High Mobility Group Box 1 and Cardiovascular Diseases: Study of Act and Connect

1.

Xu, Y., Wan, W., Zeng, H., Xiang, Z., Li, M., Yao, Y., & Wu, J. (2023). Exosomes and their derivatives as biomarkers and therapeutic delivery agents for cardiovascular diseases: Situations and challenges. Journal of Translational Internal Medicine, 11(4), 341–354.CrossRefPubMedPubMedCentral

2.

Liu, Z., Huang, Y., Li, H., Li, W., Zhang, F., Ouyang, W., Wang, S., Luo, Z., Wang, J., Chen, Y., & Xia, R. (2023). A generalized deep learning model for heart failure diagnosis using dynamic and static ultrasound. Journal of Translational Internal Medicine, 11(2), 138–144.CrossRefPubMedPubMedCentral

3.

Yang, Y., Muisha, M. B., Zhang, J., Sun, Y., & Li, Z. (2023). Research progress on N6-adenosylate methylation RNA modification in heart failure remodeling. Journal of Translational Internal Medicine, 10(4), 340–348.CrossRefPubMedPubMedCentral

4.

Frangogiannis, N. G. (2014). The inflammatory response in myocardial injury, repair, and remodelling. Nature Reviews Cardiology, 11(5), 255–265. https://doi.org/10.1038/nrcardio.2014.28CrossRefPubMedPubMedCentral

5.

Štros, M. (2010). HMGB proteins: Interactions with DNA and chromatin. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1799(1–2), 101–113. https://doi.org/10.1016/j.bbagrm.2009.09.008CrossRefPubMed

6.

Andersson, U., Wang, H., Palmblad, K., Aveberger, A. C., Bloom, O., Erlandsson-Harris, H., & Tracey, K. J. (2000). High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. The Journal of Experimental Medicine, 192(4), 565–570. https://doi.org/10.1084/jem.192.4.565CrossRefPubMedPubMedCentral

7.

Funayama, A., Shishido, T., Netsu, S., Narumi, T., Kadowaki, S., Takahashi, H., & Kubota, I. (2013). Cardiac nuclear high mobility group box 1 prevents the development of cardiac hypertrophy and heart failure. Cardiovascular Research, 99(4), 657–664. https://doi.org/10.1093/cvr/cvt128CrossRefPubMedPubMedCentral

8.

Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X. G., Yan, Z., & Sun, X. (2014). HMGB1 in health and disease. Molecular Aspects of Medicine, 40, 1–16. https://doi.org/10.1016/j.mam.2014.05.001CrossRefPubMed

9.

Sessa, L., & Bianchi, M. E. (2007). The evolution of high mobility Group Box (HMGB) chromatin proteins in multicellular animals. Gene, 387(1–2), 133–140. https://doi.org/10.1016/j.gene.2006.08.034CrossRefPubMed

10.

Calogero, S., Grassi, F., Aguzzi, A., Voigtländer, T., Ferrier, P., Ferrari, S., & Bianchi, M. E. (1999). The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nature Genetics, 22(3), 276–280. https://doi.org/10.1038/10338CrossRefPubMed

11.

Lee, G., Espirito Santo, A. I., Zwingenberger, S., Cai, L., Vogl, T., Feldmann, M., & Nanchahal, J. (2018). Fully reduced HMGB1 accelerates the regeneration of multiple tissues by transitioning stem cells to GAlert. Proceedings of the National Academy of Sciences, 115(19), E4463-E4472. https://doi.org/10.1073/pnas.1802893115

12.

Bianchi, M. E., & Agresti, A. (2005). HMG proteins: Dynamic players in gene regulation and differentiation. Current Opinion in Genetics & Development, 15(5), 496–506. https://doi.org/10.1016/j.gde.2005.08.007CrossRef

13.

Bianchi, M. E., Falciola, L., Ferrari, S., & Lilley, D. (1992). The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins. The EMBO Journal, 11(3), 1055–1063. https://doi.org/10.1002/j.1460-2075.1992.tb05144.xCrossRefPubMedPubMedCentral

14.

Bonaldi, T., Talamo, F., Scaffidi, P., Ferrera, D., Porto, A., Bachi, A., & Bianchi, M. E. (2003). Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. The EMBO Journal, 22(20), 5551–5560. https://doi.org/10.1093/emboj/cdg516CrossRefPubMedPubMedCentral

15.

Rabadi, M. M., Xavier, S., Vasko, R., Kaur, K., Goligorksy, M. S., & Ratliff, B. B. (2015). High-mobility group box 1 is a novel deacetylation target of Sirtuin1. Kidney International, 87(1), 95–108. https://doi.org/10.1038/ki.2014.217CrossRefPubMed

16.

Oh, Y. J., Youn, J. H., Ji, Y., Lee, S. E., Lim, K. J., Choi, J. E., & Shin, J. S. (2009). HMGB1 is phosphorylated by classical protein kinase C and is secreted by a calcium-dependent mechanism. The Journal of Immunology, 182(9), 5800–5809. https://doi.org/10.4049/jimmunol.0801873CrossRefPubMed

17.

Zhang, X., Wheeler, D., Tang, Y., Guo, L., Shapiro, R. A., Ribar, T. J., & Rosengart, M. R. (2008). Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages. The Journal of Immunology, 181(7), 5015–5023. https://doi.org/10.4049/jimmunol.181.7.5015CrossRefPubMed

18.

Ito, I., Fukazawa, J., & Yoshida, M. (2007). Post-translational methylation of high mobility group box 1 (HMGB1) causes its cytoplasmic localization in neutrophils. Journal of Biological Chemistry, 282(22), 16336–16344. https://doi.org/10.1074/jbc.M608467200CrossRefPubMed

19.

Wang, H., Bloom, O., Zhang, M., Vishnubhakat, J. M., Ombrellino, M., Che, J., & Tracey, K. J. (1999). HMG-1 as a late mediator of endotoxin lethality in mice. Science, 285(5425). https://doi.org/10.1126/science.285.5425.248

20.

Andersson, U., Wang, H., Palmblad, K., Aveberger, A. C., Bloom, O., Erlandsson-Harris, H., & Tracey, K. J. (2000). High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. Journal of Experimental Medicine, 192(4). https://doi.org/10.1084/jem.192.4.565

21.

Wang, H., Vishnubhakat, J. M., Bloom, O., Zhang, M., Ombrellino, M., Sama, A., & Tracey, K. J. (1999). Proinflammatory cytokines (tumor necrosis factor and interleukin 1) stimulate release of high mobility group protein-1 by pituicytes. Surgery, 126(2). https://doi.org/10.1016/S0039-6060(99)70182-0

22.

Sparatore, B., Passalacqua, M., Patrone, M., Melloni, E., & Pontremoli, S. (1996). Extracellular high-mobility group 1 protein is essential for murine erythroleukaemia cell differentiation. Biochemical Journal, 320(1). https://doi.org/10.1042/bj3200253

23.

