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Binding of lectins to “young” and “old” human erythrocytes

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Summary

“Old” human erythrocytes showed a 21.2% decrease in cell surface area and a 2% decrease in the number of WGA receptor sites, but a 27% increase in the distribution density of the WGA (lectin) receptor site, when compared with “young” human erythrocytes. For a list of lectin abbreviations, see Materials and methods). Both “young” and “old” erythrocytes exhibited very weak binding activity for 125I-labeled PNA, but there was no difference in binding activity for PNA between “young” erythrocytes and “old” ones. Compared with “young” erythrocytes, decreases in the number and distribution density of receptor sites for five lectins including LPA, Con A, RCA-II, SBA and BPA on the cell surface were observed in aged erythrocytes. “Old” erythrocytes also showed a decrease in the number of PHA-E receptor sites, while the distribution density of the same receptor site remained unchanged. In view of these and other observations, it is thought that human erythrocyte aging is accompanied by elimination of some glycoconjugates which have affinity for six lectins, LPA, Con A, RCA-II, PHA-E, SBA and BPA, whereas no WGA receptor-containing glycoconjugates are released from erythrocyte membranes. Elimination of the glycoconjugates results in shrinkage of erythrocytes to reduce their cell surface areas.

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Authors and Affiliations

  1. Department of Legal Medicine, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, 160, Tokyo, Japan

    T. Shinozuka, S. Takei & J. Yanagida

  2. Department of Legal Medicine, Saitama Medical School, 38 Morohongo, Moroyama, Iruma-gun, 350-04, Saitama, Japan

    H. Watanabe

  3. Department of Biochemistry, Tokyo College of Pharmacy, 1432-1 Horinouchi, 192-03, Hachioji, Tokyo, Japan

    S. Ohkuma

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  1. T. Shinozuka
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  2. S. Takei
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  3. J. Yanagida
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  4. H. Watanabe
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  5. S. Ohkuma
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Shinozuka, T., Takei, S., Yanagida, J. et al. Binding of lectins to “young” and “old” human erythrocytes. Blut 57, 117–123 (1988). https://doi.org/10.1007/BF00320150

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  • DOI: https://doi.org/10.1007/BF00320150

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