scholarly journals Hereditary elliptocytosis with protein band 4.1 deficiency in the dog

Blood ◽  
1983 ◽  
Vol 61 (2) ◽  
pp. 373-377 ◽  
Author(s):  
JE Smith ◽  
K Moore ◽  
M Arens ◽  
GA Rinderknecht ◽  
A Ledet
Keyword(s):  
Animal Model ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Erythrocyte Deformability ◽  
Membrane Stability ◽  
Osmotic Sensitivity ◽  
Hereditary Elliptocytosis ◽  
Membrane Cytoskeleton ◽  
Glutathione Deficiency

Abstract A dog with persistent elliptocytosis was studied. The dog had membrane protein band 4.1 deficiency, microcytosis, shortened erythrocyte lifespan, increased osmotic sensitivity, and a mild glutathione deficiency. Erythrocyte deformability and membrane stability were adversely effected. The dog's parents had decreased band 4.1, decreased stability, and some elliptocytosis. This disorder in dogs closely resembles human patients with band 4.1 deficiency and should provide a valuable animal model to study the erythrocyte membrane cytoskeleton.

scholarly journals Hereditary elliptocytosis with protein band 4.1 deficiency in the dog

Blood ◽  
1983 ◽  
Vol 61 (2) ◽  
pp. 373-377
Author(s):  
JE Smith ◽  
K Moore ◽  
M Arens ◽  
GA Rinderknecht ◽  
A Ledet
Keyword(s):  
Animal Model ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Erythrocyte Deformability ◽  
Membrane Stability ◽  
Osmotic Sensitivity ◽  
Hereditary Elliptocytosis ◽  
Membrane Cytoskeleton ◽  
Glutathione Deficiency

A dog with persistent elliptocytosis was studied. The dog had membrane protein band 4.1 deficiency, microcytosis, shortened erythrocyte lifespan, increased osmotic sensitivity, and a mild glutathione deficiency. Erythrocyte deformability and membrane stability were adversely effected. The dog's parents had decreased band 4.1, decreased stability, and some elliptocytosis. This disorder in dogs closely resembles human patients with band 4.1 deficiency and should provide a valuable animal model to study the erythrocyte membrane cytoskeleton.

scholarly journals Localization of the Ankyrin-binding Site on Erythrocyte Membrane Protein, Band 3

1989 ◽  
Vol 264 (27) ◽  
pp. 15893-15899 ◽  
Author(s):  
B M Willardson ◽  
B J M Thevenin ◽  
M L Harrison ◽  
W M Kuster ◽  
M D Benson ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Binding Site ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Band 3 ◽  
Erythrocyte Membrane Protein

scholarly journals Differential expression of erythrocyte membrane protein band 4.2 in cancers of the breast.

2021 ◽  
Author(s):  
Shahan Mamoor
Keyword(s):  
Breast Cancer ◽  
Membrane Protein ◽  
Differential Expression ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Normal Breast ◽  
Differentially Expressed ◽  
Significant Differential Expression ◽  
Primary Tumors ◽  
Erythrocyte Membrane Protein

Breast cancer affects women at relatively high frequency (1). We mined published microarray datasets (2, 3) to determine in an unbiased fashion and at the systems level genes most differentially expressed in the primary tumors of patients with breast cancer. We report here significant differential expression of the gene encoding erythrocyte membrane protein band 4.2, EPB42, when comparing primary tumors of the breast to the tissue of origin, the normal breast. EPB42 mRNA was present at significantly lower quantities in tumors of the breast as compared to normal breast tissue. Analysis of human survival data revealed that expression of EPB42 in primary tumors of the breast was correlated with overall survival in patients with normal-like subtype cancer, demonstrating a relationship between primary tumor expression of a differentially expressed gene and patient survival outcomes influenced by PAM50 molecular subtype. EPB42 may be of relevance to initiation, maintenance or progression of cancers of the female breast.

scholarly journals A variant of erythrocyte membrane skeletal protein band 4.1 associated with hereditary elliptocytosis

Blood ◽  
1984 ◽  
Vol 64 (5) ◽  
pp. 1006-1015 ◽  
Author(s):  
M Garbarz ◽  
D Dhermy ◽  
MC Lecomte ◽  
C Feo ◽  
I Chaveroche ◽  
...  
Keyword(s):  
Erythrocyte Membrane ◽  
Protein Band ◽  
Erythrocyte Membranes ◽  
Red Cell ◽  
Intact Cells ◽  
Additional Band ◽  
Whole Cells ◽  
Protein 4.1 ◽  
Hereditary Elliptocytosis ◽  
Sds Page

Abstract A family comprising three patients (a mother and two children) with mild hereditary elliptocytosis was studied. Each patient had prominent elliptocytosis, reduced red cell deformability, and normal erythrocyte thermal sensitivity. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the erythrocyte membranes in each patient showed decreased levels of band 4.1 (approximately half of the normal value) and the presence of an additional band migrating below protein band 4.2. This additional band was shown to derive from protein 4.1. Comparative partial proteolytic mapping of protein 4.1 and the additional band revealed a number of common peptides. Enzyme-linked immunoelectrotransfer blots of the patients' erythrocyte membranes using a monoclonal antibody to protein 4.1 revealed that, in addition to protein 4.1, two other bands below protein 4.2 were stained; one of these bands migrated in the same position as the additional band detected in the Coomassie Blue-stained gels. Immunoblotting of the patients' whole cells using the antibody to protein 4.1 revealed that this altered band 4.1 occurred as such in the intact red cell. SDS-PAGE of protein 4.1 purified from one patient showed the presence of two lower molecular weight bands below protein 4.1; the lower band migrated in the same position as the additional band found on SDS-PAGE of the patients' erythrocyte membranes. The patient's purified protein 4.1 displayed a decrease of about 40% in the binding activity with crude spectrin extracted from normal controls. Spectrin-spectrin interactions were normal in the three patients. The additional band present in the patients' red cell membranes probably represents a proteolytic degradation product. This alteration, present both in whole cells and isolated membranes, might affect the intact cells in vivo. We suggest that the patients' erythrocyte membrane instability may be related to the presence of an abnormal protein 4.1 whose modulatory influence on the spectrin-actin interaction in the skeleton is defective.

scholarly journals A case of spherocytosis with complete deficiency of erythrocyte membrane protein band 4.2, accompanied with arachnoid cyst and congenital ocular anomalies.

1989 ◽  
Vol 78 (7) ◽  
pp. 990-991 ◽  
Author(s):  
Hiroyuki ITO ◽  
Kenji IZUHARA ◽  
Eisuke YOKOTA ◽  
Shuji NAKANO ◽  
Kazuma FUJIMOTO ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Arachnoid Cyst ◽  
Protein Band ◽  
Erythrocyte Membrane Protein
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