al. Galectin-3: a novel mediator of heart failure development and progression. Eur J Heart Fail. 2009;11:811–7.
Henderson NC, Sethi T. The regulation of inflammation by galectin-3. Immunol Rev. 2009;230:160–71.
Dhirapong A, Lleo A, Leung P, et al. The immunological potential of galectin-1 and -3. Autoimmun Rev. 2009;8:360–3.
Newlaczyl AU, Yu LG. Galectin-3—a jack-of-all-trades in cancer. Cancer Lett. 2011;313:123–8.
de Boer RA, Yu L, van Veldhuisen DJ. Galectin-3 in cardiac remodeling and heart failure. Curr Heart Fail Rep. 2010;7:1–8.
Sherwi N, Merali S, Wong K. Personalizing biomarker strategies in heart failure with galectin-3. Futur Cardiol. 2012;8:885–94.
Sharma UC, Pokharel S, van Brakel TJ, et al. Galectin-3 marks activated macrophages in failure-prone hypertrophied hearts and contributes to cardiac dysfunction. Circulation. 2004;110:3121–8.
Liu YH, D’Ambrosio M, Liao TD, et al. N-acetyl-seryl-aspartyl-lysyl-proline prevents cardiac remodeling and dysfunction induced by galectin-3, a mammalian adhesion/growth-regulatory lectin. Am J Physiol Heart Circ Physiol. 2009;296:H404–12.
Yu L, Ruifrok WP, Meissner M, et al. Genetic and pharmacological inhibition of galectin-3 prevents cardiac remodeling by interfering with myocardial fibrogenesis. Circ Heart Fail. 2013;6:107–17.
Rabinovich GA, Baum LG, Tinari N, et al. Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response? Trends Immunol. 2002;23:313–20.
Ahmad N, Gabius HJ, Andre S, et al. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J Biol Chem. 2004;279:10841–7.
Henderson NC, Mackinnon AC, Farnworth SL, et al. Galectin-3 regulates myofibroblast activation and hepatic fibrosis. Proc Natl Acad Sci U S A. 2006;103:5060–5.
Henderson NC, Mackinnon AC, Farnworth SL, et al. Galectin-3 expression and secretion links macrophages to the promotion of renal fibrosis. Am J Pathol. 2008;172:288–98.
van den Borne SW, Diez J, Blankesteijn WM, et al. Myocardial remodeling after infarction: the role of myofibroblasts. Nat Rev Cardiol. 2010;7:30–7.
Meijers WC, van der Velde AR, de Boer RA. The ARCHITECT galectin-3 assay: comparison with other automated and manual assays for the measurement of circulating galectin-3 levels in heart failure. Exp Rev Mol Diagn. 2014;14:257--66.
de Boer RA, van Veldhuisen DJ, Gansevoort RT, et al. The fibrosis marker galectin-3 and outcome in the general population. J Intern Med. 2012;272:55–64.
Ho JE, Liu C, Lyass A, et al. Galectin-3, a marker of cardiac fibrosis, predicts incident heart failure in the community. J Am Coll Cardiol. 2012;60:1249–56.
Lok DJ, Van Der Meer P, de la Porte PW, et al. Prognostic value of galectin-3, a novel marker of fibrosis, in patients with chronic heart failure: data from the DEAL-HF study. Clin Res Cardiol. 2010;99:323–8.
Tang WH, Shrestha K, Shao Z, et al. Usefulness of plasma galectin-3 levels in systolic heart failure to predict renal insufficiency and survival. Am J Cardiol. 2011;108:385–90.
Ueland T, Aukrust P, Broch K, et al. Galectin-3 in heart failure: high levels are associated with all-cause mortality. Int J Cardiol. 2011;150:361–4.
Gullestad L, Ueland T, Kjekshus J, et al. Galectin-3 predicts response to statin therapy in the Controlled Rosuvastatin Multinational Trial in Heart Failure (CORONA). Eur Heart J. 2012;33:2290–6.
Felker GM, Fiuzat M, Shaw LK, et al. Galectin-3 in ambulatory patients with heart failure: results from the HF-ACTION study. Circ Heart Fail. 2012;5:72–8.
Baig MK, Mahon N, McKenna WJ, et al. The pathophysiology of advanced heart failure. Am Heart J. 1998;135:S216–30.
Sathisha UV, Jayaram S, Harish Nayaka MA, et al. Inhibition of galectin-3 mediated cellular interactions by pectic polysaccharides from dietary sources. Glycoconj J. 2007;24:497–507.
Pienta KJ, Naik H, Akhtar A, et al. Inhibition of spontaneous metastasis in a rat prostate cancer model by oral administration of modified citrus pectin. J Natl Cancer Inst. 1995;87:348–53.
Nangia-Makker P, Hogan V, Honjo Y, et al. Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin. J Natl Cancer Inst. 2002;94:1854–62.
Glinskii OV, Huxley VH, Glinsky GV, et al. Mechanical entrapment is insufficient and intercellular adhesion is essential for metastatic cell arrest in distant organs. Neoplasia. 2005;7:522–7.
Kolatsi-Joannou M, Price KL, Winyard PJ, et al. Modified citrus pectin reduces galectin-3 expression and disease severity in experimental acute kidney injury. PLoS ONE. 2011;6:e18683.
Schols H, Voragen A. The chemical structure of pectins. In: Seymour G, editor. Pectins and their manipulation. Oxford: Blackwell Publishing Ltd; 2002. p. 1–29.
Zannad F, Alla F, Dousset B, et al. Limitation of excessive extracellular matrix turnover may contribute to survival benefit of spironolactone therapy in patients with congestive heart failure: insights from the randomized aldactone evaluation study (RALES). Rales Investigators. Circulation. 2000;102:2700–6.
Calvier L, Miana M, Reboul P, et al. Galectin-3 mediates aldosterone-induced vascular fibrosis. Arterioscler Thromb Vasc Biol. 2013;33:67–75.
van der Velde AR, Gullestad L, Ueland T, et al. Prognostic value of changes in galectin-3 levels over time in patients with heart failure: data from CORONA and COACH. Circ Heart Fail. 2013;6:219–26.
Fiuzat M, Schulte PJ, Felker M, et al. Relationship between galectin-3 levels and mineralocorticoid receptor antagonist use in heart failure: analysis from HF-ACTION. J Card Fail. 2014;20:38–44.