REDOX SIGNALING SKIN - PMC

Javier Egea, Isabel Fabregat, Yves M. Frapart, Pietro Ghezzi, Agnes Görlach, Thomas Kietzmann, Kateryna Kubaichuk, Ulla G. Knaus, Manuela G. Lopez, Gloria Olaso-Gonzalez, Andreas Petry, Rainer Schulz, Jose Vina, Paul Winyard, Kahina Abbas, Opeyemi S. Ademowo, Catarina B. Afonso, Ioanna Andreadou, Haike Antelmann, Fernando Antunes, Mutay Aslan, Markus M. Bachschmid, Rui M. Barbosa, Vsevolod Belousov, Carsten Berndt, David Bernlohr, Esther Bertrán, Alberto Bindoli, Serge P. Bottari, Paula M. Brito, Guia Carrara, Ana I. Casas, Afroditi Chatzi, Niki Chondrogianni, Marcus Conrad, Marcus S. Cooke, João G. Costa, Antonio Cuadrado, Pham My-Chan Dang, Barbara De Smet, Bilge Debelec–Butuner, Irundika H.K. Dias, Joe Dan Dunn, Amanda J. Edson, Mariam El Assar, Jamel El-Benna, Péter Ferdinandy, Ana S. Fernandes, Kari E. Fladmark, Ulrich Förstermann, Rashid Giniatullin, Zoltán Giricz, Anikó Görbe, Helen Griffiths, Vaclav Hampl, Alina Hanf, Jan Herget, Pablo Hernansanz-Agustín, Melanie Hillion, Jingjing Huang, Serap Ilikay, Pidder Jansen-Dürr, Vincent Jaquet, Jaap A. Joles, Balaraman Kalyanaraman, Danylo Kaminskyy, Mahsa Karbaschi, Marina Kleanthous, Lars-Oliver Klotz, Bato Korac, Kemal Sami Korkmaz, Rafal Koziel, Damir Kračun, Karl-Heinz Krause, Vladimír Křen, Thomas Krieg, João Laranjinha, Antigone Lazou, Huige Li, Antonio Martínez-Ruiz, Reiko Matsui, Gethin J. McBean, Stuart P. Meredith, Joris Messens, Verónica Miguel, Yuliya Mikhed, Irina Milisav, Lidija Milković, Antonio Miranda-Vizuete, Miloš Mojović, María Monsalve, Pierre-Alexis Mouthuy, John Mulvey, Thomas Münzel, Vladimir Muzykantov, Isabel T.N. Nguyen, Matthias Oelze, Nuno G. Oliveira, Carlos M. Palmeira, Nikoletta Papaevgeniou, Aleksandra Pavićević, Brandán Pedre, Fabienne Peyrot, Marios Phylactides, Gratiela G. Pircalabioru, Andrew R. Pitt, Henrik E. Poulsen, Ignacio Prieto, Maria Pia Rigobello, Natalia Robledinos-Antón, Leocadio Rodríguez-Mañas, Anabela P. Rolo, Francis Rousset, Tatjana Ruskovska, Nuno Saraiva, Shlomo Sasson, Katrin Schröder, Khrystyna Semen, Tamara Seredenina, Anastasia Shakirzyanova, Geoffrey L. Smith, Thierry Soldati, Bebiana C. Sousa, Corinne M. Spickett, Ana Stancic, Marie José Stasia, Holger Steinbrenner, Višnja Stepanić, Sebastian Steven, Kostas Tokatlidis, Erkan Tuncay, Belma Turan, Fulvio Ursini, Jan Vacek, Olga Vajnerova, Kateřina Valentová, Frank Van Breusegem, Lokman Varisli, Elizabeth A. Veal, A. Suha Yalçın, Olha Yelisyeyeva, Neven Žarković, Martina Zatloukalová, Jacek Zielonka, Rhian M. Touyz, Andreas Papapetropoulos, Tilman Grune, Santiago Lamas, Harald H.H.W. Schmidt, Fabio Di Lisa, Andreas Daiber

Redox Biol. 2017 Oct; 13: 94–162. Published online 2017 May 18. doi: 10.1016/j.redox.2017.05.007

Correction in:: Redox Biol. 2018 Apr; 14: 694–696.

