|
|
 Previous Article | Table of Contents | Next Article 
Identification of a functional role for human erythrocyte
sialoglycoproteins beta and gamma
ME Reid, JA Chasis and N Mohandas
Four distinct erythrocyte membrane sialoglycoproteins (SGPs) denoted alpha,
beta, gamma, and delta have been described, but their functions have not
yet been defined. Recent evidence suggests that several of these SGPs
associate with membrane skeletal proteins. Because the membrane skeletal
protein network plays an important role in regulating the membrane material
properties of deformability and mechanical stability, we wanted to
determine whether the SGPs, through their interaction with the membrane
skeleton, can modulate these membrane properties. We measured membrane
mechanical stability and membrane deformability of erythrocytes that were
deficient in either alpha, or delta or beta and gamma SGPs. Only
erythrocytes deficient in beta and gamma SGP had altered membrane
properties, as evidenced by marked decreases in both membrane mechanical
stability (50% of normal) and membrane deformability (40% of normal).
Erythrocytes deficient in either alpha or delta SGP had normal
deformability and stability. Based on these data, we suggest that an
interaction of beta and/or gamma SGP with the membrane skeleton plays a
functionally important role in regulating normal erythrocyte membrane
properties.
Volume 69,
Issue 4,
pp. 1068-1072,
04/01/1987
Copyright © 1987 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
G. Rank, R. Sutton, V. Marshall, R. J. Lundie, J. Caddy, T. Romeo, K. Fernandez, M. P. McCormack, B. M. Cooke, S. J. Foote, et al.
Novel roles for erythroid Ankyrin-1 revealed through an ENU-induced null mouse mutant
Blood,
April 2, 2009;
113(14):
3352 - 3362.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. L. Peters, R. A. Swearingen, S. G. Andersen, B. Gwynn, A. J. Lambert, R. Li, S. E. Lux, and G. A. Churchill
Identification of quantitative trait loci that modify the severity of hereditary spherocytosis in wan, a new mouse model of band-3 deficiency
Blood,
April 15, 2004;
103(8):
3233 - 3240.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
H. M. Van Dort, D. W. Knowles, J. A. Chasis, G. Lee, N. Mohandas, and P. S. Low
Analysis of Integral Membrane Protein Contributions to the Deformability and Stability of the Human Erythrocyte Membrane
J. Biol. Chem.,
December 7, 2001;
276(50):
46968 - 46974.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. M. Marfatia, J. H. Morais-Cabral, A. C. Kim, O. Byron, and A. H. Chishti
The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C. ANALYSIS OF THE BINDING INTERFACE BY IN VITRO MUTAGENESIS
J. Biol. Chem.,
September 26, 1997;
272(39):
24191 - 24197.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. M. Marfatia, R. A. Lue, D. Branton, and A. H. Chishti
Identification of the Protein 4.1 Binding Interface on Glycophorin C and p55, a Homologue of the Drosophila discs-large Tumor Suppressor Protein
J. Biol. Chem.,
January 13, 1995;
270(2):
715 - 719.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. H. Chang and P. S. Low
Regulation of the Glycophorin C-Protein 4.1 Membrane-to-Skeleton Bridge and Evaluation of Its Contribution to Erythrocyte Membrane Stability
J. Biol. Chem.,
June 15, 2001;
276(25):
22223 - 22230.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