Scaffidi, P., Misteli, T., & Bianchi, M. E. (2002). Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature, 418(6894). https://doi.org/10.1038/nature00858

24.

Andrassy, M., Volz, H. C., Igwe, J. C., Funke, B., Eichberger, S. N., Kaya, Z., & Bierhaus, A. (2008). High-mobility group box-1 in ischemia-reperfusion injury of the heart. Circulation, 117(25). https://doi.org/10.1161/CIRCULATIONAHA.108.769331

25.

Yang, H., Wang, H., Czura, C. J., & Tracey, K. J. (2005). The cytokine activity of HMGB1. Journal of Leukocyte Biology, 78(1). https://doi.org/10.1189/jlb.1104648

26.

Qin, S., Wang, H., Yuan, R., Li, H., Ochani, M., Ochani, K., & Yang, H. (2006). Role of HMGB1 in apoptosis-mediated sepsis lethality. Journal of Experimental Medicine, 203(7). https://doi.org/10.1084/jem.20052203

27.

Jiang, W., & Pisetsky, D. S. (2007). Mechanisms of disease: The role of high-mobility group protein 1 in the pathogenesis of inflammatory arthritis. Nature Clinical Practice Rheumatology. https://doi.org/10.1038/ncprheum0379CrossRefPubMed

28.

Bell, C. W., Jiang, W., Reich, C. F., & Pisetsky, D. S. (2006). The extracellular release of HMGB1 during apoptotic cell death. American Journal of Physiology - Cell Physiology, 291(6). https://doi.org/10.1152/ajpcell.00616.2005

29.

Bianchi, M. E. (2007). DAMPs, PAMPs and alarmins: All we need to know about danger. Journal of Leucocyte Biology, 81(1), 1–5. https://doi.org/10.1189/jlb.0306164CrossRef

30.

Creagh, E. M., & O’Neill, L. A. (2006). TLRs, NLRs and RLRs: A trinity of pathogen sensors that co-operate in innate immunity. Trends in Immunology, 27(8), 352–357. https://doi.org/10.1016/j.it.2006.06.003CrossRefPubMed

31.

Vénéreau, E., Ceriotti, C., & Bianchi, M. E. (2015). DAMPs from cell death to new life. Frontiers in Immunology, 6, 422. https://doi.org/10.3389/fimmu.2015.00422CrossRefPubMedPubMedCentral

32.

Vénéreau, E., Ceriotti, C., & Bianchi, M. E. (2015). DAMPs from cell death to new life. Frontiers in Immunology, 6, 422. https://doi.org/10.1371/journal.pbio.1001086CrossRefPubMedPubMedCentral

33.

Liu, Y., Prasad, R., & Wilson, S. H. (2010). HMGB1: Roles in base excision repair and related function. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1799(1–2), 119–130. https://doi.org/10.1016/j.bbagrm.2009.11.008CrossRefPubMed

34.

Rovere-Querini, P., Capobianco, A., Scaffidi, P., Valentinis, B., Catalanotti, F., Giazzon, M., & Manfredi, A. A. (2004). HMGB1 is an endogenous immune adjuvant released by necrotic cells. EMBO Reports, 5(8), 825–830. https://doi.org/10.1038/sj.embor.7400205CrossRefPubMedPubMedCentral

35.

Scaffidi, P., Misteli, T., & Bianchi, M. E. (2002). Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature, 418(6894), 191–195. https://doi.org/10.1038/nature00858CrossRefPubMed

36.

Gardella, S., Andrei, C., Ferrera, D., Lotti, L. V., Torrisi, M. R., Bianchi, M. E., & Rubartelli, A. (2002). The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Reports, 3(10), 995–1001. https://doi.org/10.1093/embo-reports/kvf198CrossRefPubMedPubMedCentral

37.

Wang, H., Bloom, O., Zhang, M., Vishnubhakat, J. M., Ombrellino, M., Che, J., & Tracey, K. J. (1999). HMGB-1 as a late mediator of endotoxin lethality in mice. Science, 285(5425), 248–251. https://doi.org/10.1126/science.285.5425.248CrossRefPubMed

38.

Nyström, S., Antoine, D. J., Lundbäck, P., Lock, J. G., Nita, A. F., Högstrand, K., & Applequist, S. E. (2013). TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. The EMBO Journal, 32(1), 86–99. https://doi.org/10.1038/nature11290CrossRefPubMed

39.

Nyström, S., Antoine, D. J., Lundbäck, P., Lock, J. G., Nita, A. F., Högstrand, K., & Applequist, S. E. (2013). TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. The EMBO Journal, 32(1), 86–99. https://doi.org/10.1189/jlb.0713412CrossRefPubMed

40.

Andrassy, M., Volz, H. C., Igwe, J. C., Funke, B., Eichberger, S. N., Kaya, Z., & Bierhaus, A. (2008). High-mobility group box-1 in ischemia-reperfusion injury of the heart. Circulation, 117(25), 3216–3226. https://doi.org/10.1161/CIRCULATIONAHA.108.769331CrossRefPubMed

41.

Andrassy, M., Volz, H. C., Igwe, J. C., Funke, B., Eichberger, S. N., Kaya, Z., & Bierhaus, A. (2008). High-mobility group box-1 in ischemia-reperfusion injury of the heart. Circulation, 117(25), 3216–3226. https://doi.org/10.1084/jem.20042614CrossRefPubMed

42.

Wang, W. K., Lu, Q. H., Zhang, J. N., Wang, B., Liu, X. J., An, F. S., & Zhang, M. X. (2014). HMGB 1 mediates hyperglycaemia-induced cardiomyocyte apoptosis via ERK/Ets‐1 signalling pathway. Journal of Cellular and Molecular Medicine, 18(11), 2311–2320. https://doi.org/10.1111/jcmm.12399CrossRefPubMedPubMedCentral

43.

Ulloa, L., Batliwalla, F. M., Andersson, U., Gregersen, P. K., & Tracey, K. J. (2003). High mobility group box chromosomal protein 1 as a nuclear protein, cytokine, and potential therapeutic target in arthritis. Arthritis & Rheumatism: Official Journal of the American College of Rheumatology, 48(4), 876–881. https://doi.org/10.1002/art.10854CrossRef

44.

Maroso, M., Balosso, S., Ravizza, T., Liu, J., Aronica, E., Iyer, A. M., & Vezzani, A. (2010). Toll-like receptor 4 and high-mobility group box-1 are involved in ictogenesis and can be targeted to reduce seizures. Nature Medicine, 16(4), 413–419. https://doi.org/10.1038/nm.2127CrossRefPubMed

45.

Venereau, E., De Leo, F., Mezzapelle, R., Careccia, G., Musco, G., & Bianchi, M. E. (2016). HMGB1 as biomarker and drug target. Pharmacological Research, 111, 534–544. https://doi.org/10.1016/j.phrs.2016.06.031CrossRefPubMed

46.

