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A new insight into subinteractomes of functional antagonists: Thromboxane (CYP5A1) and prostacyclin (CYP8A1) synthases

Authors :
S A Usanov
L. A. Kaluzhskiy
Yuri Mezentsev
Andrew Ivanov
P V Ershov
Evgeniy Yablokov
Oksana Gnedenko
A. A. Gilep
A V Svirid
Victor G. Zgoda
Source :
Cell Biology International.
Publication Year :
2021
Publisher :
Wiley, 2021.

Abstract

The current article aims to summarize all possible spectrum of protein-protein interactions for thromboxane A synthase (CYP5A1) and prostacyclin synthase (CYP8A1). These enzymes metabolize the same substrate (prostaglandin H2 ) and can participate in cardiovascular, inflammatory, immune processes, and apoptosis modulation, as well as significantly influence the risk of cancers. Binary protein-protein and multiprotein complexes are of great importance in enzyme-regulating and signal-transduction pathways. However, protein partners of CYP5A1 and CYP8A1 are not yet fully identified, although both synthases are considered as prospective drug targets. At least 36 novel protein partners of CYP5A1 and CYP8A1 were revealed from different tissue types using an approach based on affinity isolation and mass spectrometry. Enrichment analysis showed that these proteins have different molecular functions: folding (refolding), unfolded protein and chaperon binding, protein transport (export/import), posttranslational modification, protein domain-specific binding, antioxidant activity, and glutathione homeostasis. A significant part of them, belonging to molecular chaperones, were common partners for CYP5A1 and CYP8A1, while other proteins were unique with the tissue-dependent distribution. New aspects of CYP5A1 and CYP8A1 interactomics and hetero-complex formation with different protein partners, including cytochrome P450s are discussed.

Details

ISSN :
10958355 and 10656995
Database :
OpenAIRE
Journal :
Cell Biology International
Accession number :
edsair.doi.dedup.....dad4b162958b8110b6973f5cacf1107d
Full Text :
https://doi.org/10.1002/cbin.11564