PMCID:: PMC5458069

Abstract Article PDF–4.8M

Select item 79378295.

Interactions of zinc- and redox-signaling pathways

Christopher Hübner, Hajo Haase

Redox Biol. 2021 May; 41: 101916. Published online 2021 Feb 24. doi: 10.1016/j.redox.2021.101916

PMCID:: PMC7937829

Abstract Article PDF–1.6M

Select item 76626516.

In Vivo Imaging with Genetically Encoded Redox Biosensors

Alexander I. Kostyuk, Anastasiya S. Panova, Aleksandra D. Kokova, Daria A. Kotova, Dmitry I. Maltsev, Oleg V. Podgorny, Vsevolod V. Belousov, Dmitry S. Bilan

Int J Mol Sci. 2020 Nov; 21(21): 8164. Published online 2020 Oct 31. doi: 10.3390/ijms21218164

PMCID:: PMC7662651

Abstract Article PDF–14M

Select item 27148807.

Supreme EnLIGHTenment: Damage Recognition and Signaling in the Mammalian UV Response

Peter Herrlich, Michael Karin, Carsten Weiss

Mol Cell. Author manuscript; available in PMC 2009 Jul 24.

Published in final edited form as: Mol Cell. 2008 Feb 15; 29(3): 279–290. doi: 10.1016/j.molcel.2008.01.001

PMCID:: PMC2714880

Abstract Article PDF–581K

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Angiotensin II Signal Transduction: An Update on Mechanisms of Physiology and Pathophysiology

Steven J. Forrester, George W. Booz, Curt D. Sigmund, Thomas M. Coffman, Tatsuo Kawai, Victor Rizzo, Rosario Scalia, Satoru Eguchi

Physiol Rev. 2018 Jul 1; 98(3): 1627–1738. Published online 2018 Jun 6. doi: 10.1152/physrev.00038.2017

PMCID:: PMC6335102

Abstract Article

Select item 60715449.

Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling

Petr Ježek, Blanka Holendová, Keith D. Garlid, Martin Jabůrek

Antioxid Redox Signal. 2018 Sep 1; 29(7): 667–714. Published online 2018 Sep 1. doi: 10.1089/ars.2017.7225

PMCID:: PMC6071544

Abstract Article PDF–2.8M

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Shedding a New Light on Skin Aging, Iron- and Redox-Homeostasis and Emerging Natural Antioxidants

Charareh Pourzand, Andrea Albieri-Borges, Nico N. Raczek

Antioxidants (Basel) 2022 Mar; 11(3): 471. Published online 2022 Feb 27. doi: 10.3390/antiox11030471

PMCID:: PMC8944509

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Neurotoxicity Linked to Dysfunctional Metal Ion Homeostasis and Xenobiotic Metal Exposure: Redox Signaling and Oxidative Stress

Carla Garza-Lombó, Yanahi Posadas, Liliana Quintanar, María E. Gonsebatt, Rodrigo Franco

Antioxid Redox Signal. 2018 Jun 20; 28(18): 1669–1703. Published online 2018 Jun 20. doi: 10.1089/ars.2017.7272

PMCID:: PMC5962337

Abstract Article PDF–1.4M

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Redox Regulation of Cell Survival

Dunyaporn Trachootham, Weiqin Lu, Marcia A. Ogasawara, Nilsa Rivera-Del Valle, Peng Huang

Antioxid Redox Signal. 2008 Aug; 10(8): 1343–1374. doi: 10.1089/ars.2007.1957

PMCID:: PMC2932530

Abstract Article PDF–538K

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Fyn is a redox sensor involved in solar ultraviolet light-induced signal transduction in skin carcinogenesis