Straino, S., Di Carlo, A., Mangoni, A., De Mori, R., Guerra, L., Maurelli, R., & Germani, A. (2008). High-mobility group box 1 protein in human and murine skin: Involvement in wound healing. Journal of Investigative Dermatology, 128(6), 1545–1553. https://doi.org/10.1038/sj.jid.5701212CrossRefPubMed

47.

Chavakis, E., Hain, A., Vinci, M., Carmona, G., Bianchi, M. E., Vajkoczy, P., & Dimmeler, S. (2007). High-mobility group box 1 activates integrin-dependent homing of endothelial progenitor cells. Circulation Research, 100(2), 204–212. https://doi.org/10.1161/01.RES.0000257774.55970.f4CrossRefPubMed

48.

Moshensky, A., Brand, C. S., Alhaddad, H., Shin, J., Masso-Silva, J. A., Advani, I., & Crotty Alexander, L. E. (2022). Effects of mango and mint pod-based e-cigarette aerosol inhalation on inflammatory states of the brain, lung, heart, and colon in mice. eLife, 11. https://doi.org/10.7554/eLife.67621

49.

Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J., Cattaneo, A., De Marchis, F., & Bianchi, M. E. (2012). Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. Journal of Experimental Medicine, 209(9), 1519–1528. https://doi.org/10.1084/jem.20120189CrossRefPubMedPubMedCentral

50.

Tirone, M., Tran, N. L., Ceriotti, C., Gorzanelli, A., Canepari, M., Bottinelli, R., & Vénéreau, E. (2018). High mobility group box 1 orchestrates tissue regeneration via CXCR4. Journal of Experimental Medicine, 215(1), 303–318. https://doi.org/10.1084/jem.20160217CrossRefPubMedPubMedCentral

51.

Maugeri, N., Rovere-Querini, P., Baldini, M., Baldissera, E., Sabbadini, M. G., Bianchi, M. E., & Manfredi, A. A. (2014). Oxidative stress elicits platelet/leukocyte inflammatory interactions via HMGB1: A candidate for microvessel injury in sytemic sclerosis. Antioxidants & Redox Signaling, 20(7), 1060–1074. https://doi.org/10.1089/ars.2013.5298CrossRef

52.

Tsung, A., Tohme, S., & Billiar, T. R. (2014). High-mobility group box‐1 in sterile inflammation. Journal of Internal Medicine, 276(5), 425–443. https://doi.org/10.1111/joim.12276CrossRefPubMed

53.

Fritz, G. (2011). RAGE: A single receptor fits multiple ligands. Trends in Biochemical Sciences, 36(12), 625–632. https://doi.org/10.1016/j.tibs.2011.08.008CrossRefPubMed

54.

Sessa, L., Gatti, E., Zeni, F., Antonelli, A., Catucci, A., Koch, M., & Bianchi, M. E. (2014). The receptor for advanced glycation end-products (RAGE) is only present in mammals, and belongs to a family of cell adhesion molecules (CAMs). PloS One, 9(1), e86903. https://doi.org/10.1371/journal.pone.0086903CrossRefPubMedPubMedCentral

55.

Kierdorf, K., & Fritz, G. (2013). RAGE regulation and signaling in inflammation and beyond. Journal of Leukocyte Biology, 94(1), 55–68. https://doi.org/10.1189/jlb.1012519CrossRefPubMed

56.

Orlova, V. V., Choi, E. Y., Xie, C., Chavakis, E., Bierhaus, A., Ihanus, E., & Chavakis, T. (2007). A novel pathway of HMGB1-mediated inflammatory cell recruitment that requires Mac‐1‐integrin. The EMBO Journal, 26(4), 1129–1139. https://doi.org/10.1038/sj.emboj.7601552CrossRefPubMedPubMedCentral

57.

Penzo, M., Molteni, R., Suda, T., Samaniego, S., Raucci, A., Habiel, D. M., & Marcu, K. B. (2010). Inhibitor of NF-κB kinases α and β are both essential for high mobility group box 1-mediated chemotaxis. The Journal of Immunology, 184(8), 4497–4509. https://doi.org/10.4049/jimmunol.0903131CrossRefPubMed

58.

Raucci, A., Cugusi, S., Antonelli, A., Barabino, S. M., Monti, L., Bierhaus, A., & Bianchi, M. E. (2008). A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). The FASEB Journal, 22(10), 3716–3727. https://doi.org/10.1096/fj.08-109033CrossRefPubMed

59.

Stark, K., Philippi, V., Stockhausen, S., Busse, J., Antonelli, A., Miller, M., & Massberg, S. (2016). Disulfide HMGB1 derived from platelets coordinates venous thrombosis in mice. Blood the Journal of the American Society of Hematology, 128(20), 2435–2449. https://doi.org/10.1182/blood-2016-04-710632CrossRef

60.

Park, J. S., Svetkauskaite, D., He, Q., Kim, J. Y., Strassheim, D., Ishizaka, A., & Abraham, E. (2004). Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein. Journal of Biological Chemistry, 279(9), 7370–7377. https://doi.org/10.1074/jbc.M306793200CrossRefPubMed

61.

Leifer, C. A., & Medvedev, A. E. (2016). Molecular mechanisms of regulation of toll-like receptor signaling. Journal of Leucocyte Biology, 100(5), 927–941. https://doi.org/10.1189/jlb.2MR0316-117RRCrossRef

62.

Conti, L., Lanzardo, S., Arigoni, M., Antonazzo, R., Radaelli, E., Cantarella, D., & Cavallo, F. (2013). The noninflammatory role of high mobility group box 1/toll-like receptor 2 axis in the self‐renewal of mammary cancer stem cells. The FASEB Journal, 27(12), 4731–4744. https://doi.org/10.1096/fj.13-230201CrossRefPubMed

63.

Qiu, Y., Yang, J., Wang, W., Zhao, W., Peng, F., Xiang, Y., & Feng, J. (2014). HMGB1-promoted and TLR2/4-dependent NK cell maturation and activation take part in rotavirus-induced murine biliary atresia. PLoS Pathogens, 10(3), e1004011. https://doi.org/10.1371/journal.ppat.1004011CrossRefPubMedPubMedCentral

64.

Urbonaviciute, V., Fürnrohr, B. G., Meister, S., Munoz, L., Heyder, P., De Marchis, F., & Voll, R. E. (2008). Induction of inflammatory and immune responses by HMGB1–nucleosome complexes: Implications for the pathogenesis of SLE. The Journal of Experimental Medicine, 205(13), 3007–3018. https://doi.org/10.1084/jem.20081165CrossRefPubMedPubMedCentral

65.

Herzog, C., Lorenz, A., Gillmann, H. J., Chowdhury, A., Larmann, J., Harendza, T., & Theilmeier, G. (2014). Thrombomodulin’s lectin-like domain reduces myocardial damage by interfering with HMGB1-mediated TLR2 signalling. Cardiovascular Research, 101(3), 400–410. https://doi.org/10.1093/cvr/cvt275CrossRefPubMed

66.

