Novel regulators of cardiac inflammation: Matricellular proteins expand their repertoire

Journal of Molecular and Cellular Cardiology

Volumn 91, Issue , 2016, Pages 172-178

  Rienks, Marieke ^a   Papageorgiou, Anna Pia ^a,b  

^a MAASTRICHT UNIVERSITY   (Netherlands)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Matricellular proteins; Matrix; Myocarditis; Sterile inflammation

Indexed keywords

BIGLYCAN; CELL PROTEIN; CONNECTIVE TISSUE GROWTH FACTOR; CYSTEINE RICH PROTEIN 61; DECORIN; GALECTIN; LUMICAN; MATRICELLULAR PROTEIN; OSTEONECTIN; OSTEOPONTIN; PATHOGEN ASSOCIATED MOLECULAR PATTERN; SCLEROPROTEIN; TENASCIN; THROMBOSPONDIN; UNCLASSIFIED DRUG; CCN PROTEIN; SPARC PROTEIN, HUMAN;

ADAPTIVE IMMUNITY; APOPTOSIS; AUTOIMMUNITY; CARDITIS; CYTOTOXIC T LYMPHOCYTE; CYTOTOXICITY; DISEASE COURSE; DISEASE SEVERITY; HEART INJURY; HUMAN; IMMUNE RESPONSE; IMMUNOCOMPETENT CELL; IMMUNOLOGICAL TOLERANCE; IMMUNOMODULATION; IMMUNOREGULATION; INNATE IMMUNITY; LYMPHOCYTE ACTIVATION; MACROPHAGE; MYOCARDITIS; NONHUMAN; PATHOGENESIS; PHAGOCYTOSIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; REVIEW; UPREGULATION; VIRUS MYOCARDITIS; VIRUS REPLICATION; ANIMAL; CARDIAC MUSCLE; FIBROSIS; GENE EXPRESSION REGULATION; GENETICS; HEART INFARCTION; INFLAMMATION; METABOLISM; PATHOLOGY; SIGNAL TRANSDUCTION;

ANIMALS; CCN INTERCELLULAR SIGNALING PROTEINS; FIBROSIS; GALECTINS; GENE EXPRESSION REGULATION; INFLAMMATION; MYOCARDIAL INFARCTION; MYOCARDITIS; MYOCARDIUM; OSTEONECTIN; OSTEOPONTIN; SIGNAL TRANSDUCTION; TENASCIN; THROMBOSPONDINS;

EID: 84954207176     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2016.01.008     Document Type: Review

References (134)

1. Dobaczewski M., Gonzalez-Quesada C., Frangogiannis N.G. The extracellular matrix as a modulator of the inflammatory and reparative response following myocardial infarction. J. Mol. Cell. Cardiol. 2010, 48(3):504-511.
2. Figdor C.G., van Kooyk Y., Adema G.J. C-type lectin receptors on dendritic cells and Langerhans cells. Nat. Rev. Immunol. 2002, 2(2):77-84.
3. Mitchell D.A., Fadden A.J., K.D. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J. Biol. Chem. 2001, 276(31):28939-28945.
4. Mogensen T.H. Pathogen recognition and inflammatory signaling in innate immune defenses. Clin. Microbiol. Rev. 2009, 22(2):240-273. (Table of Contents).
5. Akira S., Uematsu S., Takeuchi O. Pathogen recognition and innate immunity. Cell 2006, 124(4):783-801.
6. Peter M.E., Kubarenko A.V., Weber A.N., Dalpke A.H. Identification of an N-terminal recognition site in TLR9 that contributes to CpG-DNA-mediated receptor activation. J. Immunol. 2009, 182(12):7690-7697.
7. Hartupee J., Mann D.L. Role of inflammatory cells in fibroblast activation. J. Mol. Cell. Cardiol. 2015.
8. Elward K., Gasque P. "Eat me" and "don't eat me" signals govern the innate immune response and tissue repair in the CNS: emphasis on the critical role of the complement system. Mol. Immunol. 2003, 40(2-4):85-94.
