Relationships between DNA Methylation and Expression in Erythrocyte Membrane Protein (Band 3, Protein 4.2, and 3-Spectrin) Genes during Human Erythroid Development and Differentiation

2005 ◽  
Vol 82 (5) ◽  
pp. 422-429 ◽  
Author(s):  
Ralph Remus ◽  
Akio Kanzaki ◽  
Ayumi Yawata ◽  
Hideho Wada ◽  
Hidekazu Nakanishi ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Protein Band ◽  
Band 3 ◽  
Band 3 Protein ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2 ◽  
Development And Differentiation ◽  
Erythroid Development

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 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 ◽  
Author(s):  
Raja BHATTACHARYYA ◽  
Amit K. DAS ◽  
Prasun K. MOITRA ◽  
Biswajit PAL ◽  
Indranil MANDAL ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Binding Domain ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Protein 4.2

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
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