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  • Our investigation also showed NAC increased the level

    2022-08-05

    Our investigation also showed NAC increased the level of DAF and might protect HUVECs from complement activation. NAC, an antioxidant/mucous modifier, has displayed benefits in chronic obstructive pulmonary disease. Martinez de Lizarrondo et al [38] provided evidence that the molecular target underlying the thrombolytic effects of NAC is principally VWF that cross-link platelets in arterial thrombi. They also found that NAC did not worsen hemorrhagic stroke outcomes, suggesting that it exerts thrombolytic effects without significantly impairing normal hemostasis. It was reported that NAC inhibits platelet adherence to endothelial cell–anchored d cycloserine soluble ultralarge VWF multimers by reducing their size 39, 40. It has been reported that NAC resulted in a significant increase in the expression of HO-1 mRNA in liver injured by carbon tetrachloride (CCl4) [23]. In our study we found that NAC might enhance DAF expression on the cell surface, which protects endothelial d cycloserine from complement-mediated cytotoxicity. NAC may play a promising role in TA-TMA treatment in the future.
    Acknowledgments Financial disclosure: This work was supported by the National Nature Science Foundation of China (81620108001, 91439112, 91739302, 81270591, and 81670132) and grants from the Jiangsu Province of China (BK20131167 and RC2011105), Jiangsu Provincial Special Program of Social Development (SBE2016740635), Jiangsu Provincial Special Program of Medical Science (BL2012005) and the Priority Academic Program Development of Jiangsu Higher Education Institutions. Conflict of interest statement: There are no conflicts of interest to report. Authorship statement: T.P. and J.Q. contributed equally to this study.
    Introduction During past 40 years, mortality rate caused by cardiovascular diseases (CVD) decreased significantly. Nevertheless, CVDs are still the primary cause of death worldwide. Disruption of myocardial blood supply, caused by atherosclerosis or thromboembolism, leads to ischemia, myocardial infarction (MI), heart failure (HF) and even death [1]. Following MI, phagocytes (neutrophils and monocytes/macrophages) clear the necrotic tissue by removing dead cardiomyocytes and their released content. Hence MI, the prevalent cause of HF [2], is inevitably associated with immune responses, which are involved in cardiac remodeling (changes in size, shape, structure and function), as well as maintenance of its integrity, healing and preservation of contractile function (reviewed in [3]). Inflammation is generally considered a protective reaction facilitating a recovery process at the site of injury. However, preliminary evidence indicates that an excessive and prolonged proinflammatory response following MI may evoke necrosis of surviving cardiomyocytes, or elicit an exaggerated extracellular matrix degradation, resulting in excessive infarct expansion, adverse cardiac remodeling and HF development. Unfortunately, a number of therapeutic approaches designed to target the proinflammatory response following MI failed to reduce MI size or improve clinical outcomes (reviewed in: [4]). Therefore, a better understanding of the mechanisms governing timely resolution of inflammation seems to be crucial for novel and effective therapeutic strategies design. Heme oxygenase (HO) is a key enzyme involved in heme catabolism and recycling of heme iron. HO was described for the first time in 1968 as a microsomal enzyme which catalyzes the oxidation of heme and its breakdown into a bile pigment, bilirubin [5]. Soon, this enzymatic activity involving several redox reactions was characterized. The reaction of heme oxidation by HO has an absolute and stoichiometric requirement for molecular oxygen (O2) and NADPH. It also requires the participation of cytochrome P450 reductase (CyP450R) activity. As a result of its action stoichiometric amounts of carbon monoxide (CO), ferrous iron (Fe2+) and biliverdin are generated. The latter one is then converted into bilirubin by biliverdin reductase (BvR) present in the cytosol [6] (Fig. 1). In fact, the reaction catalyzed by HOs involves seven steps and is rate-limiting part of heme catabolism [7].