|
|
 Previous Article | Table of Contents | Next Article 
Hereditary elliptocytosis due to both qualitative and quantitative defects
in membrane skeletal protein 4.1
JG Conboy, R Shitamoto, M Parra, R Winardi, A Kabra, J Smith and N Mohandas
Lawrence Berkeley Laboratory, University of California, Berkeley 94720.
Protein 4.1 is an important structural component of the membrane skeleton
that helps determine erythrocyte morphology and membrane mechanical
properties. In a previous study we identified a case of human hereditary
elliptocytosis (HE) in which decreased membrane mechanical stability was
due to deletion of 80 amino acids encompassing the entire 10-Kd
spectrin-actin binding domain. A portion of this domain (21 amino acids) is
encoded by an alternatively spliced exon that is expressed in late but not
early erythroid cells. We now report a case of canine HE in which the
abnormal phenotype is caused by failure to express this alternative peptide
in the mature red blood cell (RBC) membrane skeleton, in conjunction with
quantitative deficiency of protein 4.1. Western blotting of RBC membranes
from a dog with HE showed a truncated protein 4.1 that did not react with
antibodies directed against the alternative peptide. In addition,
sequencing of cloned reticulocyte protein 4.1 cDNA showed a precise
deletion of 63 nucleotides comprising this exon. Normal dog reticulocytes
did express this exon. Expression of this 21 amino acid peptide during
erythroid maturation is therefore essential for proper assembly of a
mechanically competent membrane skeleton, because RBCs lacking this peptide
have unstable membranes.
Volume 78,
Issue 9,
pp. 2438-2443,
11/01/1991
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:
|
|
|
|
 
X. Pei, X. Guo, R. Coppel, N. Mohandas, and X. An
Plasmodium falciparum Erythrocyte Membrane Protein 3 (PfEMP3) Destabilizes Erythrocyte Membrane Skeleton
J. Biol. Chem.,
September 14, 2007;
282(37):
26754 - 26758.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
V. Bennett and A. J. Baines
Spectrin and Ankyrin-Based Pathways: Metazoan Inventions for Integrating Cells Into Tissues
Physiol Rev,
July 1, 2001;
81(3):
1353 - 1392.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. L. Gee, K. Aoyagi, R. Lersch, V. Hou, M. Wu, and J. G. Conboy
Alternative splicing of protein 4.1R exon 16: ordered excision of flanking introns ensures proper splice site choice
Blood,
January 15, 2000;
95(2):
692 - 699.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Ye, D. A. Compton, M. M. Lai, L. D. Walensky, and S. H. Snyder
Protein 4.1N Binding to Nuclear Mitotic Apparatus Protein in PC12 Cells Mediates the Antiproliferative Actions of Nerve Growth Factor
J. Neurosci.,
December 15, 1999;
19(24):
10747 - 10756.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. D. Walensky, P. Gascard, M. E. Field, S. Blackshaw, J. G. Conboy, N. Mohandas, and S. H. Snyder
The 13-kD FK506 Binding Protein, FKBP13, Interacts with a Novel Homologue of the Erythrocyte Membrane Cytoskeletal Protein 4.1
J. Cell Biol.,
April 6, 1998;
141(1):
143 - 153.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Fehon, I. Dawson, and S Artavanis-Tsakonas
A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene
Development,
January 3, 1994;
120(3):
545 - 557.
[Abstract]
[PDF]
|
|
|
|
|
