Summary
A 17-year-old patient with mild hemolytic anemia known since early childhood displayed an aberrant protein pattern of his red cell membranes when analyzed in SDS-polyacrylamide gel electrophoresis (SDS-PAGE). A double protein band in the low molecular weight region (molecular weight of about 33,000) was distinctly reduced or missing in the membranes that were investigated concomitantly with those of controls on two occasions at an interval of 6 months'. The phosphorylation pattern of membrane phosphoproteins, on the other hand, did not seem to differ from that of controls. It is suggested that a causal relationship existed between the observed membrane abnormality and the mild hemolytic anemia.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Agre P, Orringer EP, Bennet V (1982) Deficient red cell spectrin in severe, recessively inherited spherocytosis. N Engl J Med 306: 1155–1161
Bennett V (1982) The molecular basis for membrane cytoskeleton association in human erythrocytes. J Cell Biochem 18: 49–65
Bennett V, Stenbuck PJ (1979) Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J Biol Chem 254: 2533–2541
Bennett V, Stenbuck PJ (1980) Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane. J Biol Chem 255: 6424–6432
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254
Branton D, Cohen CM, Tyler J (1981) Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell 24: 24–32
Cohen CM, Branton D (1981) The normal and abnormal red cell cytoskeleton: a renewed search for molecular defects. Trends Biochem Sci 6: 266–268
Hargreaves WR, Giedd KN, Verkleij A, Branton D (1980) Reassociation of ankyrin with band 3 in erythrocyte membranes and lipid vesicles. J Biol Chem 255: 11965–11972
Humble E, Berglund L, Titanji V, Ljungström O, Edlund B, Zetterqvist Ö, Engström L (1975) Non dependence on native structure of pig liver pyruvate kinase when used as a substrate for cyclic 3', 5' AMP-stimulated protein kinase. Biochem Biophys Res Commun 66: 614–621
Kant JA, Steck TL (1973) Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes. J Biol Chem 248: 8457–8464
Lux SE (1979) Spectrin-actin membrane skeleton of normal and abnormal red blood cells. Semin Hematol 16: 21–51
Nilsson O, Ronquist G (1969) Enzyme activities and ultrastructure of a membrane fraction from human erythrocytes. Biochim Biophys Acta 183: 1–9
O'Farrell PH (1974) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007–4021
Ronquist G (1967) Formation of adenosine triphosphate by a membrane fraction from human erythrocytes. Acta Chem Scand 21: 1484–1494
Ronquist G (1969) Enzyme activities at the surface of intact human erythrocytes. Acta Physiol Scand 76: 312–320
Ronquist G, Ågren G (1966) Formation of adenosine triphosphate by human erythrocyte ghosts. Nature 209: 1091–1092
Ronquist G, Ågren G (1975) An Mg2+ - and Ca2+-stimulated adenosine triphosphatase at the outer surface of Ehrlich ascites tumor cells. Cancer Res 35: 1402–1406
Shin BC, Carraway KJ (1973) Association of glyceraldehyde 3-phosphate dehydrogenase with the human erythrocyte membrane. J Biol Chem 248: 1436–1444
Shohet SB, Greenquist AC (1977) Possible roles for membrane protein phosphorylation in the control of erythrocyte shape. Blood Cells 3: 115–133
Shotton DM, Burke BE, Branton D (1979) The molecular structure of human erythrocyte spectrin: biophysical and electron microscopic studies. J Mol Biol 131: 303–329
Tchernia G, Mohandas N, Shohet SB (1981) Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis: implications for erythrocyte membrane stability. J Clin Invest 68: 454–460
Tyler JM, Hargreaves WR, Branton D (1979) Purification of two spectrin-binding proteins: biochemical and electron microscope evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Proc Natl Acad Sci USA 76: 5192–5196
Yu J, Goodman SR (1979) Syndeins: the spectrin-binding proteins of the human erythrocyte membrane. Proc Natl Acad Sci USA 76: 2340–2344
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ronquist, G., Edlund, B., Frithz, G. et al. Aberrant protein pattern in red cell membranes of a patient with mild hemolytic anemia. Blut 52, 9–15 (1986). https://doi.org/10.1007/BF00320137
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00320137