Spontaneous, reversible protein cross-linking in the human erythrocyte membrane. Temperature and pH dependence.

Changes in pH significantly affect the morphology and physical properties of red cell membranes. We have explored the molecular basis for these phenomena by characterizing the pattern of protein disulfide cross-linkages formed spontaneously in ghost exposed to acid pH or elevated temperature (37 degrees C). Protein aggregation was analyzed by two-dimensional polyacrylamide gel electrophoresis in sodium dodecyl sulfate. incubation of ghosts at pH 4.0 to 5.5 (0-4 degrees C) yielded (i) complexes of spectrin and band 3, (ii) complexes of actin and band 3, (iii) band 3 complexes, i.e. dimer and trimer, and (iv) heterogeneous aggregates involving spectrin, band 3, band 4.2, and actin in varying proportions. Aggregation was maximal near the isoelectric points of the major membrane proteins, and appeared to reflect (i) the aggregation of intramembrane particles including band 3 and (ii) more intimate contact between spectrin-actin meshwork and band 3.

[1]  D. Branton,et al.  Reconstitution of intramembrane particles in recombinants of erythrocyte protein band 3 and lipid: effects of spectrin-actin association. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[2]  F. Kirkpatrick.  Spectrin: current understanding of its physical, biochemical, and functional properties. , 1976, Life sciences.

[3]  C. Tanford,et al.  Erythrocyte spectrin. Purification in deoxycholate and preliminary characterization. , 1976, Biochemistry.

[4]  T. Steck,et al.  Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membrane. , 1976, Biochemistry.

[5]  D. Branton,et al.  Intramembrane particle aggregation in erythrocyte ghosts. II. The influence of spectrin aggregation. , 1976, Biochimica et biophysica acta.

[6]  J. Pinder,et al.  Actin polymerisation induced by spectrin , 1975, Nature.

[7]  W. Gratzer,et al.  Properties of the high-molecular-weight protein (spectrin) from human-erythrocyte membranes. , 1975, European journal of biochemistry.

[8]  P. Detmers,et al.  Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ , 1975, The Journal of cell biology.

[9]  F. Richards,et al.  Reaction of dimethyl-3,3'-dithiobispropionimidate with intact human erythrocytes. Cross-linking of membrane proteins and hemoglobin. , 1975, The Journal of biological chemistry.

[10]  J. Avruch,et al.  Phosphorylation of endogenous substrates by erythrocyte membrane protein kinases. I. A monovalent cation-stimulated reaction. , 1974, Biochemistry.

[11]  F. Richards,et al.  An approach to nearest neighbor analysis of membrane proteins. Application to the human erythrocyte membrane of a method employing cleavable cross-linkages. , 1974, The Journal of biological chemistry.

[12]  D. Branton,et al.  INTRAMEMBRANE PARTICLE AGGREGATION IN ERYTHROCYTE GHOSTS , 1974, The Journal of cell biology.

[13]  M. Morazzani,et al.  Evidence for multiple polypeptide chains in the membrane protein spectrin. , 1974, Biochemistry.

[14]  G. Nicolson,et al.  Lectin binding and perturbation of the outer surface of the cell membrane induces a transmembrane organizational alteration at the inner surface. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[15]  S. Bhakdi,et al.  Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate , 1974 .

[16]  G. Nicolson,et al.  ANIONIC SITES OF HUMAN ERYTHROCYTE MEMBRANES , 1973, The Journal of cell biology.

[17]  F. Studier,et al.  Analysis of bacteriophage T7 early RNAs and proteins on slab gels. , 1973, Journal of molecular biology.

[18]  H. Fudenberg,et al.  Anionic sites on the membrane intercalated particles of human erythrocyte ghost membranes. Freeze-etch localization. , 1973, Experimental cell research.

[19]  Y. Yawata,et al.  Abnormal red cell metabolism causing hemolysis in uremia. A defect potentiated by tap water hemodialysis. , 1973, Annals of internal medicine.

[20]  G. Nicolson.  ANIONIC SITES OF HUMAN ERYTHROCYTE MEMBRANES , 1973, The Journal of cell biology.

[21]  O. Rosen,et al.  The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes. , 1973, Biochemical and biophysical research communications.

[22]  M. Inouye,et al.  The assembly of a structural lipoprotein in the envelope of Escherichia coli. , 1972, The Journal of biological chemistry.

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

[24]  D. Wallach,et al.  Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. , 1971, Biochemistry.

[25]  A. Rothstein.  Sulfhydryl groups in red cell membranes. , 1971, Experimental eye research.

[26]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[27]  E. Beutler.  Genetic disorders of red cell metabolism. , 1969, The Medical clinics of North America.

[28]  A. C. Peacock,et al.  Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. , 1968, Biochemistry.

[29]  H. Jacob,et al.  Effects of sulfhydryl inhibition on red blood cells. I. Mechanism of hemolysis. , 1962, The Journal of clinical investigation.

[30]  B. Chailley,et al.  Calcium-pH Interactions in the Production of Shape Change in Erythrocytes , 1973 .