Document Detail


Oxygen regulates the band 3-ankyrin bridge in the human erythrocyte membrane.
MedLine Citation:
PMID:  23013433     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The oxygenation state of erythrocytes is known to impact several cellular processes. As the only known O2-binding protein in red blood cells, haemoglobin 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 haemoglobin 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 (deoxygenated haemoglobin)-binding site, we hypothesized that deoxyHb might impact the association between band 3 and the underlying erythrocyte cytoskeleton, a link that is primarily established through band 3-ankyrin bridging. In the present paper 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.
Authors:
Marko Stefanovic; Estela Puchulu-Campanella; Gayani Kodippili; Philip S Low
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  The Biochemical journal     Volume:  449     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-10     Completed Date:  2013-02-08     Revised Date:  2014-04-10    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  143-50     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Anion Exchange Protein 1, Erythrocyte / genetics,  metabolism*
Ankyrins / genetics,  metabolism*
Erythrocyte Membrane / metabolism*,  physiology
Erythrocytes / physiology*
Humans
Oxygen / blood*
Grant Support
ID/Acronym/Agency:
R01 GM024417/GM/NIGMS NIH HHS; R01GM24417-33/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Anion Exchange Protein 1, Erythrocyte; 0/Ankyrins; S88TT14065/Oxygen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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