| First Author | Jones GL | Year | 1990 |
| Journal | Biochim Biophys Acta | Volume | 1096 |
| Issue | 1 | Pages | 33-40 |
| PubMed ID | 2268683 | Mgi Jnum | J:47395 |
| Mgi Id | MGI:1203386 | Doi | 10.1016/0925-4439(90)90009-e |
| Citation | Jones GL, et al. (1990) Human erythrocyte Band-3 has an altered N terminus in malaria-resistant Melanesian ovalocytosis. Biochim Biophys Acta 1096(1):33-40 |
| abstractText | There is a high prevalence of the erythrocyte polymorphism ovalocytosis associated with reduced susceptibility to malaria in Papua New Guinea. The major erythrocyte integral membrane protein, Band-3, showed markedly increased phosphorylation in whole cells or isolated ghosts from ovalocytic individuals. The cytoplasmic domain of the ovalocyte Band-3 was found to be approx. 3 kDa larger than the normocytic protein. The N-terminal sequence of the ovalocytic Band-3 was different from the reported sequence for human Band-3, suggesting that the increased size results from an N-terminal extension. Since this is the region of Band-3 which is phosphorylated and interacts with the red cell cytoskeleton, it is likely that this alteration in ovalocytic Band-3 is the underlying cause of the diverse alterations in ovalocytic cells including increased phosphorylation, increased membrane rigidity, decreased agglutinability by blood group antibodies and refractoriness to invasion by malarial parasites. |