Mersmann, J., Iskandar, F., Latsch, K., Habeck, K., Sprunck, V., Zimmermann, R., …Koch, A. (2013). Attenuation of myocardial injury by HMGB1 blockade during ischemia/reperfusion is toll-like receptor 2-dependent. Mediators of inflammation, 2013. https://doi.org/10.1155/2013/174168.

67.

Mittal, D., Saccheri, F., Vénéreau, E., Pusterla, T., Bianchi, M. E., & Rescigno, M. (2010). TLR4-mediated skin carcinogenesis is dependent on immune and radioresistant cells. The EMBO Journal, 29(13), 2242–2252. https://doi.org/10.1038/emboj.2010.94CrossRefPubMedPubMedCentral

68.

Yang, Z., Deng, Y., Su, D., Tian, J., Gao, Y., He, Z., & Wang, X. (2013). TLR4 as receptor for HMGB1-mediated acute lung injury after liver ischemia/reperfusion injury. Laboratory Investigation, 93(7), 792–800. https://doi.org/10.1038/labinvest.2013.66CrossRefPubMed

69.

Yao, Y., Xu, X., Zhang, G., Zhang, Y., Qian, W., & Rui, T. (2012). Role of HMGB1 in doxorubicin-induced myocardial apoptosis and its regulation pathway. Basic Research in Cardiology, 107, 1–12. https://doi.org/10.1007/s00395-012-0267-3CrossRef

70.

Yang, H., Wang, H., Ju, Z., Ragab, A. A., Lundbäck, P., Long, W., Valdes-Ferrer, S. I., He, M., Pribis, J. P., Li, J., & Lu, B. (2015). MD-2 is required for disulfide HMGB1–dependent TLR4 signaling. Journal of Experimental Medicine, 212(1), 5–14. https://doi.org/10.1084/jem.20141318CrossRefPubMedPubMedCentral

71.

He, M., Bianchi, M. E., Coleman, T. R., Tracey, K. J., & Al-Abed, Y. (2018). Exploring the biological functional mechanism of the HMGB1/TLR4/MD-2 complex by surface plasmon resonance. Molecular Medicine, 24(1), 1–9. https://doi.org/10.1186/s10020-018-0023-8CrossRef

72.

Kim, S., Kim, S. Y., Pribis, J. P., Lotze, M., Mollen, K. P., Shapiro, R., Loughran, P., Scott, M. J., & Billiar, T. R. (2013). Signaling of high mobility group box 1 (HMGB1) through toll-like receptor 4 in macrophages requires CD14. Molecular Medicine, 19, 88–98. https://doi.org/10.2119/molmed.2012.00306CrossRefPubMedPubMedCentral

73.

Campana, L., Bosurgi, L., Bianchi, M. E., Manfredi, A. A., & Rovere–Querini, P. (2009). Requirement of HMGB1 for stromal cell–derived factor–1/CXCL12–dependent migration of macrophages and dendritic cells. Journal of Leukocyte Biology, 86(3), 609–615. https://doi.org/10.1189/jlb.0908576CrossRefPubMed

74.

Di Maggio, S., Milano, G., De Marchis, F., D’Ambrosio, A., Bertolotti, M., Palacios, B. S., Badi, I., Sommariva, E., Pompilio, G., Capogrossi, M. C., & Raucci, A. (2017). Non-oxidizable HMGB1 induces cardiac fibroblasts migration via CXCR4 in a CXCL12-independent manner and worsens tissue remodeling after myocardial infarction. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1863(11), 2693–2704. https://doi.org/10.1016/j.bbadis.2017.07.012CrossRefPubMed

75.

Gazzar, M., El, Yoza, B. K., Chen, X., Garcia, B. A., Young, N. L., & McCall, C. E. (2009). Chromatin-specific remodeling by HMGB1 and linker histone H1 silences proinflammatory genes during endotoxin tolerance. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.01862-08CrossRefPubMedPubMedCentral

76.

Chen, R., Zhu, S., Fan, X. G., Wang, H., Lotze, M. T., Zeh, H. J., & Tang, D. (2018). High mobility group protein B1 controls liver cancer initiation through yes-associated protein -dependent aerobic glycolysis. Hepatology, 67(5). https://doi.org/10.1002/hep.29663

77.

DeBerardinis, R. J., & Chandel, N. S. (2020). We need to talk about the Warburg effect. Nature Metabolism. https://doi.org/10.1038/s42255-020-0172-2CrossRefPubMedPubMedCentral

78.

Tang, D., Kang, R., Livesey, K. M., Kroemer, G., Billiar, T. R., Van Houten, B., Zeh, H. J., & Lotze, M. T. (2011). High-mobility group box 1 is essential for mitochondrial quality control. Cell Metabolism. https://doi.org/10.1016/j.cmet.2011.04.008CrossRefPubMedPubMedCentral

79.

Wahid, A., Chen, W., Wang, X., & Tang, X. (2021). High-mobility group box 1 serves as an inflammation driver of cardiovascular disease. Biomedicine & Pharmacotherapy, 1(139), 111555.CrossRef

80.

Saxton, A., Chaudhry, R., & Manna, B. S. P. (2023). Anatomy, thorax, heart right coronary arteries. StatPearls Publishing.

81.

Carter, Y. M., Wehrle, C. J., & Mahajan, K. (2023). Anatomy, thorax, heart anomalous left coronary artery. StatPearls Publishing.

82.

Hussain, A., & Burns, B. (2023). Anatomy, thorax, wall. StatPearls Publishing.

83.

Saxton, A., Tariq, M. A., & Bordoni, B. (2023). Anatomy, thorax, cardiac muscle. StatPearls Publishing.

84.

Tucker, W. D., Weber, C., & Burns, B. (2023). Anatomy, thorax, heart pulmonary arteries. StatPearls Publishing.

85.

Ogobuiro, I., Wehrle, C. J., & Tuma, F. (2023). Anatomy, thorax, heart coronary arteries. StatPearls Publishing.

86.

Capobianco, S. M., Fahmy, M. W., & Sicari, V. (2023). Anatomy, thorax, subclavian veins. StatPearls Publishing.

87.

Oliver, K. A., & Ashurst, J. V. (2023). Anatomy, thorax, phrenic nerves. StatPearls Publishing.

88.

Mathew, P., & Bordoni, B. (2023). Embryology, heart. StatPearls Publishing.

89.

Mori, S., Tretter, J. T., Spicer, D. E., Bolender, D. L., & Anderson, R. H. (2019). What is the real cardiac anatomy? Clinical Anatomy, 32(3), 288–309.CrossRefPubMed

90.

Larson, W. J. (1997). Human embryology. Churchill Livingstone.

91.

Moore, K. L., & Dalley, A. F. (1999). Clinically oriented anatomy. Lippincott, Williams, and Wilkins.

92.

Netter, F. H. (2003). Atlas of Human Anatomy. ICON Learning Systems.

93.

Stedman, T. (1972). Stedman’s medical dictionary. Williams and Wilkins.

94.

Brown, J. C., Gerhardt, T. E., & Kwon, E. (2023). Risk factors for coronary artery disease. StatPearls Publishing.