9. Esko J.D., Kimata K., Lindahl U. Proteoglycans and sulfated glycosaminoglycans. Essentials of Glycobiology 2009, Cold Spring Harbor, NY. second ed. A. Varki, C. RD, E. JD, F. HH, P. Stanley, B. CR (Eds.).
10. Varki A. Since there are PAMPs and DAMPs, there must be SAMPs? Glycan "self-associated molecular patterns" dampen innate immunity, but pathogens can mimic them. Glycobiology 2011, 21(9):1121-1124.
11. Brunn G.J., Bungum M.K., Johnson G.B., Platt J.L. Conditional signaling by Toll-like receptor 4. FASEB J. 2005, 19(7):872-874.
12. Timmis J.N., Ayliffe M.A., Huang C.Y., Martin W. Endosymbiotic gene transfer: organelle genomes forge eukaryotic chromosomes. Nat. Rev. Genet. 2004, 5(2):123-135.
13. Escamilla-Tilch M., Filio-Rodriguez G., Garcia-Rocha R., Mancilla-Herrera I., Mitchison N.A., Ruiz-Pacheco J.A., et al. The interplay between pathogen-associated and danger-associated molecular patterns: an inflammatory code in cancer?. Immunol. Cell Biol. 2013, 91(10):601-610.
14. Bowles N.E., Vallejo J. Viral causes of cardiac inflammation. Curr. Opin. Cardiol. 2003, 18(3):182-188.
15. Fairweather D., Frisancho-Kiss S., Rose N.R. Viruses as adjuvants for autoimmunity: evidence from Coxsackievirus-induced myocarditis. Rev. Med. Virol. 2005, 15(1):17-27.
16. Triantafilou K., Orthopoulos G., Vakakis E., Ahmed M.A., Golenbock D.T., Lepper P.M., et al. Human cardiac inflammatory responses triggered by Coxsackie B viruses are mainly Toll-like receptor (TLR) 8-dependent. Cell. Microbiol. 2005, 7(8):1117-1126.
17. Yajima T., Knowlton K.U. Viral myocarditis: from the perspective of the virus. Circulation 2009, 119(19):2615-2624.
18. Marchant D., Si X., Luo H., McManus B., Yang D. The impact of CVB3 infection on host cell biology. Curr. Top. Microbiol. Immunol. 2008, 323:177-198.
19. Si X., Luo H., Morgan A., Zhang J., Wong J., Yuan J., et al. Stress-activated protein kinases are involved in coxsackievirus B3 viral progeny release. J. Virol. 2005, 79(22):13875-13881.
20. Corsten M.F., Schroen B., Heymans S. Inflammation in viral myocarditis: friend or foe?. Trends Mol. Med. 2012, 18(7):426-437.
21. Panayi G.S., Corrigall V.M., Henderson B. Stress cytokines: pivotal proteins in immune regulatory networks; Opinion. Curr. Opin. Immunol. 2004, 16(4):531-534.
22. Shi Y., Evans J.E., Rock K.L. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 2003, 425(6957):516-521.
23. Farkas A.M., Kilgore T.M., Lotze M.T. Detecting DNA: getting and begetting cancer. Curr. Opin. Investig. Drugs 2007, 8(12):981-986.
24. Termeer C., Benedix F., Sleeman J., Fieber C., Voith U., Ahrens T., et al. Oligosaccharides of Hyaluronan activate dendritic cells via toll-like receptor 4. J. Exp. Med. 2002, 195(1):99-111.
25. Johnson G.B., Brunn G.J., Kodaira Y., Platt J.L. Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J. Immunol. 2002, 168(10):5233-5239.
26. Ionita M.G., Arslan F., de Kleijn D.P., Pasterkamp G. Endogenous inflammatory molecules engage Toll-like receptors in cardiovascular disease. J. Innate Immun. 2010, 2(4):307-315.
27. Epelman S., Liu P.P., Mann D.L. Role of innate and adaptive immune mechanisms in cardiac injury and repair. Nat. Rev. Immunol. 2015, 15(2):117-129.
28. Prabhu S.D. It takes two to tango: monocyte and macrophage duality in the infarcted heart. Circ. Res. 2014, 114(10):1558-1560.
