Structural and Biochemical Analysis of the McLeod Erythrocyte Membrane

Abstract. The abnormal erythrocyte of the McLeod phenotype displays a reduced Kell blood group expression, an abnormal morphology in about 30% of the total red blood cell population and a decrease in water permeability. These parameters have previously been shown to be independent of membrane lipid composition, microviscosity and electrolyte transport. Findings such as these seem to implicate the involvement of a defective membrane protein. The present study investigated membrane composition by utilizing two techniques: freeze‐fracture electron microscopy and discontinuous polyacrylamide gel electrophoresis. Electrophoretic scans revealed no apparent band additions or deletions showing McLeod membrane protein composition to be normal. Freeze‐fracture electron microscopy did show a significant increase in intramembrane particle density. These findings may be resolved by proposing a dissociation of the band 3 glycoprotein. Unlinkage of this polypeptide, thought to be involved in water transport and intramembranous particle composition, could account for the decreased water transport and increased particle density seen in the McLeod erythrocyte membrane.

[1]  W. Galey,et al.  Morphology and Physiology of the McLeod Erythrocyte , 1978 .

[2]  A. Evan,et al.  Morphology and physiology of the McLeod erythrocyte. I. Scanning electron microscopy and electrolyte and water transport properties. , 1978, Vox sanguinis.

[3]  W. Galey,et al.  Haematological Changes Associated with the McLeod Phenotype of the Kell Blood Group System , 1977, British journal of haematology.

[4]  M. Tanner,et al.  Freeze-fracture electron microscopy of human erythrocytes lacking the major membrane sialoglycoprotein. , 1977, Biochimica et biophysica acta.

[5]  M. Nichols,et al.  Kx Antigen, The McLeod Phenotype, and Chronic Granulomatous Disease: Further Studies 1 , 1976, Vox sanguinis.

[6]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[7]  S. Douglas,et al.  Antigens of the Kell blood group system on neutrophils and monocytes: their relation to chronic granulomatous disease. , 1975, The Journal of pediatrics.

[8]  R. Sha’afi,et al.  Membrane proteins related to water transport in human erythrocytes , 1975, Nature.

[9]  J. Segrest,et al.  The effects of the membrane-penetrating polypeptide segment of the human erythrocyte MN-glycoprotein on the permeability of model lipid membranes. , 1975, Biochimica et biophysica acta.

[10]  T. Steck THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE , 1974, The Journal of cell biology.

[11]  P. Naccache,et al.  Effect of PCMBS on water transfer across biological membranes , 1974, Journal of cellular physiology.

[12]  D. Neville,et al.  Molecular weight determination of membrane protein and glycoprotein subunits by discontinuous gel electrophoresis in dodecyl sulfate. , 1974, Methods in enzymology.

[13]  T. Steck Cross-linking the major proteins of the isolated erythrocyte membrane. , 1972, Journal of molecular biology.

[14]  S. Pincus,et al.  Kell phenotypes in chronic granulomatous disease: a potential trnsfusion hazard. , 1971, Lancet.

[15]  E. Lonergan,et al.  SPUR-CELL ANEMIA: HEMOLYTIC ANEMIA WITH RED CELLS RESEMBLING ACANTHOCYTES IN ALCOHOLIC CIRRHOSIS. , 1964, The New England journal of medicine.

[16]  F H ALLEN,et al.  A New Phenotype (McLeod) in the Kell Blood‐group System * , 1961, Vox sanguinis.

[17]  H. Fudenberg,et al.  Studies of Anti‐Kpb, a New Antibody in the Kell Blood Group System * , 1958, Vox sanguinis.