Abstract
The Tyr-phosphorylation of the cytoplasmic domain of the major membrane-spanning band 3, rather than the Ser/Thr-phosphorylation of the membrane proteins (spectrin and band 3 itself), might be functionally related to certain morphological changes of human erythrocytes. This view is supported by the following lines of evidence: a) vanadate or its derivative pervanadate (vanadyl hydroperoxide), which markedly increase the Tyr-phosphorylation of band 3 (without practically affecting the Ser/Thr-phosphorylation of spectrin) promotes a crenation of human erythrocytes; b) okadaic acid, which selectively increases the Ser/Thr-phosphorylation of spectrin and other membrane proteins, does not promote any shape change, at least at a level detectable with scanning electron microscopy.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anion Exchange Protein 1, Erythrocyte / isolation & purification
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Anion Exchange Protein 1, Erythrocyte / metabolism
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Erythrocyte Membrane / drug effects
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Erythrocyte Membrane / metabolism*
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Erythrocyte Membrane / ultrastructure*
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Ethers, Cyclic / pharmacology
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Humans
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Membrane Proteins / blood*
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Membrane Proteins / drug effects
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Membrane Proteins / isolation & purification
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Microscopy, Electron, Scanning
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Okadaic Acid
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Phosphoprotein Phosphatases / antagonists & inhibitors
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Phosphoproteins / drug effects
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Phosphoproteins / isolation & purification
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Phosphoproteins / metabolism
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Phosphorylation
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Phosphotyrosine
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Spectrin / isolation & purification
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Spectrin / metabolism
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Tyrosine / analogs & derivatives
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Tyrosine / analysis
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Tyrosine / metabolism
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Vanadates / pharmacology
Substances
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Anion Exchange Protein 1, Erythrocyte
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Ethers, Cyclic
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Membrane Proteins
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Phosphoproteins
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pervanadate
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Spectrin
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Okadaic Acid
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Phosphotyrosine
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Vanadates
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Tyrosine
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Phosphoprotein Phosphatases