29. Dreyer W.J., Michael L.H., Nguyen T., Smith C.W., Anderson D.C., Entman M.L., et al. Kinetics of C5a release in cardiac lymph of dogs experiencing coronary artery ischemia-reperfusion injury. Circ. Res. 1992, 71(6):1518-1524.
30. Romson J.L., Hook B.G., Kunkel S.L., Abrams G.D., Schork M.A., Lucchesi B.R. Reduction of the extent of ischemic myocardial injury by neutrophil depletion in the dog. Circulation 1983, 67(5):1016-1023.
31. Jolly S.R., Kane W.J., Hook B.G., Abrams G.D., Kunkel S.L., Lucchesi B.R. Reduction of myocardial infarct size by neutrophil depletion: effect of duration of occlusion. Am. Heart J. 1986, 112(4):682-690.
32. Leuschner F., Dutta P., Gorbatov R., Novobrantseva T.I., Donahoe J.S., Courties G., et al. Therapeutic siRNA silencing in inflammatory monocytes in mice. Nat. Biotechnol. 2011, 29(11):1005-1010.
33. Mann D.L. The emerging role of innate immunity in the heart and vascular system: for whom the cell tolls. Circ. Res. 2011, 108(9):1133-1145.
34. Kain V., Prabhu S.D., Halade G.V. Inflammation revisited: inflammation versus resolution of inflammation following myocardial infarction. Basic Res. Cardiol. 2014, 109(6):444.
35. Nahrendorf M., Swirski F.K. Monocyte and macrophage heterogeneity in the heart. Circ. Res. 2013, 112(12):1624-1633.
36. Apostolakis S., Lip G.Y., Shantsila E. Monocytes in heart failure: relationship to a deteriorating immune overreaction or a desperate attempt for tissue repair?. Cardiovasc. Res. 2010, 85(4):649-660.
37. Fadok V.A., McDonald P.P., Bratton D.L., Henson P.M. Regulation of macrophage cytokine production by phagocytosis of apoptotic and post-apoptotic cells. Biochem. Soc. Trans. 1998, 26(4):653-656.
38. Voll R.E., Herrmann M., Roth E.A., Stach C., Kalden J.R., Girkontaite I. Immunosuppressive effects of apoptotic cells. Nature 1997, 390(6658):350-351.
39. Nahrendorf M., Swirski F.K., Aikawa E., Stangenberg L., Wurdinger T., Figueiredo J.L., et al. The healing myocardium sequentially mobilizes two monocyte subsets with divergent and complementary functions. J. Exp. Med. 2007, 204(12):3037-3047.
40. Wan E., Yeap X.Y., Dehn S., Terry R., Novak M., Zhang S., et al. Enhanced efferocytosis of apoptotic cardiomyocytes through myeloid-epithelial-reproductive tyrosine kinase links acute inflammation resolution to cardiac repair after infarction. Circ. Res. 2013, 113(8):1004-1012.
41. Nahrendorf M., Pittet M.J., Swirski F.K. Monocytes: protagonists of infarct inflammation and repair after myocardial infarction. Circulation 2010, 121(22):2437-2445.
42. Cooper G.M., Hausman R.E. The cell: a molecular approach 2013, xxv. Sinauer Associates, Sunderland, MA, (832 pp.). sixth ed.
43. Munz C. Antigen processing for MHC class II presentation via autophagy. Front. Immunol. 2012, 3:9.
44. Hopp A.K., Rupp A., Lukacs-Kornek V. Self-antigen presentation by dendritic cells in autoimmunity. Front. Immunol. 2014, 5:55.
45. Hofmann U., Beyersdorf N., Weirather J., Podolskaya A., Bauersachs J., Ertl G., et al. Activation of CD4+ T lymphocytes improves wound healing and survival after experimental myocardial infarction in mice. Circulation 2012, 125(13):1652-1663.
46. Li K., Xu W., Guo Q., Jiang Z., Wang P., Yue Y., et al. Differential macrophage polarization in male and female BALB/c mice infected with coxsackievirus B3 defines susceptibility to viral myocarditis. Circ. Res. 2009, 105(4):353-364.
47. Shi Y., Fukuoka M., Li G., Liu Y., Chen M., Konviser M., et al. Regulatory T cells protect mice against coxsackievirus-induced myocarditis through the transforming growth factor-coxsackie-adenovirus receptor pathway. Circulation 2010.
