Vanadium Complexes with Thioanilide Derivatives of Amino Acids: Inhibition of Human Phosphatases and Specificity  in Various Cell Models of Metabolic Disturbances

Grzegorz Kazek; Monika Głuch-Lutwin; Barbara Mordyl; Monika Kubacka; Anna Jurowska; Dariusz Cież; Bartosz Trzewik; Janusz Szklarzewicz; Monika A. Papież

doi:10.20944/preprints202304.0713.v2

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preprints.org > medicine and pharmacology > medicine and pharmacology > doi: 10.20944/preprints202304.0713.v2

Preprint Article Version 2 Preserved in Portico This version is not peer-reviewed

Vanadium Complexes with Thioanilide Derivatives of Amino Acids: Inhibition of Human Phosphatases and Specificity in Various Cell Models of Metabolic Disturbances

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Version 1 : Received: 20 April 2023 / Approved: 21 April 2023 / Online: 21 April 2023 (10:07:54 CEST)
Version 2 : Received: 24 May 2023 / Approved: 26 May 2023 / Online: 26 May 2023 (05:19:48 CEST)
Version 3 : Received: 13 February 2024 / Approved: 25 February 2024 / Online: 26 February 2024 (17:23:06 CET)

A peer-reviewed article of this Preprint also exists.

Kazek, G.; Głuch-Lutwin, M.; Mordyl, B.; Menaszek, E.; Kubacka, M.; Jurowska, A.; Cież, D.; Trzewik, B.; Szklarzewicz, J.; Papież, M.A. Vanadium Complexes with Thioanilide Derivatives of Amino Acids: Inhibition of Human Phosphatases and Specificity in Various Cell Models of Metabolic Disturbances. Pharmaceuticals 2024, 17, 229, doi:10.3390/ph17020229. Kazek, G.; Głuch-Lutwin, M.; Mordyl, B.; Menaszek, E.; Kubacka, M.; Jurowska, A.; Cież, D.; Trzewik, B.; Szklarzewicz, J.; Papież, M.A. Vanadium Complexes with Thioanilide Derivatives of Amino Acids: Inhibition of Human Phosphatases and Specificity in Various Cell Models of Metabolic Disturbances. Pharmaceuticals 2024, 17, 229, doi:10.3390/ph17020229.

Abstract

In the text, the synthesis and characteristics of the novel ONS-type vanadium(V) complexes with thioanilide derivatives of amino acids are described. They have shown inhibition of human protein tyrosine phosphatases (PTP1B, LAR, SHP1 and SHP2) in the submicromolar range, as well as inhibition of non-tyrosine phosphatases (CDC25A and PPA2) similar to bis(maltolato)oxovanadium(IV)(BMOV). The ONS complexes increased [14C]-deoxy-D-glucose transport into C2C12 myocytes, and one of them, VC070, also enhanced this transport in 3T3-L1 adipocytes. These complexes inhibited gluconeogenesis in hepatocytes HepG2, but none of them decreased lipid accumulation in the non-alcoholic fatty liver disease model using the same cells. Compared to the tested ONO-type vanadium complexes with 5-bromosalicylaldehyde and substituted benzhydrazides as Schiff base ligand components, the ONS complexes revealed stronger inhibition of protein tyrosine phosphatases, but the ONO complexes showed greater activity in the cell models in general. Moreover, the majority of the active complexes from both groups showed better effects than VOSO4 and BMOV. Complexes from both groups activated AKT and ERK signaling pathways in hepatocytes to a comparable extent. One of the ONO complexes, VC068, showed activity in all of the above models, also including glucose utilization in the myocytes and glucose transport in insulin-resistant hepatocytes. The discussion section explicates the results within the wider scope of the knowledge about vanadium complexes.

Keywords

vanadium complexes; phosphatases; in vitro; cells models; metabolic disorders; diabetes; insulin resistance; gluconeogenesis; NAFLD

Subject

Medicine and Pharmacology, Medicine and Pharmacology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Comments (1)

Comment 1

Received: 26 May 2023
Commenter: Monika Papież
Commenter's Conflict of Interests: Author

Comment: Dear Editor,
Please replace the old version of the manuscript doi:10.20944/preprints202304.0713.v1 (preprints-71482) with a new version with post-review corrections.

Best Regards
Monika Papież

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