Identification of Melittin-Like Proteins with a Molecular Weight of 67 kDa that Interact with Na+/K+-ATPase

Melittin, a peptide from bee venom, was found to be able to interact with many proteins, including calmodulin target proteins and ion-transporting P-type ATPases. It is assumed that melittin mimics a protein module involved in protein-protein interactions within cells. Previously, a Na + /K + -ATPas...

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Bibliographic Details
Published in:Molecular biology (New York) 2023-12, Vol.57 (6), p.1070-1076
Main Authors: Varfolomeeva, L. A., Klimanova, E. A., Sidorenko, S. V., Fedorov, D. A., Lopina, O. D.
Format: Article
Language:English
Subjects:
Affinity chromatography
Antibodies
Biochemistry
Biomedical and Life Sciences
Calmodulin
Chaperones
Endoplasmic reticulum
Hsp70 protein
Human Genetics
Immunoprecipitation
Kidneys
Life Sciences
Mass spectroscopy
Molecular weight
Na+/K+-exchanging ATPase
Ouabain
Protein interaction
Protein transport
Proteins
The Role of Redox-Dependent Proteins in the Implementation of Redox-Regulation of Cells
Venom
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Summary:Melittin, a peptide from bee venom, was found to be able to interact with many proteins, including calmodulin target proteins and ion-transporting P-type ATPases. It is assumed that melittin mimics a protein module involved in protein-protein interactions within cells. Previously, a Na + /K + -ATPase containing the α1 isoform of the catalytic subunit was found to co-precipitate with a protein with a molecular weight of about 70 kDa that interacts with antibodies against melittin by cross immunoprecipitation. In the presence of a specific Na + /K + -ATPase inhibitor (ouabain), the amount of protein with a molecular weight of 70 kDa interacting with Na + /K + -ATPase increases. In order to identify melittin-like protein from murine kidney homogenate, a fraction of melittin-like proteins with a molecular weight of approximately 70 kDa was obtained using affinity chromatography with immobilized antibodies specific to melittin. By mass spectrometry analysis, the obtained protein fraction was found to contain three molecular chaperones of Hsp70 superfamily: mitochondrial mtHsp70 (mortalin), Hsp73, Grp78 (BiP) of endoplasmic reticulum. These data suggest that chaperones from the HSP-70 superfamily contain a melittin-like module.
ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893323060195