48. Opavsky M.A., Penninger J., Aitken K., Wen W.H., Dawood F., Mak T., et al. Susceptibility to myocarditis is dependent on the response of alphabeta T lymphocytes to coxsackieviral infection. Circ. Res. 1999, 85(6):551-558.
49. Mena I., Perry C.M., Harkins S., Rodriguez F., Gebhard J., Whitton J.L. The role of B lymphocytes in coxsackievirus B3 infection. Am. J. Pathol. 1999, 155(4):1205-1215.
50. Godeny E.K., Gauntt C.J. Involvement of natural killer cells in coxsackievirus B3-induced murine myocarditis. J. Immunol. 1986, 137(5):1695-1702.
51. Yang Z., Day Y.J., Toufektsian M.C., Xu Y., Ramos S.I., Marshall M.A., et al. Myocardial infarct-sparing effect of adenosine A2A receptor activation is due to its action on CD4+ T lymphocytes. Circulation 2006, 114(19):2056-2064.
52. Weirather J., Hofmann U.D., Beyersdorf N., Ramos G.C., Vogel B., Frey A., et al. Foxp3+ CD4+ T cells improve healing after myocardial infarction by modulating monocyte/macrophage differentiation. Circ. Res. 2014, 115(1):55-67.
53. Bornstein P. Matricellular proteins: an overview. J. Cell Commun. Signal. 2009, 3(3-4):163-165.
54. Bornstein P. Matricellular proteins: an overview. Matrix Biol. 2000, 19(7):555-556.
55. Murphy-Ullrich J.E., Sage E.H. Revisiting the matricellular concept. Matrix Biol. 2014, 37:1-14.
56. Midwood K.S., Orend G. The role of tenascin-C in tissue injury and tumorigenesis. J. Cell Commun. Signal. 2009, 3(3-4):287-310.
57. Norris R.A., Moreno-Rodriguez R., Hoffman S., Markwald R.R. The many facets of the matricelluar protein periostin during cardiac development, remodeling, and pathophysiology. J. Cell Commun. Signal. 2009, 3(3-4):275-286.
58. Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A., Blair N.S., et al. A thrombospondin-dependent pathway for a protective ER stress response. Cell 2012, 149(6):1257-1268.
59. Frangogiannis N.G. Matricellular proteins in cardiac adaptation and disease. Physiol. Rev. 2012, 92(2):635-688.
60. Carlson C.B., Lawler J., Mosher D.F. Structures of thrombospondins. Cell. Mol. Life Sci. 2008, 65(5):672-686.
61. Bentley A.A., Adams J.C. The evolution of thrombospondins and their ligand-binding activities. Mol. Biol. Evol. 2010, 27(9):2187-2197.
62. Papageorgiou A.P., Swinnen M., Vanhoutte D., VandenDriessche T., Chuah M., Lindner D., et al. Thrombospondin-2 prevents cardiac injury and dysfunction in viral myocarditis through the activation of regulatory T-cells. Cardiovasc. Res. 2012, 94(1):115-124.
63. Lamy L., Foussat A., Brown E.J., Bornstein P., Ticchioni M., Bernard A. Interactions between CD47 and thrombospondin reduce inflammation. J. Immunol. 2007, 178(9):5930-5939.
64. Grimbert P., Bouguermouh S., Baba N., Nakajima T., Allakhverdi Z., Braun D., et al. Thrombospondin/CD47 interaction: a pathway to generate regulatory T cells from human CD4+ CD25- T cells in response to inflammation. J. Immunol. 2006, 177(6):3534-3541.
65. Savill J., Hogg N., Ren Y., Haslett C. Thrombospondin cooperates with CD36 and the vitronectin receptor in macrophage recognition of neutrophils undergoing apoptosis. J. Clin. Invest. 1992, 90(4):1513-1522.
66. Brekken R.A., Sage E.H. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 2001, 19(8):816-827.
67. Schellings M.W., Vanhoutte D., Swinnen M., Cleutjens J.P., Debets J., van Leeuwen R.E., et al. Absence of SPARC results in increased cardiac rupture and dysfunction after acute myocardial infarction. J. Exp. Med. 2009, 206(1):113-123.