95.

Bauersachs, R., Zeymer, U., Brière, J. B., Marre, C., Bowrin, K., & Huelsebeck, M. (2019). Cardiovascular Therapy, 2019, 8295054.CrossRef

96.

Adams, H. P., & Biller, J. (1988). Hemorrhagic intracranial vascular disease. Clinical Neurology, 2(16), 1–64.

97.

Bamford, J. M., & Warlow, C. P. (1988). Evolution and testing of the lacunar hypothesis. Stroke, 19, 1074–1082.CrossRefPubMed

98.

Aysert, P., Özdil, T., Dizbay, M., Güzel, Ö., & Hızel, K. (2018). Peripheral arterial disease increases the risk of multidrug-resistant bacteria and amputation in diabetic foot infections. Turkish Journal of Medical Sciences, 48(4), 845–850.CrossRef

99.

Yuksel, A., Velioglu, Y., Cayir, M. C., Kumtepe, G., & Gurbuz, O. (2018). Current status of arterial revascularization for the treatment of critical limb ischemia in Infrainguinal atherosclerotic disease. International Journal of Angiology, 27(3), 132–137.CrossRef

100.

Michos, E. D., Rice, K. M., & Szklo, M. (2009). Factors associated with low levels of subclinical vascular disease in older adults: Multi-ethnic study of atherosclerosis. Preventive Cardiology, 12, 72–79.CrossRefPubMed

101.

Ding, H. S., Yang, J., Chen, P., Yang, J., Bo, S. Q., Ding, J. W., & Yu, Q. Q. (2013). The HMGB1–TLR4 axis contributes to myocardial ischemia/reperfusion injury via regulation of cardiomyocyte apoptosis. Gene, 527(1), 389–393.CrossRefPubMed

102.

Aneja, R. K., Alcamo, A. M., Cummings, J., Vagni, V., Feldman, K., Wang, Q., Dixon, C. E., Billiar, T. R., & Kochanek, P. M. (2019). Lack of benefit on brain edema, blood–brain barrier permeability, or cognitive outcome in global inducible high mobility group box 1 knockout mice despite tissue sparing after experimental traumatic brain injury. Journal of Neurotrauma, 36(2), 360–369. https://doi.org/10.1089/neu.2018.5664CrossRefPubMed

103.

Aneja, R. K., Alcamo, A. M., Cummings, J., Vagni, V., Feldman, K., Wang, Q., Dixon, C. E., Billiar, T. R., & Kochanek, P. M. (2014). High-mobility group box 1 is dispensable for autophagy, mitochondrial quality control, and organ function in vivo. Cell Metabolism, 19(3), 539–547. https://doi.org/10.1016/j.cmet.2014.01.014CrossRef

104.

Kitahara, T., Takeishi, Y., Harada, M., Niizeki, T., Suzuki, S., Sasaki, T., Ishino, M., Bilim, O., Nakajima, O., & Kubota, I. (2008). High-mobility group box 1 restores cardiac function after myocardial infarction in transgenic mice. Cardiovascular Research, 80(1), 40–46. https://doi.org/10.1093/cvr/cvn163CrossRefPubMed

105.

Vaswani, A., Khaw, H. J., El-Medany, A., & Dougherty, S. (2022). Cardiology in a Heartbeat (p. 8). Scion Publishing Ltd.

106.

Paoletti, R., Gotto Jr, A. M., & Hajjar, D. P. (2004). Inflammation in atherosclerosis and implications for therapy. Circulation, 109(23_suppl_1), III–20. https://doi.org/10.1161/01.CIR.0000131514.71167.2eCrossRef

107.

Kalinina, N., Agrotis, A., Antropova, Y., DiVitto, G., Kanellakis, P., Kostolias, G., Ilyinskaya, O., Tararak, E., & Bobik, A. (2004). Increased expression of the DNA-binding cytokine HMGB1 in human atherosclerotic lesions: role of activated macrophages and cytokines. Arteriosclerosis, Thrombosis, and Vascular Biology, 24(12), 2320–2325. https://doi.org/10.1161/01.ATV.0000145573.36113.8aCrossRefPubMed

108.

Porto, A., Palumbo, R., Pieroni, M., Aprigliano, G., Chiesa, R., Sanvito, F., Maseri, A., Bianchi, M. E., Porto, A., Palumbo, R., & Pieroni, M. (2006). Smooth muscle cells in human atherosclerotic plaques secrete and proliferate in response to high mobility group box 1 protein. The FASEB Journal, 20(14), 2565–2566. https://doi.org/10.1096/fj.06-5867fjeCrossRefPubMed

109.

Inoue, K., Kawahara, K. I., Biswas, K. K., Ando, K., Mitsudo, K., Nobuyoshi, M., & Maruyama, I. (2007). HMGB1 expression by activated vascular smooth muscle cells in advanced human atherosclerosis plaques. Cardiovascular Pathology, 16(3), 136–143. https://doi.org/10.1016/j.carpath.2006.11.006CrossRefPubMed

110.

Kanellakis, P., Agrotis, A., Kyaw, T. S., Koulis, C., Ahrens, I., Mori, S., Takahashi, H. K., Liu, K., Peter, K., Nishibori, M., & Bobik, A. (2011). High-mobility group box protein 1 neutralization reduces development of diet-induced atherosclerosis in apolipoprotein E–deficient mice. Arteriosclerosis, Thrombosis, and Vascular Biology, 31(2), 313–319. https://doi.org/10.1161/ATVBAHA.110.218669CrossRefPubMed

111.

Andrassy, M., Volz, H. C., Schuessler, A., Gitsioudis, G., Hofmann, N., Laohachewin, D., Wienbrandt, A. R., Kaya, Z., Bierhaus, A., Giannitsis, E., & Katus, H. A. (2012). HMGB1 is associated with atherosclerotic plaque composition and burden in patients with stable coronary artery disease. PloS One, 7(12), e52081. https://doi.org/10.1371/journal.pone.0052081CrossRefPubMedPubMedCentral

112.

Hu, X., Jiang, H., Bai, Q., Zhou, X., Xu, C., Lu, Z., Cui, B., & Wen, H. (2009). Increased serum HMGB1 is related to the severity of coronary artery stenosis. Clinica Chimica Acta, 406(1–2), 139–142. https://doi.org/10.1016/j.cca.2009.06.016CrossRef

113.

Bagheri, B., Meshkini, F., Dinarvand, K., Alikhani, Z., Haysom, M., & Rasouli, M. (2016). International Journal of Preventive Medicine. https://doi.org/10.4103/2008-7802.190598CrossRefPubMedPubMedCentral

114.

Tang, Y. L., Jiang, J. H., Wang, S., Liu, Z., Tang, X. Q., Peng, J., Yang, Y. Z., & Gu, H. F. (2015). TLR4/NF-κ B signaling contributes to chronic unpredictable mild stress-induced atherosclerosis in ApoE-/-mice. PloS One https://doi.org/10.1371/journal.pone.0123685CrossRefPubMedPubMedCentral

115.

