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Your search keyword '"Bychkov, Maxim L."' showing total 18 results
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18 results on '"Bychkov, Maxim L."'

2. In Search of the Role of Three-Finger Starfish Proteins.

Author

Lyukmanova, Ekaterina N., Bychkov, Maxim L., Chernikov, Andrei M., Kukushkin, Ilya D., Kulbatskii, Dmitrii S., Shabelnikov, Sergey V., Shulepko, Mikhail A., Zhao, Ran, Guo, Wenxiao, Kirpichnikov, Mikhail P., Shenkarev, Zakhar O., and Paramonov, Alexander S.

Abstract

Three-finger proteins (TFPs), or Ly6/uPAR proteins, are characterized by the beta-structural LU domain containing three protruding "fingers" and stabilized by four conserved disulfide bonds. TFPs were initially characterized as snake alpha-neurotoxins, but later many studies showed their regulatory roles in different organisms. Despite a known expression of TFPs in vertebrates, they are poorly studied in other taxa. The presence of TFPs in starfish was previously shown, but their targets and functional role still remain unknown. Here, we analyzed expression, target, and possible function of the Lystar5 protein from the Asterias rubens starfish using bioinformatics, qPCR, and immunoassay. First, the presence of Lystar5 homologues in all classes of echinoderms was demonstrated. qPCR revealed that mRNA of Lystar5 and LyAr2 are expressed mainly in coelomocytes and coelomic epithelium of Asterias, while mRNA of other TFPs, LyAr3, LyAr4, and LyAr5, were also found in a starfish body wall. Using anti-Lystar5 serum from mice immunized by a recombinant Lystar5, we confirmed that this protein is expressed on the surface of coelomocytes and coelomic epithelium cells. According to ELISA, a recombinant analogue of Lystar5 bound to the membrane fraction of coelomocytes and coelomic epithelium but not to the body wall or starfish arm tip. Analysis by LC-MALDI MS/MS suggested integrin α-8-like protein expressed in the coelomocytes and coelomic epithelium as a target of Lystar5. Thus, our insights propose the important role of TFPs in regulation of starfish physiology and show prospects for their further research. [ABSTRACT FROM AUTHOR]

Published
2024
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3. Membrane-mediated interaction of non-conventional snake three-finger toxins with nicotinic acetylcholine receptors

Author

Shenkarev, Zakhar O., Chesnokov, Yuri M., Zaigraev, Maxim M., Chugunov, Anton O., Kulbatskii, Dmitrii S., Kocharovskaya, Milita V., Paramonov, Alexander S., Bychkov, Maxim L., Shulepko, Mikhail A., Nolde, Dmitry E., Kamyshinsky, Roman A., Yablokov, Evgeniy O., Ivanov, Alexey S., Kirpichnikov, Mikhail P., and Lyukmanova, Ekaterina N.

Published
2022
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7. Aβ1-42 Accumulation Accompanies Changed Expression of Ly6/uPAR Proteins, Dysregulation of the Cholinergic System, and Degeneration of Astrocytes in the Cerebellum of Mouse Model of Early Alzheimer Disease

Author

Bychkov, Maxim L., primary, Isaev, Aizek B., additional, Andreev-Andrievskiy, Alexander A., additional, Petrov, Konstantin, additional, Paramonov, Alexander S., additional, Kirpichnikov, Mikhail P., additional, and Lyukmanova, Ekaterina N., additional

Published
2023
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8. New Three-Finger Protein from Starfish Asteria rubens Shares Structure and Pharmacology with Human Brain Neuromodulator Lynx2

Author

Paramonov, Alexander S., primary, Shulepko, Mikhail A., additional, Makhonin, Alexey M., additional, Bychkov, Maxim L., additional, Kulbatskii, Dmitrii S., additional, Chernikov, Andrey M., additional, Myshkin, Mikhail Yu., additional, Shabelnikov, Sergey V., additional, Shenkarev, Zakhar O., additional, Kirpichnikov, Mikhail P., additional, and Lyukmanova, Ekaterina N., additional

Published
2022
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9. Mambalgin-2 Inhibits Lung Adenocarcinoma Growth and Migration by Selective Interaction With ASIC1/α-ENaC/γ-ENaC Heterotrimer