68. Bradshaw A.D., Baicu C.F., Rentz T.J., Van Laer A.O., Boggs J., Lacy J.M., et al. Pressure overload-induced alterations in fibrillar collagen content and myocardial diastolic function: role of secreted protein acidic and rich in cysteine (SPARC) in post-synthetic procollagen processing. Circulation 2009, 119(2):269-280.
69. Maurer P., Gohring W., Sasaki T., Mann K., Timpl R., Nischt R. Recombinant and tissue-derived mouse BM-40 bind to several collagen types and have increased affinities after proteolytic activation. Cell. Mol. Life Sci. 1997, 53(5):478-484.
70. Sasaki T., Gohring W., Mann K., Maurer P., Hohenester E., Knauper V., et al. Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J. Biol. Chem. 1997, 272(14):9237-9243.
71. Sage E.H., Reed M., Funk S.E., Truong T., Steadele M., Puolakkainen P., et al. Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis. J. Biol. Chem. 2003, 278(39):37849-37857.
72. Toba H., de Castro Bras L.E., Baicu C.F., Zile M.R., Lindsey M.L., Bradshaw A.D. Secreted protein acidic and rich in cysteine facilitates age-related cardiac inflammation and macrophage M1 polarization. Am. J. Physiol. Cell Physiol. 2015, 308(12):C972-C982.
73. Toba H., Brás LdC, Baicu C., Zile M., Lindsey M., Bradshaw A.D. SPARC Facilitates Inflammation in the Aging Heart and Suppresses Macrophage M2 Polarization. FASEB J. Nat. Biotechnol. 2015, vol. 29(no. 1 Supplement 1047.1).
74. Chiquet-Ehrismann R., Chiquet M. Tenascins: regulation and putative functions during pathological stress. J. Pathol. 2003, 200(4):488-499.
75. Niebroj-Dobosz I. Tenascin-C in human cardiac pathology. Clin. Chim. Acta 2012, 413(19-20):1516-1518.
76. Hsia H.C., Schwarzbauer J.E. Meet the tenascins: multifunctional and mysterious. J. Biol. Chem. 2005, 280(29):26641-26644.
77. Jones F.S., Jones P.L. The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev. Dyn. 2000, 218(2):235-259.
78. Clark R.A., Erickson H.P., Springer T.A. Tenascin supports lymphocyte rolling. J. Cell Biol. 1997, 137(3):755-765.
79. Loike J.D., Cao L., Budhu S., Hoffman S., Silverstein S.C. Blockade of alpha 5 beta 1 integrins reverses the inhibitory effect of tenascin on chemotaxis of human monocytes and polymorphonuclear leukocytes through three-dimensional gels of extracellular matrix proteins. J. Immunol. 2001, 166(12):7534-7542.
80. Midwood K., Sacre S., Piccinini A.M., Inglis J., Trebaul A., Chan E., et al. Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nat. Med. 2009, 15(7):774-780.
81. Nishioka T., Onishi K., Shimojo N., Nagano Y., Matsusaka H., Ikeuchi M., et al. Tenascin-C may aggravate left ventricular remodeling and function after myocardial infarction in mice. Am. J. Physiol. Heart Circ. Physiol. 2010, 298(3):H1072-H1078.
82. Shimojo N., Hashizume R., Kanayama K., Hara M., Suzuki Y., Nishioka T., et al. Tenascin-C may accelerate cardiac fibrosis by activating macrophages via the integrin alphaVbeta3/nuclear factor-kappaB/interleukin-6 axis. Hypertension 2015, 66(4):757-766.
83. Machino-Ohtsuka T., Tajiri K., Kimura T., Sakai S., Sato A., Yoshida T., et al. Tenascin-C aggravates autoimmune myocarditis via dendritic cell activation and Th17 cell differentiation. J. Am. Heart Assoc. 2014, 3(6):e001052.
84. Bork P. The modular architecture of a new family of growth regulators related to connective tissue growth factor. FEBS Lett. 1993, 327(2):125-130.
85. Mosher D.F., Adams J.C. Adhesion-modulating/matricellular ECM protein families: a structural, functional and evolutionary appraisal. Matrix Biol. 2012, 31(3):155-161.
