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

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Title: A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein
Authors: Hongoh, Masafumi / Haratake, Mamoru / Fuchigami, Takeshi / Nakayama, Morio
Issue Date: 28-Jun-2012
Publisher: Royal Society of Chemistry
Citation: Dalton Transactions, 41(24), pp.7340-7349; 2012
Abstract: 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.
Keywords: Active membranes / Anion exchangers / Anion-exchange mechanism / Buffer solutions / Carbon dioxide transport / Cytoplasmic domains / Energy dependent / Membrane spanning domains / Membrane transport / Red cells / Amino acids / Carbon dioxide / Cell membranes / Cytology / Ion exchange resins / Membranes / Nitric oxide / Plasmas / Proteins / Trace elements / Selenium
URI: http://hdl.handle.net/10069/29380
ISSN: 14779226
DOI: 10.1039/c2dt30707c
Rights: © 2012 The Royal Society of Chemistry.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/29380

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