| First Author | Goodman SR | Year | 1982 |
| Journal | Blood | Volume | 60 |
| Issue | 3 | Pages | 772-84 |
| PubMed ID | 7104494 | Mgi Jnum | J:47957 |
| Mgi Id | MGI:1261361 | Doi | 10.1182/blood.v60.3.772.bloodjournal603772 |
| Citation | Goodman SR, et al. (1982) Identification of the molecular defect in the erythrocyte membrane skeleton of some kindreds with hereditary spherocytosis. Blood 60(3):772-84 |
| abstractText | We have localized the molecular alteration in the membrane skeleton of two of four kindreds with hereditary spherocytosis (HS) to an alteration in the spectrin-protein-4.1 interaction due to a defective spectrin molecule. The defective spectrin-protein-4.1 interaction in these kindreds (referred to as type I HS) leads to a weakened spectrin-protein-4.1-actin ternary complex, which in turn may lead to the friable membrane skeleton and suggested membrane instability related to this disorder. Type I HS spectrin binds approximately 63% as much protein-4.1 as normal spectrin (with equal affinity). This defect does not correlate with splenic function or erythrocyte age in the circulation. However, the approximately 37% reduction in binding of protein-4.1 to HS spectrin approaches the theoretical value of 50% expected in this autosomal dominant disorder. All other type I membrane skeletal interactions (spectrin-syndein, spectrin heterodimer- heterodimer, syndein-band-3) were found to be normal. It would appear therefore that the defective HS spectrin-protein-4.1 interaction in type I hereditary spherocytosis may be the primary molecular defect rather than a secondary phenomena. |