Yang, G., Lei, Y., Inoue, A., Piao, L., Hu, L., Jiang, H., Sasaki, T., Wu, H., Xu, W., Yu, C., & Zhao, G. (2017). Exenatide mitigated diet-induced vascular aging and atherosclerotic plaque growth in ApoE-deficient mice under chronic stress. Atherosclerosis, 264, 1–10. https://doi.org/10.1016/j.atherosclerosis.2017.07.014CrossRefPubMed

116.

Wang, B., Lian, Y. J., Su, W. J., Peng, W., Dong, X., Liu, L. L., Gong, H., Zhang, T., Jiang, C. L., & Wang, Y. X. (2018). HMGB1 mediates depressive behavior induced by chronic stress through activating the kynurenine pathway. Brain, Behavior, and Immunity, 72, 51–60. https://doi.org/10.1016/j.bbi.2017.11.017CrossRefPubMed

117.

Lake, N. J., Taylor, R. L., Trahair, H., Harikrishnan, K. N., Curran, J. E., Almeida, M., Kulkarni, H., Mukhamedova, N., Hoang, A., Low, H., & Murphy, A. J. (2017). TRAK2, a novel regulator of ABCA1 expression, cholesterol efflux and HDL biogenesis. European Heart Journal, 38(48), 3579–3587. https://doi.org/10.1093/eurheartj/ehx315CrossRefPubMedPubMedCentral

118.

Chawla, A., Boisvert, W. A., Lee, C. H., Laffitte, B. A., Barak, Y., Joseph, S. B., Liao, D., Nagy, L., Edwards, P. A., Curtiss, L. K., & Evans, R. M. (2001). A PPARγ-LXR-ABCA1 pathway in macrophages is involved in cholesterol efflux and atherogenesis. Molecular Cell, 7(1), 161–171. https://doi.org/10.1016/S1097-2765(01)00164-2CrossRefPubMed

119.

Gu, H. F., Li, N., Xu, Z. Q., Hu, L., Li, H., Zhang, R. J., Chen, R. M., Zheng, X. L., Tang, Y. L., & Liao, D. F. (2019). Chronic unpredictable mild stress promotes atherosclerosis via HMGB1/TLR4-mediated downregulation of PPARγ/LXRα/ABCA1 in ApoE-/-Mice. Frontiers in Physiology, 10, 165. https://doi.org/10.3389/fphys.2019.00165CrossRefPubMedPubMedCentral

120.

Kang, R., Zhang, Q., Zeh, I. I. I., Lotze, H. J., M. T., & Tang, D. (2013). HMGB1 in cancer: Good, bad, or both? Clinical cancer Research, 19(15), 4046–4057. https://doi.org/10.1158/1078-0432.CCR-13-0495CrossRefPubMedPubMedCentral

121.

Gangemi, S., Casciaro, M., Trapani, G., Quartuccio, S., Navarra, M., Pioggia, G., & Imbalzano, E. (2015). Mediators of Inflammation. https://doi.org/10.1155/2015/164913CrossRefPubMedPubMedCentral

122.

Schiraldi, M., Raucci, A., Muñoz, L. M., Livoti, E., Celona, B., Venereau, E., Apuzzo, T., De Marchis, F., Pedotti, M., Bachi, A., & Thelen, M. (2012). HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4. Journal of Experimental Medicine, 209(3), 551–563. https://doi.org/10.1084/jem.20111739CrossRefPubMedPubMedCentral

123.

Andrassy, M., Volz, H. C., Riedle, N., Gitsioudis, G., Seidel, C., Laohachewin, D., Zankl, A. R., Kaya, Z., Bierhaus, A., Giannitsis, E., & Katus, H. A. (2011). HMGB1 as a predictor of infarct transmurality and functional recovery in patients with myocardial infarction. Journal of Internal Medicine, 270(3), 245–253. https://doi.org/10.1111/j.1365-2796.2011.02369.xCrossRefPubMed

124.

Cirillo, P., Giallauria, F., Pacileo, M., Petrillo, G., D’agostino, M., Vigorito, C., & Chiariello, M. (2009). Increased high mobility group box-1 protein levels are associated with impaired cardiopulmonary and echocardiographic findings after acute myocardial infarction. Journal of Cardiac Failure, 15(4), 362–367. https://doi.org/10.1016/j.cardfail.2008.11.010CrossRefPubMed

125.

Giallauria, F., Cirillo, P., Lucci, R., Pacileo, M., D’Agostino, M., Maietta, P., Vitelli, A., Chiariello, M., & Vigorito, C. (2010). Autonomic dysfunction is associated with high mobility group box-1 levels in patients after acute myocardial infarction. Atherosclerosis, 208(1), 280–284. https://doi.org/10.1016/j.atherosclerosis.2009.07.025CrossRefPubMed

126.

Goldstein, R. S., Gallowitsch-Puerta, M., Yang, L., Rosas-Ballina, M., Huston, J. M., Czura, C. J., Lee, D. C., Ward, M. F., Bruchfeld, A. N., Wang, H., & Lesser, M. L. (2006). Elevated high-mobility group box 1 levels in patients with cerebral and myocardial ischemia. Shock, 25(6), 571–574. https://doi.org/10.1097/01.shk.0000209540.99176.72CrossRefPubMed

127.

Hashimoto, T., Ishii, J., Kitagawa, F., Yamada, S., Hattori, K., Okumura, M., Naruse, H., Motoyama, S., Matsui, S., Tanaka, I., & Izawa, H. (2012). Circulating high-mobility group box 1 and cardiovascular mortality in unstable angina and non-ST-segment elevation myocardial infarction. Atherosclerosis, 221(2), 490–495. https://doi.org/10.1016/j.atherosclerosis.2012.01.040CrossRefPubMed

128.

Kohno, T., Anzai, T., Naito, K., Miyasho, T., Okamoto, M., Yokota, H., Yamada, S., Maekawa, Y., Takahashi, T., Yoshikawa, T., & Ishizaka, A. (2009). Role of high-mobility group box 1 protein in post-infarction healing process and left ventricular remodelling. Cardiovascular Research, 81(3), 565–573. https://doi.org/10.1093/cvr/cvn291CrossRefPubMed

129.

Kohno, T., Anzai, T., Naito, K., Miyasho, T., Okamoto, M., Yokota, H., Yamada, S., Maekawa, Y., Takahashi, T., Yoshikawa, T., & Ishizaka, A. (2009). Role of high-mobility group box 1 protein in post-infarction healing process and left ventricular remodelling. Cardiovascular Research, 81(3), 565–573. https://doi.org/10.1161/01.RES.0000186276.06104.04CrossRefPubMed

130.

Sørensen, M. V., Pedersen, S., Møgelvang, R., Skov-Jensen, J., & Flyvbjerg, A. (2011). Plasma high-mobility group box 1 levels predict mortality after ST-segment elevation myocardial infarction. JACC: Cardiovascular Interventions, 4(3), 281–286. https://doi.org/10.1016/j.jcin.2010.10.015CrossRefPubMed

131.

