pubmed-article:12531814 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12531814 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
pubmed-article:12531814 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:12531814 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:12531814 | lifeskim:mentions | umls-concept:C0230715 | lld:lifeskim |
pubmed-article:12531814 | lifeskim:mentions | umls-concept:C0205100 | lld:lifeskim |
pubmed-article:12531814 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:12531814 | pubmed:dateCreated | 2003-5-6 | lld:pubmed |
pubmed-article:12531814 | 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. | lld:pubmed |
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pubmed-article:12531814 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12531814 | pubmed:language | eng | lld:pubmed |
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pubmed-article:12531814 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:12531814 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12531814 | pubmed:month | May | lld:pubmed |
pubmed-article:12531814 | pubmed:issn | 0006-4971 | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:MohandasNarla... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:BruceLesley... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:TannerMichael... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:DelaunayJeanJ | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:RibeiroM... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:PetersLuanne... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:AnsteeDavid... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:BeckmannRolan... | lld:pubmed |
pubmed-article:12531814 | pubmed:author | pubmed-author:ChasisJoel... | lld:pubmed |
pubmed-article:12531814 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12531814 | pubmed:day | 15 | lld:pubmed |
pubmed-article:12531814 | pubmed:volume | 101 | lld:pubmed |
pubmed-article:12531814 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12531814 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12531814 | pubmed:pagination | 4180-8 | lld:pubmed |
pubmed-article:12531814 | pubmed:dateRevised | 2011-2-9 | lld:pubmed |
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pubmed-article:12531814 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12531814 | pubmed:articleTitle | A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane. | lld:pubmed |
pubmed-article:12531814 | pubmed:affiliation | Department of Biochemistry, University of Bristol, United Kingom. | lld:pubmed |
pubmed-article:12531814 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12531814 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12531814 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:12531814 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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