|
|
Previous Article | Table of Contents | Next Article 
Contribution of the band 3-ankyrin interaction to erythrocyte membrane
mechanical stability
PS Low, BM Willardson, N Mohandas, M Rossi and S Shohet
Department of Chemistry, Purdue University, West Lafayette, IN 47907- 1393.
In an effort to evaluate the role of the band 3-ankyrin linkage in
maintenance of red blood cell membrane integrity, solution conditions were
sought that would selectively dissociate the band 3-ankyrin linkage,
leaving other membrane skeletal interactions intact. For this purpose
erythrocytes were equilibrated overnight in nutrient-containing buffers at
a range of elevated pHs and then examined for changes in mechanical
stability and membrane skeletal composition. Band 3 was found to be
released from interaction with the membrane skeleton over a pH range (8.4
to 9.5) that was observed to dissociate the band 3- ankyrin interaction in
vitro. In contrast, all other membrane skeletal associations appeared to
remain intact up to pH 9.3, after which they were also seen to dissociate.
Whereas hemolysis of mechanically unstressed cells did not begin until
approximately pH 9.3, where the membrane skeletons began to disintegrate,
enhanced fragmentation of shear stressed membranes was seen to begin near
pH 8, where band 3 dissociation was first observed. Furthermore, the
shear-induced fragmentation rate was found to reach a maximum at pH 9.4,
ie, where band 3 dissociation was essentially complete. Based on these
correlations, we hypothesize that the band 3-ankyrin linkage of the
membrane skeleton to the lipid bilayer is essential for red blood cell
stability in the face of mechanical distortion but not for cellular
integrity in the absence of mechanical stress.
Volume 77,
Issue 7,
pp. 1581-1586,
04/01/1991
Copyright © 1991 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:

|
 |

|
 |
 
B. V. Alvarez, D. M. Kieller, A. L. Quon, M. Robertson, and J. R. Casey
Cardiac hypertrophy in anion exchanger 1-null mutant mice with severe hemolytic anemia
Am J Physiol Heart Circ Physiol,
March 1, 2007;
292(3):
H1301 - H1312.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Ito, I. Koshino, N. Arashiki, H. Adachi, M. Tomihari, S. Tamahara, K. Kurogi, T. Amano, K.-i. Ono, and M. Inaba
Ubiquitylation-independent ER-associated degradation of an AE1 mutant associated with dominant hereditary spherocytosis in cattle
J. Cell Sci.,
September 1, 2006;
119(17):
3602 - 3612.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Brochard-Wyart, N. Borghi, D. Cuvelier, and P. Nassoy
Hydrodynamic narrowing of tubes extruded from cells
PNAS,
May 16, 2006;
103(20):
7660 - 7663.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. Pushkin and I. Kurtz
SLC4 base (HCO3-, CO32-) transporters: classification, function, structure, genetic diseases, and knockout models
Am J Physiol Renal Physiol,
March 1, 2006;
290(3):
F580 - F599.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
T. Tiffert, V. L. Lew, H. Ginsburg, M. Krugliak, L. Croisille, and N. Mohandas
The hydration state of human red blood cells and their susceptibility to invasion by Plasmodium falciparum
Blood,
June 15, 2005;
105(12):
4853 - 4860.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Mandal, V. Baudin-Creuza, A. Bhattacharyya, S. Pathak, J. Delaunay, M. Kundu, and J. Basu
Caspase 3-mediated Proteolysis of the N-terminal Cytoplasmic Domain of the Human Erythroid Anion Exchanger 1 (Band 3)
J. Biol. Chem.,
December 26, 2003;
278(52):
52551 - 52558.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Bordin, A. M. Brunati, A. Donella-Deana, B. Baggio, A. Toninello, and G. Clari
Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes
Blood,
June 17, 2002;
100(1):
276 - 282.
[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]
|
 |
|

|
 |

|
 |
 
D. Zhang, A. Kiyatkin, J. T. Bolin, and P. S. Low
Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
Blood,
November 1, 2000;
96(9):
2925 - 2933.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. C. Wang, M. Tao, T. Wei, and P. S. Low
Identification of the Major Casein Kinase I Phosphorylation Sites on Erythrocyte Band 3
Blood,
April 15, 1997;
89(8):
3019 - 3024.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
X.-L. An, Y. Takakuwa, W. Nunomura, S. Manno, and N. Mohandas
Modulation of Band 3-Ankyrin Interaction by Protein 4.1. FUNCTIONAL IMPLICATIONS IN REGULATION OF ERYTHROCYTE MEMBRANE MECHANICAL PROPERTIES
J. Biol. Chem.,
December 27, 1996;
271(52):
33187 - 33191.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. C. Wang, R. Moriyama, C. R. Lombardo, and P. S. Low
Partial Characterization of the Cytoplasmic Domain of Human Kidney Band 3
J. Biol. Chem.,
July 28, 1995;
270(30):
17892 - 17897.
[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]
|
 |
|

|
 |

|
 |
 
J. Zhou and P. S. Low
Characterization of the Reversible Conformational Equilibrium in the Cytoplasmic Domain of Human Erythrocyte Membrane Band 3
J. Biol. Chem.,
October 5, 2001;
276(41):
38147 - 38151.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. Manno, Y. Takakuwa, and N. Mohandas
Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
PNAS,
February 19, 2002;
99(4):
1943 - 1948.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|