86. Hilfiker-Kleiner D., Kaminski K., Kaminska A., Fuchs M., Klein G., Podewski E., et al. Regulation of proangiogenic factor CCN1 in cardiac muscle: impact of ischemia, pressure overload, and neurohumoral activation. Circulation 2004, 109(18):2227-2233.
87. Yoshida Y., Togi K., Matsumae H., Nakashima Y., Kojima Y., Yamamoto H., et al. CCN1 protects cardiac myocytes from oxidative stress via beta1 integrin-Akt pathway. Biochem. Biophys. Res. Commun. 2007, 355(3):611-618.
88. Rother M., Krohn S., Kania G., Vanhoutte D., Eisenreich A., Wang X., et al. Matricellular signaling molecule CCN1 attenuates experimental autoimmune myocarditis by acting as a novel immune cell migration modulator. Circulation 2010, 122(25):2688-2698.
89. Wittchen F., Suckau L., Witt H., Skurk C., Lassner D., Fechner H., et al. Genomic expression profiling of human inflammatory cardiomyopathy (DCMi) suggests novel therapeutic targets. J. Mol. Med. (Berl.) 2007, 85(3):257-271.
90. Bai T., Chen C.C., Lau L.F. Matricellular protein CCN1 activates a proinflammatory genetic program in murine macrophages. J. Immunol. 2010, 184(6):3223-3232.
91. Lobel M., Bauer S., Meisel C., Eisenreich A., Kudernatsch R., Tank J., et al. CCN1: a novel inflammation-regulated biphasic immune cell migration modulator. Cell. Mol. Life Sci. 2012, 69(18):3101-3113.
92. Merline R., Schaefer R.M., Schaefer L. The matricellular functions of small leucine-rich proteoglycans (SLRPs). J. Cell Commun. Signal. 2009, 3(3-4):323-335.
93. Gonzalez R., Urrea R., Gonzalez M., Inestrosa N.C., Brandan E. Isolation of proteoglycans synthesized by rat heart: evidence for the presence of several distinct forms. Gen. Pharmacol. 1992, 23(2):249-255.
94. Bereczki E., Santha M. The role of biglycan in the heart. Connect. Tissue Res. 2008, 49(3):129-132.
95. Latif N., Sarathchandra P., Taylor P.M., Antoniw J., Yacoub M.H. Localization and pattern of expression of extracellular matrix components in human heart valves. J. Heart Valve Dis. 2005, 14(2):218-227.
96. Ayada Y., Kusachi S., Murakami T., Hirohata S., Takemoto S., Komatsubara I., et al. Increased expression of biglycan mRNA in pressure-overloaded rat heart. Clin. Exp. Hypertens. 2001, 23(8):633-643.
97. Ahmed M.S., Oie E., Vinge L.E., Yndestad A., Andersen G.G., Andersson Y., et al. Induction of myocardial biglycan in heart failure in rats-an extracellular matrix component targeted by AT(1) receptor antagonism. Cardiovasc. Res. 2003, 60(3):557-568.
98. Medeiros D.M., Velleman S.G., Jarrold B.B., Shiry L.J., Radin M.J., McCune S.A. Ontogeny of enhanced decorin levels and distribution within myocardium of failing hearts. Connect. Tissue Res. 2002, 43(1):32-43.
99. Doi M., Kusachi S., Murakami T., Ninomiya Y., Murakami M., Nakahama M., et al. Time-dependent changes of decorin in the infarct zone after experimentally induced myocardial infarction in rats: comparison with biglycan. Pathol. Res. Pract. 2000, 196(1):23-33.
100. Zimmerman S.D., Thomas D.P., Velleman S.G., Li X., Hansen T.R., McCormick R.J. Time course of collagen and decorin changes in rat cardiac and skeletal muscle post-MI. Am. J. Physiol. Heart Circ. Physiol. 2001, 281(4):H1816-H1822.
101. Hao J., Ju H., Zhao S., Junaid A., Scammell-La Fleur T., Dixon I.M. Elevation of expression of Smads 2, 3, and 4, decorin and TGF-beta in the chronic phase of myocardial infarct scar healing. J. Mol. Cell. Cardiol. 1999, 31(3):667-678.
