Source:http://linkedlifedata.com/resource/pubmed/id/12531814
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2003-5-6
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pubmed:abstractText |
We have studied the membrane proteins of band 3 anion exchanger (AE1)-deficient mouse and human red blood cells. It has been shown previously that proteins of the band 3 complex are reduced or absent in these cells. In this study we show that proteins of the Rh complex are also greatly reduced (Rh-associated glycoprotein, Rh polypeptides, CD47, glycophorin B) or absent (LW). These observations suggest that the Rh complex is associated with the band 3 complex in healthy RBCs. Mouse band 3(-/-) RBCs differed from the human band 3-deficient RBCs in that they retained CD47. Aquaporin 1 was reduced, and its glycosylation was altered in mouse and human band 3-deficient RBCs. Proteins of the glycophorin C complex, and other proteins with independent cytoskeletal interactions, were present in normal or increased amounts. To obtain direct evidence for the association of the band 3 and the Rh protein complexes in the RBC, we examined whether Rh complex proteins were coimmunoprecipitated with band 3 from membranes. RhAG and Rh were found to be efficiently coimmunoprecipitated with band 3 from deoxycholate-solubilized membranes. Results suggest that band 3 forms the core of a macrocomplex of integral and peripheral RBC membrane proteins. The presence of these proteins in a single structural macrocomplex makes it likely that they have linked functional or regulatory roles. We speculate that this macrocomplex may function as an integrated CO(2)/O(2) gas exchange unit (metabolon) in the erythrocyte.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/DK26263,
http://linkedlifedata.com/resource/pubmed/grant/DK32094,
http://linkedlifedata.com/resource/pubmed/grant/DL56267,
http://linkedlifedata.com/resource/pubmed/grant/HL31579,
http://linkedlifedata.com/resource/pubmed/grant/HL64885,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL064885-04
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD47,
http://linkedlifedata.com/resource/pubmed/chemical/CD47 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cd47 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rh-Hr Blood-Group System
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4180-8
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pubmed:dateRevised |
2011-2-9
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pubmed:meshHeading |
pubmed-meshheading:12531814-Amino Acid Substitution,
pubmed-meshheading:12531814-Animals,
pubmed-meshheading:12531814-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:12531814-Antigens, CD,
pubmed-meshheading:12531814-Antigens, CD47,
pubmed-meshheading:12531814-Carrier Proteins,
pubmed-meshheading:12531814-Erythrocyte Membrane,
pubmed-meshheading:12531814-Humans,
pubmed-meshheading:12531814-Macromolecular Substances,
pubmed-meshheading:12531814-Membrane Proteins,
pubmed-meshheading:12531814-Mice,
pubmed-meshheading:12531814-Mice, Knockout,
pubmed-meshheading:12531814-Rh-Hr Blood-Group System
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pubmed:year |
2003
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pubmed:articleTitle |
A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane.
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pubmed:affiliation |
Department of Biochemistry, University of Bristol, United Kingom.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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