Preferential lectin binding to specific layers of rat oral epithelium and modification by enzyme pretreatment.
Three fluorescein-labeled lectins were shown to bind differentially to cell surfaces in different epithelial layers of rat oral mucosa regardless of the age or the site of origin of the tissue. Griffonia simplicifolia (GS-1-B4), specific for alpha-D-galactosyl end groups, labeled basal cells only; Ulex europeus (Ulex 1) specific for alpha-L-fucosyl groups labeled spinous cells; and Bandeiraea simplicifolia (BSII), specific for N-acetyl-D-glucosamine, labeled cornified cells. Pretreatment of sections with alpha-galactosidase completely abolished the staining of basal cells by GS-1-B4, but had no effect on the staining of spinous cells by Ulex 1. In contrast, alpha-fucosidase abolished the staining of spinous cells by Ulex 1 and caused staining of both basal and spinous cells by GS-1-B4. Neuraminidase and chondroitinase ABC produced results similar to one another, with staining of basal cells by GS-1-B4 and labeling of both basal and spinous cells with Ulex 1. beta-galactosidase, beta-glucuronidase, and testicular hyaluronidase did not affect the staining pattern of GS-1-B4 or Ulex 1, whereas chymotrypsin completely abolished any staining with either lectin. The results demonstrate a complex arrangement of cell surface carbohydrates in the epithelium of rat oral mucosa. The findings indicate a possible simplification in the spatial arrangements of cell surface carbohydrates during the differentiation of basal to spinous cells.
D000818:Animals; D004848:Epithelium / Q000032:analysis; D005260:Female; D005696:Galactosidases / Q000494:pharmacology*; D006023:Glycoproteins / Q000032:analysis; D037102:Lectins / Q000378:metabolism*; D008565:Membrane Proteins / Q000032:analysis; D009061:Mouth Mucosa / Q000378:metabolism*; D011247:Pregnancy; D051381:Rats; D000519:alpha-Galactosidase / Q000494:pharmacology*
D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D005696:Galactosidases; D000519:alpha-Galactosidase