Sadamura-Takenaka, Y., Ito, T., Noma, S., Oyama, Y., Yamada, S., Kawahara, K. I., Inoue, H., & Maruyama, I. (2014). HMGB1 promotes the development of pulmonary arterial hypertension in rats. PloS One https://doi.org/10.1371/journal.pone.0102482CrossRefPubMedPubMedCentral

132.

Bauer, E. M., Shapiro, R., Zheng, H., Ahmad, F., Ishizawar, D., Comhair, S. A., Erzurum, S. C., Billiar, T. R., & Bauer, P. M. (2012). High mobility group box 1 contributes to the pathogenesis of experimental pulmonary hypertension via activation of Toll-like receptor 4. Molecular Medicine, 18, 1509–1518. https://doi.org/10.2119/molmed.2012.00283CrossRefPubMedCentral

133.

Li, W. J., Hu, K., Yang, J. P., Xu, X. Y., Li, N., Wen, Z. P., & Wang, H. (2017). HMGB1 affects the development of pulmonary arterial hypertension via RAGE. European Review for Medical & Pharmacological Sciences, 21(17), 3950–3958.

134.

Huang, Y. Y., Su, W., Zhu, Z. W., Tang, L., Hu, X. Q., Zhou, S. H., Fang, Z. F., & Li, J. (2016). Elevated serum HMGB1 in pulmonary arterial hypertension secondary to congenital heart disease. Vascular Pharmacology, 85, 66–72. https://doi.org/10.1016/j.vph.2016.08.009CrossRefPubMed

135.

Huang, Y. Y., Su, W., Zhu, Z. W., Tang, L., Hu, X. Q., Zhou, S. H., Fang, Z. F., & Li, J. (2016). Elevated serum HMGB1 in pulmonary arterial hypertension secondary to congenital heart disease. Vascular Pharmacology, 85, 66–72. https://doi.org/10.4414/smw.2015.14202CrossRefPubMed

136.

Wang, J., Tian, X. T., Peng, Z., Li, W. Q., Cao, Y. Y., Li, Y., & Li, X. H. (2019). HMGB1/TLR4 promotes hypoxic pulmonary hypertension via suppressing BMPR2 signaling. Vascular Pharmacology, 117, 35–44. https://doi.org/10.1016/j.vph.2018.12.006CrossRefPubMed

137.

Wang, J., Tian, X. T., Peng, Z., Li, W. Q., Cao, Y. Y., Li, Y., & Li, X. H. (2019). HMGB1/TLR4 promotes hypoxic pulmonary hypertension via suppressing BMPR2 signaling. Vascular Pharmacology, 117, 35–44. https://doi.org/10.1016/j.yexcr.2015.05.011CrossRefPubMed

138.

Lucena, J. S., Garamendi, P. M., Guzzo-Merello, G., & García-Pavía, P. (2014). Cardiovascular pathology secondary to alcohol consumption, drugs of abuse and medication. Clinico-pathological atlas of cardiovascular diseases (pp. 299–316). Springer. https://doi.org/10.1007/978-3-319-11146-9_8CrossRef

139.

Arbustini, E., Giuliani, L., Di Toro, A., & Favalli, V. (2018). Inherited cardiac muscle disease: Dilated cardiomyopathy. Cardiovascular Genetics and Genomics: Principles and Clinical Practice, 319–366. https://doi.org/10.1007/978-3-319-66114-8_10

140.

Lu, B., Antoine, D. J., Kwan, K., Lundbäck, P., Wähämaa, H., Schierbeck, H., Robinson, M., Van Zoelen, M. A., Yang, H., Li, J., & Erlandsson-Harris, H. (2014). JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation. Proceedings of the National Academy of Sciences, 111(8), 3068–3073. https://doi.org/10.1073/pnas.1316925111CrossRef

141.

Narumi, T., Shishido, T., Otaki, Y., Kadowaki, S., Honda, Y., Funayama, A., Honda, S., Hasegawa, H., Kinoshita, D., Yokoyama, M., Nishiyama, S., & Kubota, I. (2015). High-mobility group box 1-mediated heat shock protein beta 1 expression attenuates mitochondrial dysfunction and apoptosis. Journal of Molecular and Cellular Cardiology, 82, 1–12. https://doi.org/10.1016/j.yjmcc.2015.02.018CrossRefPubMed

142.

Volz, H. C., Kaya, Z., Katus, H. A., & Andrassy, M. (2010). The role of HMGB1/RAGE in inflammatory cardiomyopathy. Seminars in Thrombosis and Hemostasis, 36(02), 185–194. https://doi.org/10.1055/s-0030-1251503CrossRefPubMed

143.

Agunbiade, T. A., Zaghlol, R. Y., & Barac, A. (2019). Heart failure in relation to anthracyclines and other chemotherapies. Methodist DeBakey Cardiovascular Journal. https://doi.org/10.1016/j.jacc.2014.06.1167CrossRefPubMedPubMedCentral

144.

Luo, P., Zhu, Y., Chen, M., Yan, H., Yang, B., Yang, X., & He, Q. (2018). HMGB1 contributes to adriamycin-induced cardiotoxicity via up-regulating autophagy. Toxicology Letters, 292, 115–122. https://doi.org/10.1016/j.toxlet.2018.04.034CrossRefPubMed

145.

Volz, H. C., Seidel, C., Laohachewin, D., Kaya, Z., Müller, O. J., Pleger, S. T., Lasitschka, F., Bianchi, M. E., Remppis, A., Bierhaus, A., & Katus, H. A. (2010). HMGB1: The missing link between diabetes mellitus and heart failure. Basic Research in Cardiology, 105, 805–820. https://doi.org/10.1007/s00395-010-0114-3CrossRefPubMed

146.

Wang, W. K., Wang, B., Lu, Q. H., Zhang, W., Qin, W. D., Liu, X. J., Liu, X. Q., An, F. S., Zhang, Y., & Zhang, M. X. (2014). Inhibition of high-mobility group box 1 improves myocardial fibrosis and dysfunction in diabetic cardiomyopathy. International Journal of Cardiology, 172(1), 202–212. https://doi.org/10.1016/j.ijcard.2014.01.011CrossRefPubMed

147.

Song, J., Liu, Q., Tang, H., Tao, A., Wang, H., Kao, R., & Rui, T. (2016). Activation of PI3Kγ/Akt pathway increases cardiomyocyte HMGB1 expression in diabetic environment. Oncotarget, 7(49), 80803. https://doi.org/10.18632/oncotarget.13096CrossRefPubMedPubMedCentral

148.

Wu, H., Sheng, Z. Q., Xie, J., Li, R., Chen, L., Li, G. N., Wang, L., & Xu, B. (2016). Reduced HMGB 1-mediated pathway and oxidative stress in resveratrol-treated diabetic mice: A possible mechanism of cardioprotection of resveratrol in diabetes mellitus. Oxidative Medicine and Cellular Longevity. https://doi.org/10.1155/2016/9836860CrossRefPubMedPubMedCentral

149.

