DOI: 10.1111/j.1432-1033.1983.tb07613.x. Increased methyl esterification of membrane proteins in aged red‐blood cells

Increased methyl esterification of membrane proteins in aged red‐blood cells

10.1111/j.1432-1033.1983.tb07613.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

The enzymatic carboxyl methyl esterification of erythrocyte membrane proteins has been investigated in three different age‐related fractions of human erythrocytes. When erythrocytes of different mean age, separated by density gradient centrifugation, were incubated under physiological conditions (pH 7.4, 37°C) in the presence of l‐[methyl‐3H]methionine, the precursor in vivo of the methyl donor S‐adenosylmethionine, a fourfold increase in membrane‐protein carboxyl methylation was observed in the oldest cells compared with the youngest ones.The identification of methylated species, based on comigration of radioactivity with proteins stained with Coomassie blue, analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, shows, in all cell fractions, a pattern similar to that reported for unfractionated erythrocytes. However in the membrane of the oldest erythrocytes the increase in methylation of the cytoskeletal proteins, bands 2.1 and 4.1, appears to be significantly more marked compared with that observed in the other methylated polypeptides. Furthermore the turnover rate of incorporated [3H]methyl groups in the membrane proteins of the oldest cells markedly increases during cell ageing. Particularly in band 4.1 the age‐related increase in methyl esterification is accompanied by a significant reduction of the half‐life of methyl esters.The activity of cytoplasmic protein methylase II does not change during cell ageing, while the isolated ghosts from erythrocytes of different age show an age‐related increased ability to act as methyl‐accepting substrates, when incubated in presence of purified protein methylase II and methyl‐labelled S‐adenosylmethionine, therefore the relevance of membrane structure in determining membrane protein methylation levels can be postulated.Finally the possible correlation of this posttranslational protein modification with erythrocyte ageing is discussed.

Bibliography

GALLETTI, P., INGROSSO, D., NAPPI, A., GRAGNANIELLO, V., IOLASCON, A., & PINTO, L. (1983). Increased methyl esterification of membrane proteins in aged redâblood cells. European Journal of Biochemistry, 135(1), 25â31. Portico.

Authors 6

Patrizia GALLETTI (first)
Diego INGROSSO (additional)
Ausilia NAPPI (additional)
Vincenzo GRAGNANIELLO (additional)
Achille IOLASCON (additional)
Luciano PINTO (additional)

References 44 Referenced 40

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{'key': 'e_1_2_3_4_2', 'volume-title': 'Protein Methylation', 'author': 'Paik W. K.', 'year': '1980'} / Protein Methylation by Paik W. K. (1980)
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Dates

Type	When
Created	20 years, 6 months ago (March 4, 2005, 10:07 a.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 5:57 a.m.)
Indexed	1 year, 9 months ago (Nov. 23, 2023, 2:20 p.m.)
Issued	42 years ago (Sept. 1, 1983)
Published	42 years ago (Sept. 1, 1983)
Published Online	20 years, 6 months ago (March 4, 2005)
Published Print	42 years ago (Sept. 1, 1983)

Funders 0

None

BibTeX

@article{GALLETTI_1983, title={Increased methyl esterification of membrane proteins in aged red‐blood cells: Preferential esterification of ankyrin and band‐4.1 cytoskeletal proteins}, volume={135}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1983.tb07613.x}, DOI={10.1111/j.1432-1033.1983.tb07613.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={GALLETTI, Patrizia and INGROSSO, Diego and NAPPI, Ausilia and GRAGNANIELLO, Vincenzo and IOLASCON, Achille and PINTO, Luciano}, year={1983}, month=sep, pages={25–31} }

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