Just Accepted by Free Radical Research
Special issue on “Peroxidase” Clare Hawkins and Pierre Van Antwerpen
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
Doi: 10.3109/10715762.2015.1038259
© 2015 Informa UK, Ltd. This provisional PDF corresponds to the article as it appeared upon acceptance. Fully formatted PDF and full text (HTML) versions will be made available soon. DISCLAIMER: The ideas and opinions expressed in the journal’s Just Accepted articles do not necessarily reflect those of Informa Healthcare (the Publisher), the Editors or the journal. The Publisher does not assume any responsibility for any injury and/or damage to persons or property arising from or related to any use of the material contained in these articles. The reader is advised to check the appropriate medical literature and the product information currently provided by the manufacturer of each drug to be administered to verify the dosages, the method and duration of administration, and contraindications. It is the responsibility of the treating physician or other health care professional, relying on his or her independent experience and knowledge of the patient, to determine drug dosages and the best treatment for the patient. Just Accepted articles have undergone full scientific review but none of the additional editorial preparation, such as copyediting, typesetting, and proofreading, as have articles published in the traditional manner. There may, therefore, be errors in Just Accepted articles that will be corrected in the final print and final online version of the article. Any use of the Just Accepted articles is subject to the express understanding that the papers have not yet gone through the full quality control process prior to publication.
Special issue on “Peroxidase”
Clare Hawkins1 and Pierre Van Antwerpen2,3 1
Heart Research Institute, Inflammation group, Universite Libre de Bruxelles, Sydney,
Australia, 2Laboratory of Pharmaceutical Chemistry, Universite Libre de Bruxelles, Brussels, Belgium, 3Analytical Platform of the Faculty of Pharmacy, Universite Libre de
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
Bruxelles, Brussels, Belgium
Correspondence: Pierre Van Antwerpen, Laboratory of Pharmaceutical Chemistry, Bd du Triomphe, Campus Plaine 205/5, Brussels, 1050 Belgium. E-mail: [email protected]
In this special issue of Free Radical Research, we have organized 9 articles or reviews from contributors of the “8th International Human Peroxidase Meeting”, which was held in Sydney (Australia) between September 9-12, 2013. The next meeting will be held at Koln (Germany) between September 14-17, 2015. The themes of this meeting were the roles, functions, physiopathological impacts of enzymes from the peroxidase-cyclooxygenase superfamily and especially, Chordata peroxidases including myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The articles of this special issue cover a large panel of research topics from laboratories that contribute to the
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
peroxidase field. Two research articles are related to the detection of halogenating activity by dyes. The research for these specific and sensitive markers is of importance to detect and/or quantify the peroxidase activity in vitro or ex vivo. The research article written by Arnhold and colleagues focuses on the detection of the halogenating activity in neutrophils and eosinophils by a fluorescent dye, namely aminophenyl fluorescein (1). This method could be applied to flow cytometry but also to detect production of hypohalogenous acids by myeloperoxidase (MPO) and eosinophil peroxidase (EPO) from their respective leukocytes. Sokolov et al. validate celestin blue B as an interesting probe for the measurement of myeloperoxidase activity, and demonstrate its suitability for assessing MPO inhibition (2). A third article by Franck et al. validate a combined assay for the quantity and the activity of MPO in biological fluids. Using the immunocapture of the enzyme, they first specifically quantify the amount of MPO by a second antibody before measuring its activity by the Amplex Red method in a second step (3). In the research article entitled: “Interaction of ceruloplasmin with eosinophil peroxidase (EPO) as compared to its interplay with myeloperoxidase: reciprocal effect on enzymatic properties”, Sokolov and his co-workers propose a comprehensive study of the interaction between EPO and ceruloplasmin (4). Ceruloplasmin is a plasma protein that can interact with peroxidases and modulates their activity. As this interaction has been already observed for MPO, the authors compare ceruloplasmin interaction with both peroxidases. Thiocyanate is a pseudohalogenous anion, which is a substrate for peroxidases such as MPO, EPO, and LPO. Hypothiocyanous acid, which is the product of the reaction of thiocyanate and peroxidases, specifically oxidises thiol (Cys) residues of proteins, resulting in the
