onr:"swepub:oai:DiVA.org:umu-82575"
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03482naa a2200397 4500 | |
| 001 | oai:DiVA.org:umu-82575 | |
| 003 | SwePub | |
| 008 | 131105s2002 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-825752 URI |
| 024 | 7 | a https://doi.org/10.1182/blood-2002-03-07062 DOI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Bruce, Lesley J4 aut |
| 245 | 1 0 | a Absence of CD47 in protein 4.2-deficient hereditary spherocytosis in man :b an interaction between the Rh complex and the band 3 complex. |
| 264 | c 2002-05-13 | |
| 264 | 1 | b American Society of Hematology,c 2002 |
| 338 | a print2 rdacarrier | |
| 520 | a We present data on a patient of South Asian origin with recessive hereditary spherocytosis (HS) due to absence of protein 4.2 [4.2 (-) HS]. Protein 4.2 cDNA sequence analysis showed the presence of a novel 41-bp frameshift deletion that predicts a truncated peptide designated protein 4.2 Hammersmith. Quantitative reverse transcription-polymerase chain reaction indicated that the mutant mRNA was unstable. Sequencing of protein 4.2 genomic DNA revealed that the deletion stems from aberrant splicing. The proband was homozygous for a G>T substitution at position 1747 (cDNA numbering) that activates a cryptic acceptor splice site within exon 11 of the protein 4.2 gene (EPB42). The proband's mother was found to be heterozygous for this substitution. Unlike protein 4.2 null mice, the proband's red cells showed no evidence for abnormal cation permeability. Quantitation of red cell membrane proteins was carried out by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting, and flow cytometric measurement. CD47, a protein associated with the Rh complex, was markedly reduced to about 1% (in the proband) and 65% (in the mother) that found in healthy controls. The Rh-associated glycoprotein migrated with a higher than normal apparent molecular weight on SDS-PAGE. There was no obvious reduction in Rh polypeptides. These observations indicate that protein 4.2 and CD47 interact in the human red cell membrane. They provide further evidence for an association between the band 3 complex (band 3, ankyrin, protein 4.2, glycophorin A) and the Rh complex (Rh-associated glycoprotein, Rh polypeptides, glycophorin B, CD47, LW) and define a point of attachment between the Rh complex and the red cell cytoskeleton. | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaper0 (SwePub)3012 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicine0 (SwePub)3012 hsv//eng |
| 700 | 1 | a Ghosh, Sandip4 aut |
| 700 | 1 | a King, May Jean4 aut |
| 700 | 1 | a Layton, D Mark4 aut |
| 700 | 1 | a Mawby, William J4 aut |
| 700 | 1 | a Stewart, Gordon W4 aut |
| 700 | 1 | a Oldenborg, Per-Arneu Umeå universitet,Histologi med cellbiologi4 aut0 (Swepub:umu)peol0001 |
| 700 | 1 | a Delaunay, Jean4 aut |
| 700 | 1 | a Tanner, Michael J A4 aut |
| 710 | 2 | a Umeå universitetb Histologi med cellbiologi4 org |
| 773 | 0 | t Bloodd : American Society of Hematologyg 100:5, s. 1878-1885q 100:5<1878-1885x 0006-4971x 1528-0020 |
| 856 | 4 | u https://ashpublications.org/blood/article-pdf/100/5/1878/1254035/h81702001878.pdf |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-82575 |
| 856 | 4 8 | u https://doi.org/10.1182/blood-2002-03-0706 |
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