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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1999-8-4
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pubmed:abstractText |
Protein 4.2 is a major component of the red blood cell (RBC) membrane skeleton. We used targeted mutagenesis in embryonic stem (ES) cells to elucidate protein 4.2 functions in vivo. Protein 4. 2-null (4.2(-/-)) mice have mild hereditary spherocytosis (HS). Scanning electron microscopy and ektacytometry confirm loss of membrane surface in 4.2(-/-) RBCs. The membrane skeleton architecture is intact, and the spectrin and ankyrin content of 4. 2(-/-) RBCs are normal. Band 3 and band 3-mediated anion transport are decreased. Protein 4.2(-/-) RBCs show altered cation content (increased K+/decreased Na+)resulting in dehydration. The passive Na+ permeability and the activities of the Na-K-2Cl and K-Cl cotransporters, the Na/H exchanger, and the Gardos channel in 4. 2(-/-) RBCs are significantly increased. Protein 4.2(-/-) RBCs demonstrate an abnormal regulation of cation transport by cell volume. Cell shrinkage induces a greater activation of Na/H exchange and Na-K-2Cl cotransport in 4.2(-/-) RBCs compared with controls. The increased passive Na+ permeability of 4.2(-/-) RBCs is also dependent on cell shrinkage. We conclude that protein 4.2 is important in the maintenance of normal surface area in RBCs and for normal RBC cation transport.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359562-127037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359562-1284644,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10359562-9516379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359562-9927493
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9738
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pubmed:author |
pubmed-author:BrugnaraCC,
pubmed-author:ChoM RMR,
pubmed-author:CohenC MCM,
pubmed-author:GomesE FEF,
pubmed-author:GwynnBB,
pubmed-author:JindelH KHK,
pubmed-author:JohnK MKM,
pubmed-author:KorsgrenCC,
pubmed-author:LuxS ESE,
pubmed-author:MohandasNN,
pubmed-author:PetersL LLL
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pubmed:issnType |
Print
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pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1527-37
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pubmed:dateRevised |
2011-6-20
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pubmed:meshHeading |
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