Jong-Eun Kim, Eunmiri Roh, Mee Hyun Lee, Dong Hoon Yu, Dong Joon Kim, Tae-Gyu Lim, Sung Keun Jung, Cong Peng, Yong-Yeon Cho, Sally Dickinson, Dave Alberts, G. Tim Bowden, Janine Einspahr, Steven P Stratton, Clara Curiel, Ann M. Bode, Ki Won Lee, Zigang Dong

Oncogene. Author manuscript; available in PMC 2016 Aug 10.

Published in final edited form as: Oncogene. 2016 Aug 4; 35(31): 4091–4101. Published online 2015 Dec 21. doi: 10.1038/onc.2015.471

PMCID:: PMC4916055

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Understanding the mechanobiology of phytoacoustics through molecular Lens: Mechanisms and future perspectives

Sajad Ali, Anshika Tyagi, Suvin Park, Hanhong Bae

J Adv Res. 2024 Nov; 65: 47–72. Published online 2023 Dec 13. doi: 10.1016/j.jare.2023.12.011

PMCID:: PMC11518948

Abstract Article PDF–4.5M

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Regulation of Cellular Redox Signaling by Matricellular Proteins in Vascular Biology, Immunology, and Cancer

David D. Roberts, Sukhbir Kaur, Jeffrey S. Isenberg

Antioxid Redox Signal. 2017 Oct 20; 27(12): 874–911. Published online 2017 Oct 20. doi: 10.1089/ars.2017.7140

PMCID:: PMC5653149

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Redox States of Protein Cysteines in Pathways of Protein Turnover and Cytoskeleton Dynamics Are Changed with Aging and Reversed by Slc7a11 Restoration in Mouse Lung Fibroblasts

Yuxuan Zheng, Michael L. Merchant, Tom J. Burke, Jeffrey D. Ritzenthaler, Ming Li, Adam E. Gaweda, Frederick W. Benz, Jesse Roman, Walter H. Watson

Oxid Med Cell Longev. 2020; 2020: 2468986. Published online 2020 Jun 7. doi: 10.1155/2020/2468986

PMCID:: PMC7298344

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Cell–cell communication: new insights and clinical implications

Jimeng Su, Ying Song, Zhipeng Zhu, Xinyue Huang, Jibiao Fan, Jie Qiao, Fengbiao Mao

Signal Transduct Target Ther. 2024; 9: 196. Published online 2024 Aug 7. doi: 10.1038/s41392-024-01888-z

PMCID:: PMC11382761

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Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases

Bowen Yang, Yumeng Lin, Yibo Huang, Ying-Qiang Shen, Qianming Chen

Redox Biol. 2024 Apr; 70: 103032. Published online 2024 Jan 13. doi: 10.1016/j.redox.2024.103032

PMCID:: PMC10827563

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Targeting the Redox Balance in Inflammatory Skin Conditions

Frank A. D. T. G. Wagener, Carine E. Carels, Ditte M. S. Lundvig

Int J Mol Sci. 2013 May; 14(5): 9126–9167. Published online 2013 Apr 26. doi: 10.3390/ijms14059126

PMCID:: PMC3676777

Abstract Article PDF–359K

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Thioredoxins, Glutaredoxins, and Peroxiredoxins—Molecular Mechanisms and Health Significance: from Cofactors to Antioxidants to Redox Signaling

Eva-Maria Hanschmann, José Rodrigo Godoy, Carsten Berndt, Christoph Hudemann, Christopher Horst Lillig

Antioxid Redox Signal. 2013 Nov 1; 19(13): 1539–1605. doi: 10.1089/ars.2012.4599

PMCID:: PMC3797455

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Figure 3

Cold physical plasma-derived generation and delivery of ROS/RNS triggers redox modifications and accelerates physiological responses in wound healing. Redox sensitive signaling pathways (e.g., Nrf2, p53) provide protection from excess ROS/RNS to eventually re-establish redox homeostasis. Cold physical plasma-derived ROS/RNS are efficient triggers of such signaling events in skin cells in vitro and in vivo. Accordingly, plasma treatment promotes several cellular and tissue responses linked to molecular signatures accompanying enhanced wound healing.