formation of reversible thiol oxidation products including sulfenic acids. These products can be reduced back to Cys by antioxidant enzyme systems. In the review entitled: “Biochemical mechanisms and therapeutic potential of thiocyanate in human health”, Chandler and Day explore the oxidation of thiocyanate by Chordata peroxidases and underline the potential role of thiocyanate as therapeutical agent that could modulate peroxidase deleterious activity (5). Interestingly, Morgan et al. demonstrate that the thiocyanate supplementation decreases the atherosclerotic plaque development in human MPO transgenic mice (6). These authors emphasize the specific reversible oxidative modifications generated by hypothiocyanous acid
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
compared to hypochlorous acid also produced by MPO, which produces irreversible oxidation products. Konradi et al. explore the role of reactive oxygen species (ROS) in vascular dysfunction (7). This condition is generally admitted as an initial step in the development of heart failure and leukocyte peroxidases seem to be one of the promoting factors. The authors propose new therapeutical approaches that could include peroxidases as interesting drug targets. There is significant evidence that peroxidases contribute to the production of ROS in vivo. In this context, the review of Carroll et al. entitled: “Reaction of low molecular mass organoselenium compounds (and their sulfur analogues) with inflammation-associated oxidants” provides a comprehensive overview of the role of selenium as an antioxidant (8). Selenium has similar chemical properties to sulfur but in general, organoselenium compounds have a higher reactivity towards ROS. This exhaustive review explores the benefits of such compounds in the struggle against ROS, notably those produced by peroxidases. Finally, Van Antwerpen and Zouaoui Boudjeltia propose a review entitled: “Rational drug design applied to myeloperoxidase inhibition” (9). As MPO was pointed out as a therapeutical target, many authors are trying to develop specific MPO inhibitors. This review illustrates the rational drug design approach applied to MPO inhibition and its benefit for the research of new MPO inhibitors. In summary, the 9 articles in this special issue of Free Radical Research will bring readers new insights into the interesting world of human peroxidases, a subfamily of enzymes which contribute to the production of ROS and hypohalous acids. These articles cover technologies, comprehensive reviews, and fundamental research related to these heme-containing
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
enzymes. We hope that readers of Free Radical Research will enjoy reading this special
issue.
References 1. Flemmig J, Remmler J, Zschaler J, Arnhold J. Detection of the halogenating activity of haem peroxidases in leukocytes by aminophenyl fluorescein. Free Radical Research 2015. 2. Sokolov AV, Kostevich VA, Kozlov SO, Donskoy ES, Vlasova II, Rudenko AO, Zakharova ET, Vasilyev VB, Panasenko OM. Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. Free Radical Research 2015.
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
3. Franck T, Minguet G, Delporte C, Derochette S, Zouaoui Boudjeltia K, Van Antwerpen P, Gach O, Deby-Dupont G, Mouithys-Mickalad A, Serteyn D. An immunological method to combine the measurement of active and total myeloperoxidase on the same biological fluid and its application in finding inhibitors which interact directly with the enzyme. Free Radical Research 2015. 4. Sokolov AV, VKostevich VA, Zakharova ET, Samygina VR, Panasenko OM, Vasilyev VB. Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: reciprocal effect on enzymatic properties. Free Radical Research 2015. 5. Chandler JD, Day BJ. Biochemical Mechanisms and Therapeutic Potential of the Pseudohalide Thiocyanate in Human Health. Free Radical Research 2015. 6. Morgan PE, Laura RP, R. Maki A, Reynolds WF, Davies MJ. Thiocyanate supplementation decreases atherosclerotic plaque in mice expressing human myeloperoxidase. Free Radical Research 2015. 7. Konradi J, Mollenhauer M, Baldus S, Klinke A. Redox-Sensitive Mechanisms underlying Vascular Dysfunction in Heart Failure. Free Radical Research 2015. 8. Carroll L, Davies MJ, Pattison DI. Reaction of low molecular mass organoselenium compounds (and their sulfur analogues) with inflammation-associated oxidants. Free Radical Research 2015. 9. Van Antwerpen P, Zouaoui Boudjeltia K. Rational drug design applied to myeloperoxidase inhibition. Free Radical Research 2015.
