Elliptocytosis-associated spectrin Rouen (beta 220/218) has a truncated but still phosphorylatable beta chain

• Published in: British journal of haematology Vol. 80; no. 2; p. 242
• Main Authors: Lecomte, M C, Gautero, H, Bournier, O, Galand, C, Lahary, A, Vannier, J P, Garbarz, M, Delaunay, J, Tchernia, G, Boivin, P
• Format: Journal Article
• Language: English
• Published: England 01-02-1992
• Subjects: Electrophoresis, Polyacrylamide Gel; Elliptocytosis, Hereditary - blood; Elliptocytosis, Hereditary - genetics; Erythrocyte Deformability - physiology; Hot Temperature; Humans; Pedigree; Phosphorylation; Spectrin - chemistry; Spectrin - isolation & purification; Trypsin
• ISSN: 0007-1048
• DOI: 10.1111/j.1365-2141.1992.tb08907.x

Spectrin Rouen (beta 220/218) is a novel variant, carrying a shortened beta chain with an apparent molecular weight of 218 kDa. It was detected in a French family. All affected members suffered from haemolytic hereditary elliptocytosis. As other shortened beta chain variants described before, the beta Rouen chain is truncated at its carboxyl terminus. Spectrin Rouen is associated with a defect in spectrin dimer self-association and with an abnormally high amount of the alpha I 74 kDa peptide following partial tryptic digestion. Dimer reconstitution experiments from normal and abnormal purified Sp subunits indicated that the increased alpha I 74 kDa fragment is induced by the altered beta chain. However, spectrin Rouen is different from other mutants with a truncated beta chain in several respects: its amount is low (less than 10%) and the spectrin dimer self-associated defect is mild. Critically, the beta Rouen chain has retained the ability of undergoing phosphorylation, even though it is modified in its C-terminal region. These results, compared to those obtained with beta 220/214 spectrin Le Puy and beta 220/216 spectrin Nice, allowed better localization of the beta chain sites that can be phosphorylated by a membrane-bound casein kinase.