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Binding of lectins to ?young? and ?old? human erythrocytes

✍ Scribed by Shinozuka, T. ;Takei, S. ;Yanagida, J. ;Watanabe, H. ;Ohkuma, S.


Publisher
Springer-Verlag
Year
1988
Weight
644 KB
Volume
57
Category
Article
ISSN
1432-0584

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✦ Synopsis


"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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The incubation of 14C-furosemide at high specific activity with intact red blood cells at 37 degrees C, pH 7.4, has enabled the furosemide binding sites to be characterized with respect to time course, affinity and specificity. The binding reaction was rapid, reversible and close to thermodynamic eq