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Postnatal changes in lectin binding to microvillus membranes from rat intestine
Biochemical and Biophysical Research Communications
|June 15, 1983
Summary
During rat intestinal development, peanut agglutinin (PNA) binding sites decrease while soybean lectin and Ricinus communis toxin binding sites increase, indicating changes in gut surface glycoproteins.
Area of Science:
- Biochemistry
- Developmental Biology
- Glycobiology
Background:
- The intestinal microvillus membrane's surface composition changes significantly during development.
- Glycopeptides on the membrane surface contain specific carbohydrate residues that can be recognized by lectins.
Purpose of the Study:
- To investigate the changes in intestinal microvillus membrane glycopeptides during rat weaning.
- To identify alterations in lectin-binding sites associated with developmental changes in the gut.
Main Methods:
- Utilized radiolabeled lectins, including 125I-labeled peanut agglutinin (PNA), soybean lectin, and Ricinus communis toxin.
- Analyzed glycopeptides from rat intestinal microvillus membranes at different developmental stages (suckling vs. weaned).
Main Results:
- Suckling rat intestinal microvillus membranes showed abundant PNA-reactive sites, rich in beta, D-Gal(1 to 3)D-GalNAc residues.
- Weaning led to the loss of unsubstituted PNA sites and partial loss of sialyl-substituted sites.
- Concurrently, increased binding of soybean lectin and Ricinus communis toxin indicated new terminal D-GalNAc and D-Gal residues in mature membranes.
Conclusions:
- Developmental loss of PNA-reactive sites in rat intestinal microvillus membranes is linked to O-glycan modifications in mucin-type glycoproteins.
- These changes may involve D-GalNAc substitution and steric hindrance during glycosylation, altering membrane surface characteristics.