| Oxygen regulates the band 3-ankyrin bridge in the human erythrocyte membrane. | |
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MedLine Citation:
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PMID: 23013433 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The oxygenation state of erythrocytes is known to impact several cellular processes. As the only known O2 binding protein in red blood cells, hemoglobin has been implicated in the oxygenation-mediated control of cell pathways and properties. Band 3, an integral membrane protein linked to the spectrin/actin cytoskeleton, preferentially binds deoxygenated hemoglobin at its N-terminus, and has been postulated to participate in the mechanism by which oxygenation controls cellular processes. Because the ankyrin binding site on band 3 is located near the deoxyHb binding site, we hypothesized that deoxygenated hemoglobin might impact the association between band 3 and the underlying erythrocyte cytoskeleton, a link that is primarily established through band 3-ankyrin bridging. Here we show that deoxygenation of human erythrocytes results in displacement of ankyrin from band 3, leading to release of the spectrin/actin cytoskeleton from the membrane. This weakening of membrane-cytoskeletal interactions during brief periods of deoxygenation could prove beneficial to blood flow, but during episodes of prolonged deoxygenation, such as during sickle cell occlusive crises, could promote unwanted membrane vesiculation. |
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Authors:
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Marko Stefanovic; Estela Puchulu-Campanella; Gayani Kodippili; Philip S Low |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-9-27 |
Journal Detail:
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Title: The Biochemical journal Volume: - ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-9-27 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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