Brozena, S. C., & Jessup, M. (2003). The new staging system for heart failure. What every primary care physician should know. Geriatrics (Basel Switzerland), 58(6), 31–36.

150.

Pfeffer, M. A., Swedberg, K., Granger, C. B., & Failure, H. (2003). Heart failure. The Nurse Practitioner. https://doi.org/10.1016/S0140-6736(05)66621-4CrossRef

151.

De Souza, A. W. S., Westra, J., Limburg, P. C., Bijl, M., & Kallenberg, C. G. M. (2012). HMGB1 in vascular diseases: Its role in vascular inflammation and atherosclerosis. Autoimmunity Reviews, 11(12), 909–917. https://doi.org/10.1016/j.autrev.2012.03.007CrossRefPubMed

152.

Dumitriu, I. E., Baruah, P., Manfredi, A. A., Bianchi, M. E., & Rovere-Querini, P. (2005). HMGB1: Guiding immunity from within. Trends in Immunology, 26(7), 381–387. https://doi.org/10.1016/j.it.2005.04.009CrossRefPubMed

153.

Karuppagounder, V., Giridharan, V. V., Arumugam, S., Sreedhar, R., Palaniyandi, S. S., Krishnamurthy, P., Quevedo, J., Watanabe, K., Konishi, T., & Thandavarayan, R. A. (2016). Modulation of macrophage polarization and HMGB1-TLR2/TLR4 cascade plays a crucial role for cardiac remodeling in senescence-accelerated prone mice. PloS One, 11(4), e0152922.CrossRefPubMedPubMedCentral

154.

Braunwald, E. (2015). The war against heart failure: The Lancet lecture. The Lancet, 385(9970), 812–824. https://doi.org/10.1016/S0140-6736(14)61889-4CrossRef

155.

Takahashi, T., Shishido, T., Kinoshita, D., Watanabe, K., Toshima, T., Sugai, T., Narumi, T., Otaki, Y., Tamura, H., Nishiyama, S., & Arimoto, T. (2019). Cardiac nuclear high-mobility group box 1 ameliorates pathological cardiac hypertrophy by inhibiting DNA damage response. Basic to Translational Science, 4(2), 234–247. https://doi.org/10.1016/j.jacbts.2018.11.011CrossRefPubMedPubMedCentral

156.

Salzano, M., Sanz-García, M., Monsalve, D. M., Moura, D. S., & Lazo, P. A. (2015). VRK1 chromatin kinase phosphorylates H2AX and is required for foci formation induced by DNA damage. Epigenetics, 10(5), 373–383. https://doi.org/10.1038/nrc2523CrossRefPubMedPubMedCentral

157.

Thrasher, P., Singh, M., & Singh, K. (2017). Ataxia-telangiectasia mutated kinase: Role in myocardial remodeling. Journal of Rare Diseases Research & Treatment, 2(1), 32.CrossRef

158.

Kikuchi, K., Tancharoen, S., Ito, T., Morimoto-Yamashita, Y., Miura, N., Kawahara, K. I., Maruyama, I., Murai, Y., & Tanaka, E. (2013). Potential of the angiotensin receptor blockers (ARBs)telmisartan, irbesartan, and candesartan for inhibiting the HMGB1/RAGE axis in prevention and acute treatment of stroke. International Journal of Molecular Sciences, 14(9), 18899–18924. https://doi.org/10.3390/ijms140918899CrossRefPubMedPubMedCentral

159.

Richard, S. A., Jiang, Y., Xiang, L. H., Zhou, S., Wang, J., Su, Z., & Xu, H. (2017). Post-translational modifications of high mobility group box 1 and cancer. American Journal of Translational Research, 9(12), 5181. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5752874/PubMedPubMedCentral

160.

Tang, Y., Zhao, X., Antoine, D., Xiao, X., Wang, H., Andersson, U., Billiar, T. R., Tracey, K. J., & Lu, B. (2016). Regulation of posttranslational modifications of HMGB1 during immune responses. Antioxidants & Redox Signaling, 24(12), 620–634. https://doi.org/10.1089/ars.2015.6409CrossRef

161.

Jia, Z., Xue, R., Liu, G., Li, L., Yang, J., Pi, G., Ma, S., & Kan, Q. (2014). Involved in the protective effect of the PPARα agonist fenofibrate against cardiac hypertrophy. Ppar Research. https://doi.org/10.1155/2014/541394CrossRefPubMedPubMedCentral

162.

Lin, H., Shen, L., Zhang, X., Xie, J., Hao, H., Zhang, Y., Chen, Z., Yamamoto, H., Liao, W., Bin, J., & Cao, S. (2016). HMGB1-RAGE axis makes no contribution to cardiac remodeling induced by pressure-overload. PLoS One https://doi.org/10.1371/journal.pone.0158514CrossRefPubMedPubMedCentral

163.

Zhang, L., Liu, M., Jiang, H., Yu, Y., Yu, P., Tong, R., Wu, J., Zhang, S., Yao, K., Zou, Y., & Ge, J. (2016). Extracellular high-mobility group box 1 mediates pressure overload-induced cardiac hypertrophy and heart failure. Journal of Cellular and Molecular Medicine, 20(3), 459–470. https://doi.org/10.1111/jcmm.12743CrossRefPubMed

164.

Tian, J., Avalos, A. M., Mao, S. Y., Chen, B., Senthil, K., Wu, H., Parroche, P., Drabic, S., Golenbock, D., Sirois, C., & Hua, J. (2007). Toll-like receptor 9–dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nature Immunology, 8(5), 487–496.CrossRefPubMed

165.

Padimalla, T. M. J. M. T., & Muzaffar, A. (2023). Myocarditis and pericarditis. Innovations in Technology and Science Education, 2(9), 1885–1896. https://doi.org/10.1016/S0140-6736(11)60648-XCrossRef

166.

Comarmond, C., & Cacoub, P. (2017). Myocarditis in auto-immune or auto-inflammatory diseases. Autoimmunity Reviews, 16(8), 811–816. https://doi.org/10.1016/j.autrev.2017.05.021CrossRefPubMed

167.

Bangert, A., Andrassy, M., Müller, A. M., Bockstahler, M., Fischer, A., Volz, C. H., Leib, C., Göser, S., Korkmaz-Icöz, S., Zittrich, S., & Jungmann, A. (2016). Critical role of RAGE and HMGB1 in inflammatory heart disease. Proceedings of the National Academy of Sciences, 113(2), 155–164. https://doi.org/10.1073/pnas.1522288113CrossRef

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Rhein Alleviates Doxorubicin-Induced Myocardial Injury by Inhibiting the p38 MAPK/HSP90/c-Jun/c-Fos Pathway-Mediated Apoptosis

Exosomes from Hypoxic Pretreatment ADSCs Ameliorate Cardiac Damage Post-MI via Activated circ-Stt3b/miR-15a-5p/GPX4 Signaling and Decreased Ferroptosis