scholarly journals High incidence of a polymorphic variant of erythrocyte membrane protein, Band 3-Memphis, on a western Japanese island

1995 ◽  
Vol 40 (3) ◽  
pp. 265-270 ◽  
Author(s):  
Kenji Izuhara ◽  
Hiroshi Ideguchi ◽  
Takeshi Otsuka ◽  
Kenshi Okubo ◽  
Tomonori Ogo ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Band 3 ◽  
Polymorphic Variant ◽  
Japanese Island ◽  
Erythrocyte Membrane Protein ◽  
High Incidence

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 Erythrocyte Membrane Protein Band 3 Predicts Interferon Ribavirin-Induced Anemia

2019 ◽  
Vol 08 (02) ◽  
pp. 5-16
Author(s):  
Engin Altintas ◽  
Serap Yalin ◽  
Orhan Sezgin ◽  
Enver Ucbilek ◽  
Anil Tombak ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Band 3 ◽  
Erythrocyte Membrane Protein

scholarly journals Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2

1999 ◽  
Vol 340 (2) ◽  
pp. 505-512 ◽  
Author(s):  
Raja BHATTACHARYYA ◽  
Amit K. DAS ◽  
Prasun K. MOITRA ◽  
Biswajit PAL ◽  
Indranil MANDAL ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Amino Acid Residues ◽  
Fusion Peptides ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2 ◽  
Positive Modulator

Evidence accumulated over the years suggests that human erythrocyte membrane protein 4.2 is one of the proteins involved in strengthening the cytoskeleton-membrane interactions in the red blood cell. Deficiency of protein 4.2 is linked with a variety of hereditary haemolytic anaemia. However, the interactions of protein 4.2 with other proteins of the erythrocyte membrane remain poorly understood. The major membrane-binding site for protein 4.2 resides on the cytoplasmic domain of band 3 (CDB3). In order to carry out an initial characterization of its interaction with the CDB3, protein 4.2 was subjected to proteolytic cleavage and gel renaturation assay, and the 23-kDa N-terminal domain was found to interact with band 3. This domain contained two putative palmitoylatable cysteine residues, of which cysteine 203 was identified as the palmitoylatable cysteine. Recombinant glutathione S-transferase-fusion peptides derived from this domain were characterized with respect to their ability to interact with the CDB3. Whereas these studies do not rule out the involvement of other subsites on protein 4.2 in interaction with the CDB3, the evidence suggests that the region encompassing amino acid residues 187-211 is one of the domains critical for the protein 4.2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction.

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.

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