Glutathionylation of Na,K-ATPase Alpha-Subunit Alters Enzyme Conformation and Sensitivity to Trypsinolysis
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Published:2018-08
Issue:8
Volume:83
Page:969-981
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ISSN:0006-2979
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Container-title:Biochemistry (Moscow)
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language:en
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Short-container-title:Biochemistry Moscow
Author:
Dergousova E. A.,Poluektov Y. M.,Klimanova E. A.,Petrushanko I. Y.,Mitkevich V. A.,Makarov A. A.,Lopina O. D.
Publisher
Pleiades Publishing Ltd
Subject
Biochemistry,General Medicine
Reference16 articles.
1. Petrushanko, I. Y., Yakushev, S., Mitkevich, V. A., Kamanina, Y. V., Ziganshin, R. H., Meng, X., Anashkina, A. A., Makhro, A., Lopina, O. D., Gassmann, M., Makarov, A. A., and Bogdanova, A. (2012) S–glutathionylation of the Na,K–ATPase catalytic α subunit is a determinant of the enzyme redox sensitivity, J. Biol. Chem., 287, 32195–32205. 2. Petrushanko, I. Y., Mitkevich, V. A., Lakunina, V. A., Anashkina, A. A., Spirin, P. V., Rubtsov, P. M., Prassolov, V. S., Bogdanov, N. B., Hanggi, P., Fuller, W., Makarov, A. A., and Bogdanova, A. (2017) Cysteine residues 244 and 458–459 within the catalytic subunit of Na,K–ATPase control the enzyme’s hydrolytic and signaling function under hypoxic conditions, Redox Biol., 13, 310–319. 3. Dergousova, E. A., Petrushanko, I. Y., Klimanova, E. A., Mitkevich, V. A., Ziganshin, R. H., Lopina, O. D., and Makarov, A. A. (2017) Effect of reduction of redox modifications of Cys residues in the Na,K–ATPase α1–subunit on its activity, Biomolecules, 7, 18. 4. Mitkevich, V. A., Petrushanko, I. Y., Poluektov, Y. M., Burnysheva, K. M., Lakunina, V. A., Anashkina, A. A., and Makarov, A. A. (2016) Basal glutathionylation of Na,K–ATPase α–subunit depends on redox status of cells during the enzyme biosynthesis, Oxid. Med. Cell. Longev., 2016, doi: 10.1155/2016/9092328. 5. Smith, T. W. (1988) Purification of Na+,K+–ATPase from the supraorbital salt gland of the duck, Methods Enzymol., 156, 46–48.
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