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Biomolecules
Volume 10
Issue 7
10.3390/biom10071060
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Article

Probing Structure and Function of Alkali Sensor IRR with Monoclonal Antibodies

by
Alexander S. Goryashchenko
1,*,
Andrey A. Mozhaev
1,2,
Oxana V. Serova
1,
Tatiana N. Erokhina
3,
Alexander N. Orsa
1,
Igor E. Deyev
4 and
Alexander G. Petrenko
1
1
Laboratory of Receptor Cell Biology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia
2
Laboratory of Bioorganic Structures, Department of X-ray and Synchrotron Studies, A.V. Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics” of Russian Academy of Sciences, 119333 Moscow, Russia
3
Laboratory of Molecular Diagnostics, Department of Plant Molecular Biology and Biotechnology, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia
4
Group of Molecular Physiology, Department of Peptide and Protein Technologies, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(7), 1060; https://doi.org/10.3390/biom10071060
Received: 25 March 2020 / Revised: 6 July 2020 / Accepted: 13 July 2020 / Published: 16 July 2020
(This article belongs to the Section Molecular Biology)
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Abstract

To study the structure and function of the pH-regulated receptor tyrosine kinase insulin receptor-related receptor (IRR), а member of the insulin receptor family, we obtained six mouse monoclonal antibodies against the recombinant IRR ectodomain. These antibodies were characterized in experiments with exogenously expressed full-length IRR by Western blotting, immunoprecipitation, and immunocytochemistry analyses. Utilizing a previously obtained set of IRR/IR chimeras with swapped small structural domains and point amino acid substitutions, we mapped the binding sites of the obtained antibodies in IRR. Five of them showed specific binding to different IRR domains in the extracellular region, while one failed to react with the full-length receptor. Unexpectedly, we found that 4D5 antibody can activate IRR at neutral pH, and 4C2 antibody can inhibit activation of IRR by alkali. Our study is the first description of the instruments of protein nature that can regulate activity of the orphan receptor IRR and confirms that alkali-induced activation is an intrinsic property of this receptor tyrosine kinase. View Full-Text
Keywords: IRR; monoclonal antibody; activator; inhibitor; receptor tyrosine kinase; alkali sensor IRR; monoclonal antibody; activator; inhibitor; receptor tyrosine kinase; alkali sensor
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MDPI and ACS Style

Goryashchenko, A.S.; Mozhaev, A.A.; Serova, O.V.; Erokhina, T.N.; Orsa, A.N.; Deyev, I.E.; Petrenko, A.G. Probing Structure and Function of Alkali Sensor IRR with Monoclonal Antibodies. Biomolecules 2020, 10, 1060. https://doi.org/10.3390/biom10071060

AMA Style

Goryashchenko AS, Mozhaev AA, Serova OV, Erokhina TN, Orsa AN, Deyev IE, Petrenko AG. Probing Structure and Function of Alkali Sensor IRR with Monoclonal Antibodies. Biomolecules. 2020; 10(7):1060. https://doi.org/10.3390/biom10071060

Chicago/Turabian Style

Goryashchenko, Alexander S., Andrey A. Mozhaev, Oxana V. Serova, Tatiana N. Erokhina, Alexander N. Orsa, Igor E. Deyev, and Alexander G. Petrenko. 2020. "Probing Structure and Function of Alkali Sensor IRR with Monoclonal Antibodies" Biomolecules 10, no. 7: 1060. https://doi.org/10.3390/biom10071060

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