Membrane skeletal protein 4.1 of avian erythrocytes is composed of multiple variants that exhibit tissue-specific expression.
The avian analog of mammalian erythrocyte protein 4.1, a structural component of the membrane skeleton, has been identified. It is present at the plasma membranes of avian erythrocytes and lens cells, but has not been found elsewhere in comparable amounts. In chickens, it exists as six variants with molecular masses of 87, 100, 115, 150, 160, and 175 kd. The corresponding polypeptides in turkeys are each about 3 kd smaller, suggesting that all may be encoded by a single gene. These variants have similar solubility properties and nearly identical two-dimensional iodopeptide maps that are similar to those of mammalian protein 4.1, but they are differentially phosphorylated. The three smallest variants are the predominant forms in avian erythrocytes, while the two largest variants predominate in avian lens cells. In contrast, mammalian erythrocytes and lens cells exhibit patterns of variants that are more similar to each other. These results show that only a subset of spectrin-containing cells possess protein 4.1, and that these cells differentially express the variants of protein 4.1 in a manner that may reflect corresponding functional differences.
D000818:Animals; D001798:Blood Proteins / Q000235:genetics*; D002645:Chickens; D003598:Cytoskeletal Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D014644:Genetic Variation; D008565:Membrane Proteins; D008970:Molecular Weight; D009479:Neuropeptides; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation
D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009479:Neuropeptides; D010446:Peptide Fragments; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1