Interaction of Cytochrome C Oxidase with Steroid Hormones

Oleynikov, Ilya P.; Azarkina, Natalia V.; Vygodina, Tatiana V.; Konstantinov, Alexander A.

doi:10.3390/cells9102211

Cited by 8 publications

(26 citation statements)

References 37 publications

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“…It should be noted that at high DM concentrations titration curves are slightly shifted along the X-axis to the right, without changing the values of Ki(app). A similar effect was observed earlier on steroids [14] and Triton TX-100 [15]. Though the exact origin of this "lag-phase" remains unclear we assume it to be associated with interaction of the inhibitor and the empty DM micelles.…”

Section: Inhibition Of Solubilized Enzymesupporting

confidence: 85%

“…to Figure 1b). Such an effect of DM concentration on the level of inhibition was observed earlier with testosterone [14]. Figure 1e represents the dependence of Ki(app) values for T4 on [DM].…”

Section: Inhibition Of Solubilized Enzymesupporting

confidence: 76%

“…As shown recently [14,15] a number of steroid hormones and structurally similar compounds are effective inhibitors of the oxidase activity of CcO from mitochondria but at the same time do not affect the peroxidase reaction catalyzed by the enzyme. The data below show that none of the thyroid hormones T2, T3, and T4 inhibits the peroxidase activity of mitochondrial CcO.…”

Section: Thyroid Hormones Do Not Inhibit the Cco Peroxidase Activitymentioning

confidence: 83%

“…where v is the normalized rate of the oxidase reaction, I is the concentration of the hormone, and Ki(app) is the apparent inhibition constant at a given concentration of DM. It was found that similar to steroid hormones [14], the inhibition by thyroid hormones depends significantly on DM concentration in the medium. The dependence of Ki(app) values on [DM] is shown in Figure 1c.…”

Section: Inhibition Of Solubilized Enzymementioning

confidence: 95%

“…At the same time, no effect of steroid sex hormones on the activity of bacterial enzyme was found. However our group has shown recently that steroid hormones as well as structurally similar to them secosteroids and detergent Triton X-100 (which spatially mimic estrogen molecules in some respects) are able to bind with BABS and inhibit the activity of mitochondrial CcO [14,15].…”

Section: Introductionmentioning

confidence: 99%

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Direct Interaction of Mitochondrial Cytochrome c Oxidase with Thyroid Hormones: Evidence for Two Binding Sites

Oleynikov¹,

Azarkina²,

Vygodina³

2022

Preprint

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Thyroid hormones regulate tissue metabolism establishing an energy balance in the cell, in particular by affecting oxidative phosphorylation. Their long-term impact is mainly associated with changes in gene expression, while the short-term effects may differ in mechanism. Our work is devoted to short-term effects of hormones T2, T3, and T4 on mitochondrial cytochrome c oxidase (CcO) mediated by a direct contact with the enzyme. The data obtained indicate the existence of two separate sites of CcO interaction with thyroid hormones differing in location, affinity and specificity to hormone binding. It is shown that T3 and T4 but not T2 inhibit oxidase activity of CcO in solution and on membrane preparations with Кi≈100–200 M. In solution, T3 and T4 compete in a 1:1 ratio with the detergent dodecyl-maltoside for binding to the enzyme. Peroxidase and catalase partial activities of CcO are not sensitive to hormones while electron transfer from heme a to the oxidized binuclear center is affected. We believe that T3 and T4 are ligands of the Bile Acid Binding Site found in the 3D structure of CсO by Ferguson-Miller’s group, and hormone induced inhibition is associated with dysfunction of the K- proton channel. Similar conclusion we made recently with regard to steroid-like compounds. It is found that T2, T3, and T4 inhibit superoxide generation by oxidized CcO in the presence of excess Н2О2. Inhibition is characterized by Ki values of 0.3 – 5 M and apparently affects the formation of О2• at the protein surface. The second binding site for thyroid hormones presumably coincides with the point of tight T2 binding on the Va subunit described in the literature.

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Section: Inhibition Of Solubilized Enzymesupporting

confidence: 85%

Section: Inhibition Of Solubilized Enzymesupporting

confidence: 76%

Section: Thyroid Hormones Do Not Inhibit the Cco Peroxidase Activitymentioning

confidence: 83%

Section: Inhibition Of Solubilized Enzymementioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Direct Interaction of Mitochondrial Cytochrome c Oxidase with Thyroid Hormones: Evidence for Two Binding Sites

Oleynikov¹,

Azarkina²,

Vygodina³

2022

Preprint

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Mechanism of Inhibition of Cytochrome c Oxidase by Triton X-100

Oleynikov

Azarkina

Vygodina

et al. 2021

Biochemistry Moscow

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Metabolic signatures of pregnancy-induced cardiac growth

Fulghum

Smith

Chariker

et al. 2022

American Journal of Physiology-Heart and Circulatory Physiology

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The goal of this study was to develop an atlas of the metabolic, transcriptional, and proteomic changes that occur with pregnancy in the maternal heart. Timed pregnancy studies in FVB/NJ mice revealed significant increases in heart size by day 8 of pregnancy (mid-pregnancy; MP), which was sustained throughout the rest of the term compared with non-pregnant controls. Cardiac hypertrophy and myocyte cross-sectional area were highest 7 d after birth (post-birth; PB) and were associated with significant increases in end-diastolic and end-systolic left ventricular volumes and cardiac output. Metabolomics analyses revealed that, by day 16 of pregnancy (late pregnancy; LP), metabolites associated with nitric oxide production as well as acylcholines, sphingomyelins, and fatty acid species were elevated, which coincided with a lower activation state of phosphofructokinase and higher levels of pyruvate dehydrogenase kinase 4 (Pdk4). In the postpartum period, urea cycle metabolites, polyamines, and phospholipid levels were markedly elevated in the maternal heart. Cardiac transcriptomics in LP revealed significant increases in not only Pdk4, but also genes that regulate glutamate and ketone body oxidation, which were preceded in MP by higher expression of transcripts controlling cell proliferation and angiogenesis. Proteomics analysis of the maternal heart in LP and PB revealed significant reductions in several contractile filaments and mitochondrial complex subunits. Collectively, these findings describe the coordinated molecular changes that occur in the maternal heart during and after pregnancy.

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Interaction of Cytochrome C Oxidase with Steroid Hormones

Cited by 8 publications

References 37 publications

Direct Interaction of Mitochondrial Cytochrome c Oxidase with Thyroid Hormones: Evidence for Two Binding Sites

Direct Interaction of Mitochondrial Cytochrome c Oxidase with Thyroid Hormones: Evidence for Two Binding Sites

Mechanism of Inhibition of Cytochrome c Oxidase by Triton X-100

Metabolic signatures of pregnancy-induced cardiac growth

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