Biochemistry of Redox-Active Sulphur Compounds in Mammalian Cells and Approaches to Detecting Them

Мұқаба

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Тек жазылушылар үшін

Аннотация

The discovery of new classes of regulatory molecules in human and animal metabolism always leads to a large-scale study of their properties in the context of biochemistry, physiology, and pharmacology. About 20 years ago, hydrogen sulfide (H2S) and its derivatives – active sulfur forms (ASFs): persulfides, polysulfides, nitrosothiols, sulfenic acids, etc. – became one of such classes of molecules. The participation of ASFs in a variety of physiological and pathological processes, such as regulation of vascular tone, inflammation, long-term potentialization in the central nervous system, etc., has been shown. Changes in ASF levels or patterns of modification of their targets are associated with a wide range of pathologies: cardiovascular, oncologic, neurodegenerative, and others. For a part of these processes, mechanisms have been studied that involve direct modification of regulatory (NF-κB, Keap1) or effector (GAFD, eNOS, TRPA1) proteins through reactions of cysteine residues and metal-containing centers with APS. The presence of different regulated enzymatic systems producing APS and numerous molecular targets allows us to consider H2S and its derivatives as an important class of small regulatory molecules. H2S is counted among the so-called “gas transmitters”, along with nitric oxide(II) and carbon monoxide. Over the last 20 years, a huge amount of data on the biochemistry of these compounds and approaches to their study has been accumulated.

Толық мәтін

Рұқсат жабық

Авторлар туралы

R. Raevsky

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Pirogov Russian National Research Medical University

Email: d.s.bilan@gmail.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; ul. Ostrovityanova 1, Moscow, 117997

V. Katrukha

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; Faculty of Biology, Department of Biochemistry, Lomonosov Moscow State University

Email: yul.khramova@gmail.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskye gory 1/12, Moscow, 119234

Y. Khramova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; Faculty of Biology, Department of Biochemistry, Lomonosov Moscow State University

Хат алмасуға жауапты Автор.
Email: yul.khramova@gmail.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskye gory 1/12, Moscow, 119234

D. Bilan

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Pirogov Russian National Research Medical University

Email: d.s.bilan@gmail.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; ul. Ostrovityanova 1, Moscow, 117997

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2. Fig. 1. Active forms of sulfur, ordered by the formal oxidation states of sulfur atoms. Arrows indicate genealogical relationships discussed further in the text.

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3. Fig. 2. The main pathways of H2S formation in the mammalian organism. CBS – cystathionine-β-synthase, CGL – cystathionine γ-lyase, CAT – cysteine ​​aminotransferase, 3MP – 3-mercaptopyruvate, 3-MST – 3-mercaptopyruvate sulfotransferase.

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4. Fig. 3. Main APS-mediated modifications of protein molecules, explanations in the text.

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5. Fig. 4. Mitochondrial metabolism of H2S and interaction with components of the respiratory chain. CytC – cytochrome c, Q – ubiquinone, QH₂ – ubiquinol, PDO – persulfide dioxygenase, SHR – sulfoquinone reductase, CO – sulfite oxidase, III – the third complex of the respiratory chain ubiquinol-cytochrome c reductase, IV – the fourth complex of the respiratory chain cytochrome c oxidase.

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6. Fig. 5. Regulation of vasodilation by H₂S and ∙NO. PRGC – calcitonin gene-related peptide, KATP channel – ATP-dependent K⁺ channel, AC – adenylate cyclase, GC – guanylate cyclase, CGL – cystathionine-γ-lyase, VEGF – vascular endothelial growth factor, eNOS – endothelial nitric oxide synthase, NOX – NADPH oxidase.

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7. Fig. 6. APS-mediated regulation in neurons, explanations in the text. NMDAR – ionotropic NMDA receptor, APP – amyloid precursor protein, TRPA1 – Transient receptor potential cation channel subfamily A member 1, Nrf2 – nuclear E2 related factor 2, Keap1 – Kelch-like ECH-associated protein 1.

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8. Fig. 7. Fluorescent dyes for detection of H₂S (a–g) and sulfane compounds (d, e). (a, b) – Representatives of dyes that reduce H₂S to an amino group from an azide group (a) or a nitro group (b); (c) – dyes with two electrophilic groups, discrimination of H₂S from other thiol agents is shown; (d) – precipitation dye based on the formation of CuS from Cu²⁺, leading to increased fluorescence; (d, e) – dyes that react with sulfane compounds based on nucleophilic (d) or electrophilic (f) groups, followed by increased fluorescence.

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9. Fig. 8. Approaches for detection of APS-mediated modifications of proteins and peptides. MMTS – S-methylmethanethiosulfonate, biotin-GPDP – N-[6-(biotinamido)hexyl]-3′-(2′-pyridylthio)propionamide, DTT – dithiothreitol, PEG₂ – polyethyleneglycol, MSBT – methylsulfonylbenzothiazole. See text for explanations.

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