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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
1998-12-14
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pubmed:abstractText |
The erythrocyte membrane cytoskeletal protein 4.1 (4.1R) is a structural protein that confers stability and flexibility to erythrocytes via interactions with the cytoskeletal proteins spectrin and F-actin and with the band 3 and glycophorin C membrane proteins. Mutations in 4.1R can cause hereditary elliptocytosis, a disease characterized by a loss of the normal discoid morphology of erythrocytes, resulting in hemolytic anemia [1]. Different isoforms of the 4.1 protein have been identified in a wide variety of nonerythroid tissues by immunological methods [2-5]. The variation in molecular weight of these different 4.1 isoforms, which range from 30 to 210 kDa [6], has been attributed to complex alternative splicing of the 4.1R gene [7]. We recently identified two new 4.1 genes: one is generally expressed throughout the body (4. 1G) [8] and the other is expressed in central and peripheral neurons (4.1N) [9]. Here, we examined 4.1R expression by in situ hybridization analysis and found that 4.1R was selectively expressed in hematopoietic tissues and in specific neuronal populations. In the brain, high levels of 4.1R were discretely localized to granule cells in the cerebellum and dentate gyrus. We generated mice that lacked 4.1R expression; these mice had deficits in movement, coordination, balance and learning, in addition to the predicted hematological abnormalities. The neurobehavioral findings are consistent with the distribution of 4.1R in the brain, suggesting that 4.1R performs specific functions in the central nervous system.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane band 4.1...,
http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte membrane protein band...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0960-9822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1269-72
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pubmed:dateRevised |
2011-6-20
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pubmed:meshHeading |
pubmed-meshheading:9822582-Animals,
pubmed-meshheading:9822582-Brain,
pubmed-meshheading:9822582-Cytoskeletal Proteins,
pubmed-meshheading:9822582-Erythrocyte Membrane,
pubmed-meshheading:9822582-Female,
pubmed-meshheading:9822582-Gene Deletion,
pubmed-meshheading:9822582-Learning Disorders,
pubmed-meshheading:9822582-Membrane Proteins,
pubmed-meshheading:9822582-Mice,
pubmed-meshheading:9822582-Nervous System Diseases,
pubmed-meshheading:9822582-Neuropeptides,
pubmed-meshheading:9822582-Psychomotor Performance
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pubmed:year |
1998
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pubmed:articleTitle |
Neurobehavioral deficits in mice lacking the erythrocyte membrane cytoskeletal protein 4.1.
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pubmed:affiliation |
Department of Neuroscience The Johns Hopkins School of Medicine Baltimore, Maryland 21205, USA.
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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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