http://purl.uniprot.org/citations/16774987 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16774987 | http://www.w3.org/2000/01/rdf-schema#comment | "Moderate hemolytic anemia, abnormal erythrocyte morphology (spherocytosis), and decreased membrane stability are observed in mice with complete deficiency of all erythroid protein 4.1 protein isoforms (4.1(-/-); Shi TS et al. J Clin Invest 103: 331, 1999). We have examined the effects of erythroid protein 4.1 (4.1R) deficiency on erythrocyte cation transport and volume regulation. 4.1(-/-) mice exhibited erythrocyte dehydration that was associated with reduced cellular K and increased Na content. Increased Na permeability was observed in these mice, mostly mediated by Na/H exchange with normal Na-K pump and Na-K-2Cl cotransport activities. The Na/H exchange of 4.1(-/-) erythrocytes was markedly activated by exposure to hypertonic conditions (18.2 +/-3.2 in 4.1(-/-) vs. 9.8 +/-1.3 mmol/10(13) cell x h in control mice), with an abnormal dependence on osmolality (EC(50) = 417 +/- 42 in 4.1(-/-) vs. 460 +/-35 mosmol/kgH(2)O in control mice), suggestive of an upregulated functional state. While the affinity for internal protons was not altered (K(0.5) = 489.7 +/- 0.7 vs. 537.0 +/-0.56 nM in control mice), the V(max) of the H-induced Na/H exchange activity was markedly elevated in 4.1(-/-) erythrocytes (V(max) 91.47 +/-7.2 compared with 46.52 +/-5.4 mmol/10(13) cell x h in control mice). Na/H exchange activation by okadaic acid was absent in 4.1(-/-) erythrocytes. Altogether, these results suggest that erythroid protein 4.1 plays a major role in volume regulation and physiologically downregulates Na/H exchange in mouse erythrocytes. Upregulation of the Na/H exchange is an important contributor to the elevated cell Na content of 4.1(-/-) erythrocytes."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpcell.00436.2005"xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "Mohandas N."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "Rivera A."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "Brugnara C."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "De Franceschi L."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "Peters L.L."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/author | "Gascard P."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/name | "Am J Physiol Cell Physiol"xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/pages | "C880-6"xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/title | "Effect of complete protein 4.1R deficiency on ion transport properties of murine erythrocytes."xsd:string |
http://purl.uniprot.org/citations/16774987 | http://purl.uniprot.org/core/volume | "291"xsd:string |
http://purl.uniprot.org/citations/16774987 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16774987 |
http://purl.uniprot.org/citations/16774987 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16774987 |
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