102. Song R., Zeng Q., Ao L., Yu J.A., Cleveland J.C., Zhao K.S., et al. Biglycan induces the expression of osteogenic factors in human aortic valve interstitial cells via Toll-like receptor-2. Arterioscler. Thromb. Vasc. Biol. 2012, 32(11):2711-2720.
103. Mersmann J., Habeck K., Latsch K., Zimmermann R., Jacoby C., Fischer J.W., et al. Left ventricular dilation in toll-like receptor 2 deficient mice after myocardial ischemia/reperfusion through defective scar formation. Basic Res. Cardiol. 2011, 106(1):89-98.
104. Schaefer L., Babelova A., Kiss E., Hausser H.J., Baliova M., Krzyzankova M., et al. The matrix component biglycan is proinflammatory and signals through Toll-like receptors 4 and 2 in macrophages. J. Clin. Invest. 2005, 115(8):2223-2233.
105. Babelova A., Moreth K., Tsalastra-Greul W., Zeng-Brouwers J., Eickelberg O., Young M.F., et al. Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors. J. Biol. Chem. 2009, 284(36):24035-24048.
106. Merline R., Moreth K., Beckmann J., Nastase M.V., Zeng-Brouwers J., Tralhao J.G., et al. Signaling by the matrix proteoglycan decorin controls inflammation and cancer through PDCD4 and MicroRNA-21. Sci. Signal. 2011, 4(199):ra75.
107. Wu F., Vij N., Roberts L., Lopez-Briones S., Joyce S., Chakravarti S. A novel role of the lumican core protein in bacterial lipopolysaccharide-induced innate immune response. J. Biol. Chem. 2007, 282(36):26409-26417.
108. Carlson E.C., Lin M., Liu C.Y., Kao W.W., Perez V.L., Pearlman E. Keratocan and lumican regulate neutrophil infiltration and corneal clarity in lipopolysaccharide-induced keratitis by direct interaction with CXCL1. J. Biol. Chem. 2007, 282(49):35502-35509.
109. Hwang J.J., Allen P.D., Tseng G.C., Lam C.W., Fananapazir L., Dzau V.J., et al. Microarray gene expression profiles in dilated and hypertrophic cardiomyopathic end-stage heart failure. Physiol. Genomics 2002, 10(1):31-44.
110. Bergquist J., Baykut G., Bergquist M., Witt M., Mayer F.J., Baykut D. Human myocardial protein pattern reveals cardiac diseases. Int. J. Proteomics 2012, 2012:342659.
111. Engebretsen K.V., Lunde I.G., Strand M.E., Waehre A., Sjaastad I., Marstein H.S., et al. Lumican is increased in experimental and clinical heart failure, and its production by cardiac fibroblasts is induced by mechanical and proinflammatory stimuli. FEBS J. 2013, 280(10):2382-2398.
112. Yang R.Y., Rabinovich G.A., Liu F.T. Galectins: structure, function and therapeutic potential. Expert Rev. Mol. Med. 2008, 10:e17.
113. Elola M.T., Wolfenstein-Todel C., Troncoso M.F., Vasta G.R., Rabinovich G.A. Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival. Cell. Mol. Life Sci. 2007, 64(13):1679-1700.
114. Sato S., St-Pierre C., Bhaumik P., Nieminen J. Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs). Immunol. Rev. 2009, 230(1):172-187.
115. Pello A.M., Cristobal C., Tarin N., Huelmos A., Acena A., Carda R., et al. Differential profile in inflammatory and mineral metabolism biomarkers in patients with ischemic heart disease without classical coronary risk factors. J. Cardiol. 2015, 66(1):22-27.
116. Weir R.A., Petrie C.J., Murphy C.A., Clements S., Steedman T., Miller A.M., et al. Galectin-3 and cardiac function in survivors of acute myocardial infarction. Circ. Heart Fail. 2013, 6(3):492-498.
117. Seropian I.M., Cerliani J.P., Toldo S., Van Tassell B.W., Ilarregui J.M., Gonzalez G.E., et al. Galectin-1 controls cardiac inflammation and ventricular remodeling during acute myocardial infarction. Am. J. Pathol. 2013, 182(1):29-40.
