The effects of hypochlorous acid and neutrophil proteases on the structure and function of extracellular superoxide dismutase

Morales, Karla; Olesen, Mads Nikolaj; Poulsen, Ebbe Toftgaard; Larsen, Ulrike G.; Enghild, Jan J.; Petersen, Steen V.

doi:10.1016/j.freeradbiomed.2014.12.027

Cited by 9 publications

(6 citation statements)

References 52 publications

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“…Hypochlorous acid (HOCl) is a type of ROS that is released from neutrophils and macrophages [25]. Compounds that have roles in ROS removal, such as hypochlorous acid, peroxynitrite, and hydrogen peroxide, contain thiol groups (glutathione, methionine, and taurine) [26].…”

Section: Discussionmentioning

confidence: 99%

Thiol/Disulfide homeostasis in patients with rheumatoid arthritis

Tuzcu

Baykara

Omma

et al. 2019

Romanian Journal of Internal Medicine

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Background. Oxidative stress may play an important role in rheumatoid arthritis (RA) etiopathogenesis. The thiol group is a very strong antioxidant. In this study, we aimed to investigate the presence of oxidative stress in patients with RA by evaluating thiol/disulfide homeostasis. Material and methods. A total of 50 female RA patients and 50 healthy female controls were included in this study. Thiol and disulfide values were calculated utilizing novel methods. Results. Native thiol (p < 0.001) and total thiol (p < 0.001) levels of RA patients were significantly lower compared to values in the control group. However, the disulfide (p < 0.001) levels of RA patients were strongly higher than in healthy individuals. A negative correlation was found between thiol and disease activity score-28 among the patients, whereas a positive correlation was found between disulfide and disease activity score-28 among the patients. Conclusion. We found that the thiol–disulfide rate deteriorated in RA patients, with the proportion of disulfide increasing. There is a strong correlation between the decrease in thiol levels, increase in disulfide levels and the disease activity scores.

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Section: Discussionmentioning

confidence: 99%

Thiol/Disulfide homeostasis in patients with rheumatoid arthritis

Tuzcu

Baykara

Omma

et al. 2019

Romanian Journal of Internal Medicine

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“…In vertebrate, EcSOD regulates extracellular concentrations of reactive oxygen species and reactive nitrogen species (Fridovich, 1995), and consequently involves in immune response during inflammatory insults (Morales et al, 2015). Whereas invertebrate EcSOD is of great interest for its distinct RGD-motif which is absent in vertebrate (Gonzalez et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…R/KGD motif was reported to recognize and bind to Integrin family members, and it had been described as the essential cell attachment site for fibronectin, fibrinogen and vitronectin to bind to Integrins (Takagi, 2004). Moreover, many R/KGD motif containing proteins were evidenced with specific binding ability to a wide range of foreign invaders (Hostetter, 2000;Narasimhan et al, 1994). As a consequence of the adhesion interaction of R/KGD motif containing proteins with Integrins, pathogenic microbes are internalized by nonprofessional phagocytes (Hauck et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The modulation of extracellular superoxide dismutase in the specifically enhanced cellular immune response against secondary challenge of Vibrio splendidus in Pacific oyster (Crassostrea gigas)

Liu

Zhang

Wang

et al. 2016

Developmental & Comparative Immunology

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“…It is susceptible to PTMs by neutrophil-derived HOCl at the inflammatory sites of lung injury. The destabilization of a protein's structure via the oxidation of the N-terminal region and the formation of intermolecular cross linking increase the protein's susceptibility to proteolysis by neutrophil-secreted proteases [151]. Apparently, SOD3 is necessary to protect cells from oxidative stress in healthy tissues.…”

Section: Redox Regulation Of Proteases Involved In Inflammationmentioning

confidence: 99%

Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning

Petushkova

Zamyatnin

2020

Biomolecules

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Proteolytic enzymes play a crucial role in metabolic processes, providing the cell with amino acids through the hydrolysis of multiple endogenous and exogenous proteins. In addition to this function, proteases are involved in numerous protein cascades to maintain cellular and extracellular homeostasis. The redox regulation of proteolysis provides a flexible dose-dependent mechanism for proteolytic activity control. The excessive reactive oxygen species (ROS) and reactive nitrogen species (RNS) in living organisms indicate pathological conditions, so redox-sensitive proteases can swiftly induce pro-survival responses or regulated cell death (RCD). At the same time, severe protein oxidation can lead to the dysregulation of proteolysis, which induces either protein aggregation or superfluous protein hydrolysis. Therefore, oxidative stress contributes to the onset of age-related dysfunction. In the present review, we consider the post-translational modifications (PTMs) of proteolytic enzymes and their impact on homeostasis.

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The effects of hypochlorous acid and neutrophil proteases on the structure and function of extracellular superoxide dismutase

Cited by 9 publications

References 52 publications

Thiol/Disulfide homeostasis in patients with rheumatoid arthritis

Thiol/Disulfide homeostasis in patients with rheumatoid arthritis

The modulation of extracellular superoxide dismutase in the specifically enhanced cellular immune response against secondary challenge of Vibrio splendidus in Pacific oyster (Crassostrea gigas)

Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning

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