Special issue on “Peroxidase” Clare Hawkins and Pierre Van Antwerpen
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
Doi: 10.3109/10715762.2015.1038259
© 2015 Informa UK, Ltd. This provisional PDF corresponds to the article as it appeared upon acceptance. Fully formatted PDF and full text (HTML) versions will be made available soon. DISCLAIMER: The ideas and opinions expressed in the journal’s Just Accepted articles do not necessarily reflect those of Informa Healthcare (the Publisher), the Editors or the journal. The Publisher does not assume any responsibility for any injury and/or damage to persons or property arising from or related to any use of the material contained in these articles. The reader is advised to check the appropriate medical literature and the product information currently provided by the manufacturer of each drug to be administered to verify the dosages, the method and duration of administration, and contraindications. It is the responsibility of the treating physician or other health care professional, relying on his or her independent experience and knowledge of the patient, to determine drug dosages and the best treatment for the patient. Just Accepted articles have undergone full scientific review but none of the additional editorial preparation, such as copyediting, typesetting, and proofreading, as have articles published in the traditional manner. There may, therefore, be errors in Just Accepted articles that will be corrected in the final print and final online version of the article. Any use of the Just Accepted articles is subject to the express understanding that the papers have not yet gone through the full quality control process prior to publication.
Special issue on “Peroxidase”
Clare Hawkins1 and Pierre Van Antwerpen2,3 1
Heart Research Institute, Inflammation group, Universite Libre de Bruxelles, Sydney,
Australia, 2Laboratory of Pharmaceutical Chemistry, Universite Libre de Bruxelles, Brussels, Belgium, 3Analytical Platform of the Faculty of Pharmacy, Universite Libre de
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
Bruxelles, Brussels, Belgium
Correspondence: Pierre Van Antwerpen, Laboratory of Pharmaceutical Chemistry, Bd du Triomphe, Campus Plaine 205/5, Brussels, 1050 Belgium. E-mail: [email protected]
In this special issue of Free Radical Research, we have organized 9 articles or reviews from contributors of the “8th International Human Peroxidase Meeting”, which was held in Sydney (Australia) between September 9-12, 2013. The next meeting will be held at Koln (Germany) between September 14-17, 2015. The themes of this meeting were the roles, functions, physiopathological impacts of enzymes from the peroxidase-cyclooxygenase superfamily and especially, Chordata peroxidases including myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The articles of this special issue cover a large panel of research topics from laboratories that contribute to the
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
peroxidase field. Two research articles are related to the detection of halogenating activity by dyes. The research for these specific and sensitive markers is of importance to detect and/or quantify the peroxidase activity in vitro or ex vivo. The research article written by Arnhold and colleagues focuses on the detection of the halogenating activity in neutrophils and eosinophils by a fluorescent dye, namely aminophenyl fluorescein (1). This method could be applied to flow cytometry but also to detect production of hypohalogenous acids by myeloperoxidase (MPO) and eosinophil peroxidase (EPO) from their respective leukocytes. Sokolov et al. validate celestin blue B as an interesting probe for the measurement of myeloperoxidase activity, and demonstrate its suitability for assessing MPO inhibition (2). A third article by Franck et al. validate a combined assay for the quantity and the activity of MPO in biological fluids. Using the immunocapture of the enzyme, they first specifically quantify the amount of MPO by a second antibody before measuring its activity by the Amplex Red method in a second step (3). In the research article entitled: “Interaction of ceruloplasmin with eosinophil peroxidase (EPO) as compared to its interplay with myeloperoxidase: reciprocal effect on enzymatic properties”, Sokolov and his co-workers propose a comprehensive study of the interaction between EPO and ceruloplasmin (4). Ceruloplasmin is a plasma protein that can interact with peroxidases and modulates their activity. As this interaction has been already observed for MPO, the authors compare ceruloplasmin interaction with both peroxidases. Thiocyanate is a pseudohalogenous anion, which is a substrate for peroxidases such as MPO, EPO, and LPO. Hypothiocyanous acid, which is the product of the reaction of thiocyanate and peroxidases, specifically oxidises thiol (Cys) residues of proteins, resulting in the