118. Sano H., Hsu D.K., Yu L., Apgar J.R., Kuwabara I., Yamanaka T., et al. Human galectin-3 is a novel chemoattractant for monocytes and macrophages. J. Immunol. 2000, 165(4):2156-2164.
119. Jaquenod De Giusti C., AE U., Rivadeneyra L., Schattner M., RM G. Macrophages and galectin 3 play critical roles in CVB3-induced murine acute myocarditis and chronic fibrosis. J. Mol. Cell. Cardiol. 2015, 85:58-70.
120. Martinez-Martinez E., Calvier L., Fernandez-Celis A., Rousseau E., Jurado-Lopez R., Rossoni L.V., et al. Galectin-3 blockade inhibits cardiac inflammation and fibrosis in experimental hyperaldosteronism and hypertension. Hypertension 2015, 66(4):767-775.
121. Wang K.X., Denhardt D.T. Osteopontin: role in immune regulation and stress responses. Cytokine Growth Factor Rev. 2008, 19(5-6):333-345.
122. Murry C.E., Giachelli C.M., Schwartz S.M., Vracko R. Macrophages express osteopontin during repair of myocardial necrosis. Am. J. Pathol. 1994, 145(6):1450-1462.
123. Dobaczewski M., Bujak M., Zymek P., Ren G., Entman M.L., Frangogiannis N.G. Extracellular matrix remodeling in canine and mouse myocardial infarcts. Cell Tissue Res. 2006, 324(3):475-488.
124. Rollo E.E., Denhardt D.T. Differential effects of osteopontin on the cytotoxic activity of macrophages from young and old mice. Immunology 1996, 88(4):642-647.
125. Zhu B., Suzuki K., Goldberg H.A., Rittling S.R., Denhardt D.T., McCulloch C.A., et al. Osteopontin modulates CD44-dependent chemotaxis of peritoneal macrophages through G-protein-coupled receptors: evidence of a role for an intracellular form of osteopontin. J. Cell. Physiol. 2004, 198(1):155-167.
126. Koguchi Y., Kawakami K., Kon S., Segawa T., Maeda M., Uede T., et al. Penicillium marneffei causes osteopontin-mediated production of interleukin-12 by peripheral blood mononuclear cells. Infect. Immun. 2002, 70(3):1042-1048.
127. Vetrone S.A., Montecino-Rodriguez E., Kudryashova E., Kramerova I., Hoffman E.P., Liu S.D., et al. Osteopontin promotes fibrosis in dystrophic mouse muscle by modulating immune cell subsets and intramuscular TGF-beta. J. Clin. Invest. 2009, 119(6):1583-1594.
128. Szalay G., Sauter M., Haberland M., Zuegel U., Steinmeyer A., Kandolf R., et al. Osteopontin: a fibrosis-related marker molecule in cardiac remodeling of enterovirus myocarditis in the susceptible host. Circ. Res. 2009, 104(7):851-859.
129. Simpson D.M., Ross R. Effects of heterologous antineutrophil serum in guinea pigs. Hematologic and ultrastructural observations. Am. J. Pathol. 1971, 65(1):79-102.
130. Simpson D.M., Ross R. The neutrophilic leukocyte in wound repair a study with antineutrophil serum. J. Clin. Invest. 1972, 51(8):2009-2023.
131. Martin P., D'Souza D., Martin J., Grose R., Cooper L., Maki R., et al. Wound healing in the PU.1 null mouse-tissue repair is not dependent on inflammatory cells. Curr. Biol. 2003, 13(13):1122-1128.
132. Frangogiannis N.G. Inflammation in cardiac injury, repair and regeneration. Curr. Opin. Cardiol. 2015, 30(3):240-245.
133. Rienks M., Papageorgiou A.P., Frangogiannis N.G., Heymans S. Myocardial extracellular matrix: an ever-changing and diverse entity. Circ. Res. 2014, 114(5):872-888.
134. de Haan J.J., Smeets M.B., Pasterkamp G., Arslan F. Danger signals in the initiation of the inflammatory response after myocardial infarction. Mediat. Inflamm. 2013, 2013:206039.