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Lectin binding to cell surfaces: comparisons between normal and migrating corneal epithelium
Developmental Biology
|April 1, 1983
Summary
Cell surface sugars on migrating corneal epithelium differ from normal epithelium, with migrating cells showing characteristics similar to basal cells. This suggests a potential origin or alteration during migration.
Area of Science:
- Cell Biology
- Epithelial Biology
- Wound Healing
Background:
- Cell surface glycoproteins play crucial roles in cell-cell interactions and tissue dynamics.
- Understanding changes in cell surface characteristics during epithelial migration is vital for comprehending wound healing processes.
Purpose of the Study:
- To investigate and compare the cell surface lectin-binding characteristics of normal and migrating rat corneal epithelium.
- To identify differences in concanavalin A (Con A) and wheat germ agglutinin (WGA) binding patterns between normal and migrating epithelial cells.
Main Methods:
- Utilized three methods to monitor lectin binding: ferritin-conjugated Con A and WGA, [3H]Con A binding, and fluorescein isothiocyanate (FITC)-conjugated Con A and WGA.
- Localized and quantified lectin binding to cell surfaces of normal stratified and migrating corneal epithelium.
Main Results:
- Apical cell membranes of migrating epithelia exhibited higher Con A and WGA binding compared to superficial cells of normal epithelia.
- Migrating epithelial cells showed intense fluorescence with FITC-Con A and FITC-WGA, unlike normal epithelia where FITC-WGA binding was restricted to basal layers.
- These findings indicate distinct apical cell surface sugar profiles in migrating versus normal corneal epithelium.
Conclusions:
- Apical cell surface sugars on migrating corneal epithelium differ significantly from those of normal epithelium.
- The lectin-binding profile of migrating cells resembles that of basal cells in normal stratified epithelium.
- This suggests that the leading edge of migrating epithelium may originate from basal cells or undergo surface glycoprotein alterations during migration.