formation of reversible thiol oxidation products including sulfenic acids. These products can be reduced back to Cys by antioxidant enzyme systems. In the review entitled: “Biochemical mechanisms and therapeutic potential of thiocyanate in human health”, Chandler and Day explore the oxidation of thiocyanate by Chordata peroxidases and underline the potential role of thiocyanate as therapeutical agent that could modulate peroxidase deleterious activity (5). Interestingly, Morgan et al. demonstrate that the thiocyanate supplementation decreases the atherosclerotic plaque development in human MPO transgenic mice (6). These authors emphasize the specific reversible oxidative modifications generated by hypothiocyanous acid
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
compared to hypochlorous acid also produced by MPO, which produces irreversible oxidation products. Konradi et al. explore the role of reactive oxygen species (ROS) in vascular dysfunction (7). This condition is generally admitted as an initial step in the development of heart failure and leukocyte peroxidases seem to be one of the promoting factors. The authors propose new therapeutical approaches that could include peroxidases as interesting drug targets. There is significant evidence that peroxidases contribute to the production of ROS in vivo. In this context, the review of Carroll et al. entitled: “Reaction of low molecular mass organoselenium compounds (and their sulfur analogues) with inflammation-associated oxidants” provides a comprehensive overview of the role of selenium as an antioxidant (8). Selenium has similar chemical properties to sulfur but in general, organoselenium compounds have a higher reactivity towards ROS. This exhaustive review explores the benefits of such compounds in the struggle against ROS, notably those produced by peroxidases. Finally, Van Antwerpen and Zouaoui Boudjeltia propose a review entitled: “Rational drug design applied to myeloperoxidase inhibition” (9). As MPO was pointed out as a therapeutical target, many authors are trying to develop specific MPO inhibitors. This review illustrates the rational drug design approach applied to MPO inhibition and its benefit for the research of new MPO inhibitors. In summary, the 9 articles in this special issue of Free Radical Research will bring readers new insights into the interesting world of human peroxidases, a subfamily of enzymes which contribute to the production of ROS and hypohalous acids. These articles cover technologies, comprehensive reviews, and fundamental research related to these heme-containing
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
enzymes. We hope that readers of Free Radical Research will enjoy reading this special
issue.
References 1. Flemmig J, Remmler J, Zschaler J, Arnhold J. Detection of the halogenating activity of haem peroxidases in leukocytes by aminophenyl fluorescein. Free Radical Research 2015. 2. Sokolov AV, Kostevich VA, Kozlov SO, Donskoy ES, Vlasova II, Rudenko AO, Zakharova ET, Vasilyev VB, Panasenko OM. Kinetic method for assaying the halogenating activity of myeloperoxidase based on reaction of celestine blue B with taurine halogenamines. Free Radical Research 2015.
Free Radic Res Downloaded from informahealthcare.com by Yale Dermatologic Surgery on 05/15/15 For personal use only.
3. Franck T, Minguet G, Delporte C, Derochette S, Zouaoui Boudjeltia K, Van Antwerpen P, Gach O, Deby-Dupont G, Mouithys-Mickalad A, Serteyn D. An immunological method to combine the measurement of active and total myeloperoxidase on the same biological fluid and its application in finding inhibitors which interact directly with the enzyme. Free Radical Research 2015. 4. Sokolov AV, VKostevich VA, Zakharova ET, Samygina VR, Panasenko OM, Vasilyev VB. Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: reciprocal effect on enzymatic properties. Free Radical Research 2015. 5. Chandler JD, Day BJ. Biochemical Mechanisms and Therapeutic Potential of the Pseudohalide Thiocyanate in Human Health. Free Radical Research 2015. 6. Morgan PE, Laura RP, R. Maki A, Reynolds WF, Davies MJ. Thiocyanate supplementation decreases atherosclerotic plaque in mice expressing human myeloperoxidase. Free Radical Research 2015. 7. Konradi J, Mollenhauer M, Baldus S, Klinke A. Redox-Sensitive Mechanisms underlying Vascular Dysfunction in Heart Failure. Free Radical Research 2015. 8. Carroll L, Davies MJ, Pattison DI. Reaction of low molecular mass organoselenium compounds (and their sulfur analogues) with inflammation-associated oxidants. Free Radical Research 2015. 9. Van Antwerpen P, Zouaoui Boudjeltia K. Rational drug design applied to myeloperoxidase inhibition. Free Radical Research 2015.
