Hypochlorite-induced damage of plasminogen molecules: structural-functional disturbance

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Abstract


Plasminogen being a precursor of plasmin, a serine protease which plays a fundamental role in the intravascular thrombolysis. For the first time, by using high-resolution mass spectrometry, data were obtained of oxidative modifications of the plasminogen molecule under induced oxidation. The FTIR data show that under oxidation on the protein, its secondary structure also undergoes the rearrangements. The high tolerance of plasminogen to oxidation can be due to both the closed conformation and the ability of some Met residues to serve as ROS trap.


About the authors

A. D. Vasilyeva

Institute of Biochemical Physics of the Russian Academy of Sciences

Author for correspondence.
Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

L. V. Yurina

Institute of Biochemical Physics of the Russian Academy of Sciences

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

A. N. Shchegolikhin

Institute of Biochemical Physics of the Russian Academy of Sciences

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

A. E. Bugrova

Institute of Biochemical Physics of the Russian Academy of Sciences

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

T. S. Konstantinova

Institute of Biochemical Physics of the Russian Academy of Sciences

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

M. I. Indeykina

Institute of Biochemical Physics of the Russian Academy of Sciences; Moscow Institute of Physics and Technology

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991; 9, Institutskij, Dolgoprudny, Moscow region, 141701

A. S. Kononikhin

Institute of Biochemical Physics of the Russian Academy of Sciences; Moscow Institute of Physics and Technology; Skolkovo Institute of Science and Technology

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991; 9, Institutskij, Dolgoprudny, Moscow region, 141701; 3, Nobelya street, Moscow, 143026

E. N. Nikolaev

Institute of Biochemical Physics of the Russian Academy of Sciences; Skolkovo Institute of Science and Technology

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991; 3, Nobelya street, Moscow, 143026

Corresponding Member of the Russian Academy of Sciences

M. A. Rosenfeld

Institute of Biochemical Physics of the Russian Academy of Sciences

Email: alexandra.d.vasilyeva@gmail.com

Russian Federation, 4, Kosygina street, Moscow, 119991

References

  1. Castellino F. J., Ploplis V.A. // Thromb. Haemost. 2005. V. 93. P. 647-654.
  2. Law R.H., Caradoc-Davies T., Cowieson N., Horvath A.J., Quek A.J., Encarnacao J.A., Steer D., Co-wan A., Zhang Q., Lu B.G., Pike R.N., Smith A.I., Coughlin P.B., Whisstock J.C. // Cell Rep. 2012. V. 1. P. 185-190.
  3. Ponting C.P., Marshall J M., Cederholm-Williams S.A. // Blood Coagul. Fibrinolysis. 1992. V. 3. P. 605-614.
  4. Rijken D.C. Sakharov D.V. // Thromb. Res. 2001. V. 103. Suppl. 1:S41-9.
  5. Malle E., Furtmuller P.G., Sattler W., Obinger C. // Br. J. Pharmacol. 2007. V. 152. P. 838-854.
  6. Deutsch D.G., Mertz E.J. // Science. 1970. V. 170. P. 1095-1096.
  7. Weigand K.M., White N., Chung D., Ellingson E., Wang Y., Fu X., Pozzo D.C. // Biophys. J. 2012. V. 103. P. 2399-2407.
  8. Gugliucci A. // Clin. Chem. Lab. Med. 2008. V. 46. P. 1403-1409.
  9. Galetskiy D., Lohscheider J.N., Kononikhi A.S., Popo I.A., Nikolaev E.N., Adamska I. // Rapid Commun. Mass Spectrom. 2011. V. 25. P. 184-190.
  10. Vasilyeva A.D., Yurina L.V., Indeykina M.I., Bychkova A.V., Bugrova A.E., Biryukova M.I., Kononikhin A.S., Nikolaev E. N., Rosenfeld M. A. // BBA - Proteins and Proteomics. 2018. V. 1866. P. 875-884.
  11. Rosenfeld M.A., Shchegolikhin A.N., Bychkova A.V., Leonova V.B., Biryukova M.I., Kostanova E. A. // Free Radic. Biol. Med. 2014. V. 77. P 106-120.
  12. Hawkins C. L., Pattison D. I., Davies M. J. // Amino Acids. 2003. V. 25. P. 259-274.
  13. Yang H., Yang S., Kong J., Dong A., Yu S. // Nature Protocols. 2015. V. 10. P. 382-396.
  14. Lim J., Kim G., Levine R. // Neurochem. Res. 2019. V. 44. P. 247-257. doi: 10.1007/s11064-017-2460-0

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