Characterization of epithelial domains in the nasal passages of chick embryos: spatial and temporal mapping of a range of extracellular matrix and cell surface molecules during development of the nasal placode.
The formation of the nasal passages involves complex morphogenesis and their lining develops a spatially ordered pattern of differentiation, with distinct domains of olfactory and respiratory epithelium. Using antibodies to the neural cell adhesion molecule (N-CAM), keratan sulphate and heparan sulphate proteoglycan (HSPG) and a panel of lectins (agglutinins of Canavalia ensiformis (ConA), Dolichos biflorus (DBA), peanut (PNA), Ricinis communis (RCA1), soybean (SBA), Ulex europaeus (UEA1), and wheatgerm (WGA], we have documented cell surface characteristics of each epithelial domain. Binding of antibodies to N-CAM and to keratan sulphate, and the lectins ConA, PNA, RCA1, SBA and WGA marks the olfactory epithelial domain only. The restriction of N-CAM to the sensory region of the epithelium has also been reported in the developing ear. This striking similarity is consistent with the idea that N-CAM may be involved in the division of functionally and histologically distinct cell groups within an epithelium. We traced the olfactory-specific cell markers during development to gain insights into the origin of the epithelial lining of the nasal passages. All reagents bind at early stages to the thickened nasal placode and surrounding head ectoderm and then become progressively restricted to the olfactory domain. The expression of these characteristics appears to be modulated during development rather than being cell autonomous. The distribution of keratan sulphate was compared with collagen type II in relation to the specification of the chondrocranium. Keratan sulphate and collagen type II are only colocalized at the epithelial-mesenchymal interface during early nasal development. At later stages, only collagen type II is expressed at the interface throughout the nasal passages, whereas keratan sulphate is absent beneath the respiratory epithelium.
Croucher
S J
SJ
Department of Anatomy and Developmental Biology, University College & Middlesex School of Medicine, London, UK.
Tickle
C
C
D000818:Animals; D015415:Biomarkers / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis*; D002462:Cell Membrane / Q000648:ultrastructure; D002642:Chick Embryo; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis; D004847:Epithelial Cells; D005109:Extracellular Matrix / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate / Q000032:analysis; D007632:Keratan Sulfate / Q000032:analysis; D037102:Lectins; D009666:Nose / Q000166:cytology / Q000196:embryology*; D013194:Staining and Labeling
D015415:Biomarkers; D002241:Carbohydrates; D015816:Cell Adhesion Molecules, Neuronal; D011508:Chondroitin Sulfate Proteoglycans; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D007632:Keratan Sulfate; D037102:Lectins