Selenium binding to human hemoglobin via selenotrisulfide

Haratake, Mamoru; Fujimoto, Katsuyoshi; Ono, Masahiro; Nakayama, Morio

doi:10.1016/j.bbagen.2005.02.002

Cited by 30 publications

(34 citation statements)

References 18 publications

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“…These mass spectral data were identical to our previous work, in which penicillamine selenotrisulfide (PenSSeSPen) reacted only with the reactive Cys-β93 via the thiol exchange mechanism [12]. In addition, no remarkable difference in the structural organization between the Hb-Se complex and Hb was observed in the circular dichroism spectral data over the range from 190 to 350 nm (Fig.…”

Section: Resultssupporting

confidence: 74%

“…Since Hb did not allow the forming of Hb selenotrisulfide (HbSSeSHb) in the reaction with selenite probably due to a steric hindrance, the Painter reaction with glutathione (GSH) could also be involved in the metabolism of selenite in the RBC. We have demonstrated that selenotrisulfide preferentially reacts with the Cys-β93 by the thiol exchange mechanism to form HbSSeSR, and selenium is not eliminated from Hb in the presence of GSH [12]. Consequently, selenite in the RBC is thought to transform into GSSeSG, and subsequently, GSSeSG could react with Cys-β93 to form the HbSSeSG.…”

Section: Resultsmentioning

confidence: 99%

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Hemoglobin-mediated selenium export from red blood cells

et al. 2008

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On the basis of the fact that selenium (Se) from selenite binds to hemoglobin (Hb), we investigated the missing process in the selenium export from red blood cells (RBCs), i.e., the transfer of selenium bound to Hb to RBC membrane proteins. To elucidate the molecular events of the Hbassociated selenium export from RBC, an Hb-Se complex was synthesized from thiol-exchange of Cys-β93 in Hb with penicillamine-substituted glutathione selenotrisulfide, as a model of major metabolic intermediates, and then interactions between the Hb-Se complex and RBC inside-out vesicles (IOVs) were examined. Selenium bound to Hb was transferred to the IOV membrane on the basis of the intrinsic interactions between Hb and the cytoplasmic domains of Band 3 protein (CDB3). The observed selenium transfer was inhibited by the pretreatments of IOVs with iodoacetamide and the α-chymotrypsin digestion, indicating that the Hb mediates the selenium transfer to the thiol groups of CDB3. In addition, it was found that deoxygenated Hb with a high binding affinity for CDB3 more favorably transferred selenium to the IOV membranes than oxygenated Hb with a low affinity. When selenium export from RBC to the plasma was examined by continuously introducing nitrogen gas, the selenium export rate was promoted with an increase in the rate of deoxygenated Hb. Overall, these data suggested that Hb could possibly play a role in the selenium export from RBC treated with selenite in an oxygen-linked fashion.

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Section: Resultssupporting

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Hemoglobin-mediated selenium export from red blood cells

et al. 2008

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“…40 Biogenic thiols in the bloodstream, such as Hb and glutathione in red cells and albumin in the plasma, can participate in the metabolism and/or transport of selenium species inside the red cells and the subsequent transport to the peripherals. 39,45,49 The thiols of spectrins can be interactive with glutathione to form disulfide bond, which associates to the flexible deformation of red cells in the peripheral capillaries. 50 Thus, spectrin thiols could possibly interact with selenium metabolites, and the selenium binding to spectrins was actually observed (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…L-Penicillamine selenotrisulfide (Pen-SSeS-Pen) was synthesized from Pen and selenious acid according to a previously described procedure 44,45 : Elemental analysis (%), calculated for Co., Ltd.). The red cell membranes were suspended in 5P8 containing 1 % SDS and added to an equal volume of a 1 mM DTNB solution.…”