Redox for Repair: Cold Physical Plasmas and Nrf2 Signaling Promoting Wound Healing

Antioxidants (Basel). 2018 Oct;7(10):146.
Figure 1

Redox regulation by oxidation of redox sensitive cysteine residues. The thiol group (SH) of specific cysteine residues of proteins can be oxidized by oxidized glutathione (GSSG) or other molecules, including cysteine-reactive electrophiles, causing S-glutathionylation or other types of cysteine oxidation, such as intermolecular disulfide bond formation. These types of post-translational modifications can influence the properties of proteins and the activity of enzymes, which is termed redox regulation or redox signaling.

Electrophiles against (Skin) Diseases: More Than Nrf2

Biomolecules. 2020 Feb;10(2):271.
Fig. 9

Redox imbalance leads to terminal differentiation, aging, and apoptosis of wool follicles in MF wool lambs. a The left: Activity of the PI3K/AKT signaling pathway in longitudinal sections of Meg3 (IG-DMR)-KO mouse skin tissue as determined using immunofluorescence. The letter DP indicates dermal papilla. Middle: detection of the ROS level of 1-d reciprocal cross progeny between ALC and MF using 8-OHDG staining. The black arrow indicates the dermal papilla cell. Right: detection of skin cell apoptosis of 1-d reciprocal cross progeny between ALC and MF using TUNEL staining. b The left: detection of skin cell proliferation of 1-d reciprocal cross progeny between ALC and MF using Ki67 immunostaining. Right: skin section observations of 1-d reciprocal cross progeny by using transmission electron microscopy. The red dotted line indicates the position of dermal papillae, DP: dermal papilla, Nu: cell nucleus, Mito: mitochondria. c Detection of mitochondria DNA copy numbers in the skin tissue of 1-d reciprocal cross progeny between ALC and MF lambs (n = 5; **P < 0.01). d Detection of ATP levels in the skin tissue of 1-d reciprocal cross progeny between ALC and MF lambs (n = 10; ***P < 0.001). e Detection of H₂O₂ levels in the skin tissue of 1-d reciprocal cross progeny between ALC and MF lambs (n = 10; **P < 0.01). f Detection of reactive oxygen species (ROS) levels in the skin tissue of 1-d reciprocal cross progeny between ALC and MF lambs (n = 10; **P < 0.01)

Epigenetic mechanism of Gtl2-miRNAs causes the primitive sheep characteristics found in purebred Merino sheep

Cell Biosci. 2023;13:190.
Figure 6

The KEAP1/NRF2 signaling pathway in keratinization and related skin diseases. (a) Phenotypes of the cornified cell envelope (CE). The oxidized status preferentially stabilizes the CE, and loricrin (LOR) promotes cytoskeletal cross-linkage. NRF2 repairs a defective barrier, probably in response to a perturbed redox balance, whereas persistent NRF2 activation hampers the formation of disulfide cross-linkage and makes the CE fragile. (b) Keratinization and disease phenotypes. An oxidative environment favors retention keratosis, which can lead to common dry skin conditions such as atopic dermatitis (AD) (clinically non-inflamed skin), or comedo (occluded hair follicle due to infundibular keratinization). On the other hand, strong and persistent NRF2 activation may be associated with autosomal recessive congenital ichthyosis (ARCI) or metabolizing acquired dioxin-induced skin hamartomas (MADISH).

The KEAP1/NRF2 Signaling Pathway in Keratinization

Antioxidants (Basel). 2020 Aug;9(8):751.