Author

Sudarikova, Anastasia V., primary, Bychkov, Maxim L., additional, Kulbatskii, Dmitrii S., additional, Chubinskiy-Nadezhdin, Vladislav I., additional, Shlepova, Olga V., additional, Shulepko, Mikhail A., additional, Koshelev, Sergey G., additional, Kirpichnikov, Mikhail P., additional, and Lyukmanova, Ekaterina N., additional

Published
2022
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13. SLURP-1 Controls Growth and Migration of Lung Adenocarcinoma Cells, Forming a Complex With α7-nAChR and PDGFR/EGFR Heterodimer

Author

Bychkov, Maxim L., primary, Shulepko, Mikhail A., additional, Shlepova, Olga V., additional, Kulbatskii, Dmitrii S., additional, Chulina, Irina A., additional, Paramonov, Alexander S., additional, Baidakova, Ludmila K., additional, Azev, Viatcheslav N., additional, Koshelev, Sergey G., additional, Kirpichnikov, Mikhail P., additional, Shenkarev, Zakhar O., additional, and Lyukmanova, Ekaterina N., additional

Published
2021
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14. Water‐soluble variant of human Lynx1 positively modulates synaptic plasticity and ameliorates cognitive impairment associated with α7‐nAChR dysfunction

Author

Shenkarev, Zakhar O., primary, Shulepko, Mikhail A., additional, Bychkov, Maxim L., additional, Kulbatskii, Dmitrii S., additional, Shlepova, Olga V., additional, Vasilyeva, Nathalia A., additional, Andreev-Andrievskiy, Alexander A., additional, Popova, Anfisa S., additional, Lagereva, Evgeniya A., additional, Loktyushov, Eugene V., additional, Koshelev, Sergey G., additional, Thomsen, Morten S., additional, Dolgikh, Dmitry A., additional, Kozlov, Sergey A., additional, Balaban, Pavel M., additional, Kirpichnikov, Mikhail P., additional, and Lyukmanova, Ekaterina N., additional

Published
2020
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16. Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1) Is a Selective Allosteric Antagonist of α7 Nicotinic Acetylcholine Receptor

Author

Lyukmanova, Ekaterina N., primary, Shulepko, Mikhail A., additional, Kudryavtsev, Denis, additional, Bychkov, Maxim L., additional, Kulbatskii, Dmitrii S., additional, Kasheverov, Igor E., additional, Astapova, Maria V., additional, Feofanov, Alexey V., additional, Thomsen, Morten S., additional, Mikkelsen, Jens D., additional, Shenkarev, Zakhar O., additional, Tsetlin, Victor I., additional, Dolgikh, Dmitry A., additional, and Kirpichnikov, Mikhail P., additional

Published
2016
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18. Biochemical Basis of Skin Disease Mal de Meleda: SLURP-1Mutants Differently Affect Keratinocyte Proliferation and Apoptosis

Author

Shulepko, Mikhail A., Bychkov, Maxim L., Shenkarev, Zakhar O., Kulbatskii, Dmitrii S., Makhonin, Alexey M., Paramonov, Alexander S., Chugunov, Anton O., Kirpichnikov, Mikhail P., and Lyukmanova, Ekaterina N.

Abstract

Mal de Meleda is an autosomal recessive palmoplantar keratoderma associated with mutations in a gene encoding SLURP-1. SLURP-1 controls growth, differentiation, and apoptosis of keratinocytes by interaction with α7-type nicotinic acetylcholine receptors. SLURP-1 has a three-finger structure with a β-structural core (head) and three prolonged loops (fingers). To determine the role of SLURP-1 mutations, we produced 22 mutant variants of the protein, including those involved in Mal de Meleda pathogenesis. All mutants except R71H, R71P, T52A, R96P, and L98P were produced in the folded form. SLURP-1 reduces the growth of Het-1A keratinocytes; thus, we studied the influence of the mutations on its antiproliferative activity. Mutations in loops I and III led to the protein inactivation, whereas most mutations in loop II increased SLURP-1 antiproliferative activity. Alanine substitutions of R96 and L98 residues located in the protein head resulted in the appearance of additional pro-apoptotic activity. Our results agree with the diversity of Mal de Meleda phenotypes. Using obtained functional data, the SLURP-1/α7 type nicotinic acetylcholine receptor complex was modeled in silico. Our study provides functional and structural information about the role of the SLURP-1 mutations in Mal de Meleda pathogenesis and predicts SLURP-1 variants, which could drive the disease.

Published
2021
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