Section: Reaction Of Pen-sses-pen With Red Cell Membranesmentioning

confidence: 99%

A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein

et al. 2012

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In this paper, we describe a thiol-mediated and energy-dependent membrane transport of selenium by erythroid anion exchanger 1 (AE1, also known as band 3 protein). The AE1 is the most abundant integral protein of red cell membranes and plays a critical role in the carbon dioxide transport system in which carbon dioxide is carried as bicarbonate in the plasma. This protein mediates the membrane transport of selenium, an essential antioxidant micronutrient, from red cells to the plasma in a manner that is distinct from the already known anion exchange mechanism. In this pathway, selenium bound to the cysteine 93 of the hemoglobin β chain (Hb-Cysβ93) is transported by the relay mechanism to the Cys317 of the amino-terminal cytoplasmic domain of the AE1 on the basis of the intrinsic interaction between the two proteins and is subsequently exported to the plasma via the Cys843 of the membrane-spanning domain. The selenium export did not occur in plain isotonic buffer solutions and required thiols, such as albumin, in the outer medium. Such a membrane transport mechanism would also participate in the export pathways of the nitric oxide vasodilator activity and other thiol-reactive substances bound to the Hb-Cysβ93 from red cells to the plasma and/or peripherals. 2 IntroductionSelenium belongs to chalcogens that shares similar chemical properties especially with sulfur and, to a lesser extent, with tellurium. This element is an essential micronutrient for humans and other higher animal species. 1 Selenocysteine (SeCys), the 21st naturally occurring amino acid encoded by the UGA codon, is the form of selenium present in enzymes and proteins. In humans, 25 SeCys-containing proteins (selenoproteins) are identified on the basis of their selenoproteome analysis. 2 The best-known selenoproteins are the glutathione peroxidases (GPxs) that can catalyze the reduction of certain peroxide species (R−OOH) to the alcohols (R−OH) at their active center SeCys residue. 1,3 Nutritional selenium is thought to be obtained from a variety of selenium compounds in the diet, mostly in organic forms, such as SeCys and selenomethionine (SeMet). During the systemic delivery of selenium, selenoprotein P that is present in the plasma is thought to be the selenium supply protein for the biosynthesis of the other selenoproteins including GPxs. 4,5 Recent evidence in selenoprotein P (SelP) knockout mice has shown that the distribution of selenium from the liver to testis and brain is mediated by Sel P. 6,7 It is also found that in the absence of SelP, selenium from selenious acid (SA, H 2 SeO 3 ) in the diet can be distributed to the peripherals by a yet unknown mechanism. 8 So far, little is known about the membrane transport of selenium from selenium source compounds, including SA. Inorganic SA is rare as a chemical form of the food source compounds, but highly bioavailable SA is most frequently used as a source compound for the treatment of a selenium deficiency. 9Selenium-enriched yeast (a common form of selenium supplement) is found to contain ...

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“…1 top) was synthesized according to a previously described procedure. 27,28) Briefly, a 1 mM selenious acid solution was poured into a 4 mM Pen solution and the mixture was allowed to react with stirring for 3 h at room temperature and left for another 20 h at 4°C. The resulting snow-white precipitate was isolated and carefully washed twice with cold water and then washed twice with cold methanol.…”

Section: Methodsmentioning

confidence: 99%

A Comprehensive Analysis of Selenium-Binding Proteins in the Brain Using Its Reactive Metabolite

Yoshida

Hori

Ura

et al. 2016

CHEMICAL & PHARMACEUTICAL BULLETIN

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The intracellular metabolism of selenium in the brain currently remains unknown, although the antioxidant activity of this element is widely acknowledged to be important in maintaining brain functions. In this study, a comprehensive method for identifying the selenium-binding proteins using PenSSeSPen as a model of the selenium metabolite, selenotrisulfide (RSSeSR, STS), was applied to a complex cell lysate generated from the rat brain. Most of the selenium from L-penicillamine selenotrisulfide (PenSSeSPen) was captured by the cytosolic protein thiols in the form of STS through the thiol-exchange reaction (R-SH PenSSeSPen→R-SSeSPen PenSH). The cytosolic protein species, which reacted with the PenSSeSPen mainly had a molecular mass of less than 20 kDa. A thiol-containing protein at m/z 15155 in the brain cell lysate was identified as the cystatin-12 precursor (CST12) from a rat protein database search and a tryptic fragmentation experiment. CST12 belongs to the cysteine proteinase inhibitors of the cystatin superfamily that are of interest in mechanisms regulating the protein turnover and polypeptide production in the central nervous system and other tissues. Consequently, CST12 is suggested to be one of the cytosolic proteins responsible for the selenium metabolism in the brain.

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Selenium binding to human hemoglobin via selenotrisulfide

Cited by 30 publications

References 18 publications

Hemoglobin-mediated selenium export from red blood cells

Hemoglobin-mediated selenium export from red blood cells

A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein

A Comprehensive Analysis of Selenium-Binding Proteins in the Brain Using Its Reactive Metabolite

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