Preferential sulfoxidation of the methionine residues of glycophorin A

Hardy, Robert E.; Dill, Kilian

doi:10.1016/0014-5793(82)80717-5

FEBS Letters

1982

DOI: 10.1016/0014-5793(82)80717-5

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Preferential sulfoxidation of the methionine residues of glycophorin A

Robert E. Hardy

Kilian Dill

Abstract: Carbon-13 nuclear magnetic resonance spectroscopy was used to monitor the preferential sulfoxidation of the two methionine residues (8 and 81) of glycophorin A. In urea Met-8 is readily oxidized. However, Met-81 can only be oxidized in trifluoroacetic acid containing hydrogen peroxide. Our results also give some insight into the reagent accessibility of different portions of the protein molecule and the general stability of this glycoprotein.

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Cited by 8 publications

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“…The elevated level of Met(O) in the newly synthesized proteins suggests that methionine residues in nascent polypeptide chains are more susceptible to oxidation than are those in intact proteins. It is known that the reactivity of methionine residues with oxidizing reagents is dependent on their location in the protein (43)(44)(45)(46)(47). Because methionine residues are usually located within the hydrophobic interior of proteins (31), they may, therefore, be more resistant to oxidation than methionine residues in nascent polypeptide chains.…”

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Oxidation of methionine residues in proteins of activated human neutrophils.

Fliss¹,

Weissbach²,

Brot³

1983

Proc. Natl. Acad. Sci. U.S.A.

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A simple assay for the detection of 35S-labeled methionine sulfoxide residues in proteins is described. The assay, which is based on the ability of CNBr to react with methionine but not with methionine sulfoxide, requires the prelabeling of cellular proteins with [3S]methionine. The assay was used to study the extent of methionine oxidation in newly synthesized proteins of both activated and quiescent human neutrophils. In cells undergoing a phorbol 12-myristate 13-acetate-induced respiratory burst, about 66% of all methionine residues in newly synthesized proteins were oxidized to the sulfoxide derivative, as compared with 9% in cells not treated with the phorbol ester. In contrast, quantitation of methionine sulfoxide content in the total cellular protein by means of amino acid analysis showed that only 22% of all methionine residues were oxidized in activated cells as compared with 9% in quiescent cells. It is proposed that methionine residues in nascent polypeptide chains are more susceptible to oxidation than those in completed proteins.Methionine residues in proteins can readily be oxidized to the sulfoxide derivative in the presence of suitable oxidizing reagents, a reaction that can result in the inactivation of certain proteins (for reviews, see refs. 1 and 2). Despite indications that sulfoxidation of methionine may occur frequently under physiological conditions, the importance of this reaction remains largely unrecognized (3). The absence of a rapid facile assay for the detection of methionine sulfoxide [Met(O)] residues in proteins has hindered studies in this area. Because Met(O) is unstable to acid hydrolysis (4), long and tedious methods, involving alkaline hydrolysis or alkylation of methionine, are normally used (5). The present report describes a simple assay for the detection of Met(O) residues in proteins labeled with [3S]-methionine. The assay, which is based on the ability of CNBr to react with methionine but not with methionine sulfoxide (6), was used to examine the oxidation of methionine residues in human neutrophils. Neutrophils were chosen for these studies because of their ability to produce copious quantities of oxidizing reagents on activation. As part of their microbicidal response, neutrophils can be activated by a variety of agents such as chemotactic peptides, complement, insoluble particles, and others (7). The activated cells undergo a respiratory burst during which they produce oxidizing reagents such as superoxide anion (O°), hydrogen peroxide (H202), hydroxyl radicals, and hypochlorite ions (8-10), which are highly toxic to extracellular microorganisms and tissues (9, 11-13). These reagents can also inactivate chemotactic peptides and other polypeptides through selective oxidation of methionine residues (14-18). Recently, it has become apparent that the indiscriminate release of these oxy-radicals can damage the neutrophils themselves. Several studies have shown that the respiratory burst can lead to a decrease in neutrophil function through autooxidation (19)(20...

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confidence: 99%

Oxidation of methionine residues in proteins of activated human neutrophils.

Fliss¹,

Weissbach²,

Brot³

1983

Proc. Natl. Acad. Sci. U.S.A.

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Specific 13C reductive methylation of glycophorin A. Possible relation of the N-terminal amino acid and the lysine residues to MN blood group specificities

Hardy

Batstone-Cunningham

Dill

1983

Archives of Biochemistry and Biophysics

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13C-NMR spectral studies of the n—terminal portion of glycophorins

Dill

Carter

1986

Progress in Nuclear Magnetic Resonance Spectroscopy

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Preferential sulfoxidation of the methionine residues of glycophorin A

Cited by 8 publications

References 17 publications

Oxidation of methionine residues in proteins of activated human neutrophils.

Oxidation of methionine residues in proteins of activated human neutrophils.

Specific 13C reductive methylation of glycophorin A. Possible relation of the N-terminal amino acid and the lysine residues to MN blood group specificities

13C-NMR spectral studies of the n—terminal portion of glycophorins

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