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A selection of lectins was used to investigate developmentally regulated changes in the distribution of cell surface oligosaccharides during the gastrulation and neurulation stages of early chick embryo development. Lectins from three specificity classes were used: glucose/mannose specificity (concanavalin A [Con A], Lens culinaris agglutinin [LCA], Pisum sativum agglutinin [PSA]); N-acetylglucosamine specificity (Lycopersicon esculentum agglutinin [LEA], wheat germ agglutinin [WGA], succinylated WGA [sWGA]); N-acetylgalactosamine/galactose specificity (Dolichos biflorus agglutinin [DBA], soybean agglutinin [SBA], Sophora japonica agglutinin [SJA], Bandeiraea (Griffonia) simplicifolia lectin I [BSL I], peanut agglutinin [PNA], Artocarpus integrifolia lectin [Jacalin], Ricinus communis agglutinin-1 [RCA-1], Erythrina cristagalli lectin [ECL]). At gastrulation stages, patterns of lectin binding could be distinguished in the epiblast, mesoderm, and endoderm cell layers. The primitive streak failed to bind any of the lectins, but LEA and WGA bound to the epiblast in regions lateral to the streak, indicating the loss of some glucosamine residues medially in preparation for the ingression movements of gastrulation. Several lectins showed marked binding to the mesoderm cells after their passage through the primitive streak; these were LCA, PSA, WGA, sWGA, BSL, and most particularly PNA. Therefore, the epithelial-mesenchymal transformation from epiblast to mesoderm at the primitive streak is accompanied by cell surface oligosaccharide changes in the epiblast and mesoderm that involve all classes of lectins including the PNA-binding sequence Gal beta 1-3GalNAc. Ultrastructurally, PNA was shown to bind extracellularly to matrix fibrils. Jacalin, having the same sugar specificity as PNA, but binding to serine/threonine linked chains rather than asparagine linked chains showed no binding to the mesoderm.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1991 Oct
PMID:Changes in glycoconjugate expression during early chick embryo development: a lectin-binding study. 174 24

Septation of the tubular heart to form the multi-chambered heart involves endocardial cell mesenchymal transformation at discrete sites. These sites include the crests of endocardial cushions at the atrioventricular junction, crests of the spiral ridges within the outflow tract, and the leading edge of the atrial septum. The factors involved in this multi-step inductive process appear to include the neural cell adhesion molecule (NCAM). The down-regulation of NCAM coincident with mesenchymal transformation has been documented at the atrioventricular cushion tissue. In view of the function-regulation properties of polysialylated NCAM (PSA-NCAM), we hypothesized that this form of NCAM would be playing a role during the dramatic changes in cell-cell interactions occurring in the endocardium at the leading edge of the primary atrial septum. Chicken hearts at stages during primary atrial septum development were fixed with paraformaldehyde and either immunofluorescently stained for the light microscope analysis or immunoperoxidase stained for ultrastructural analysis. A monoclonal antibody to an NCAM polypeptide epitope (5E) was used to detect all forms of NCAM, while a monoclonal to the polysialic acid (5A5) was used to detect that subset of NCAM which is highly polysialylated (PSA-NCAM). By light microscope level analysis, an increase in immunostaining for NCAM and the appearance of PSA-NCAM was detected on embryonic chicken endocardial cells at the leading edge of the growing atrial septum. The ultrastructural analysis revealed that there is also a change in the pattern of NCAM and PSA-NCAM from a polarized localization to a more ubiquitous distribution over the endocardial cell surface as these cells send out processes, form multiple layers, and sink or move into the underlying extracellular matrix. PSA-NCAM was also detected along cell appositions of cells within the matrix. Both NCAM and PSA-NCAM levels were reduced on cells deep within the matrix. These findings indicate that during primary atrial septation, PSA-NCAM may be deployed on endocardial epithelial cells in order to down-regulate cell-cell interactions and allow the detachment and migration of some of these cells into the underlying matrix.
Anat Rec 1997 01
PMID:Polysialylated NCAM expression on endocardial cells of the chick primary atrial septum. 898 5

The present histochemical and cytochemical study using a lectin panel (WGA, GSI-A4, GSI-B4, PSA UEA-I, PNA, LCA, Con-A, DBA, MPA, BPA) has demonstrated that, in Podarcis sicula, the differentiation of small follicle cells into pyriform cells by means of intermediate cells is accompanied by the appearance of glycoproteins bearing alpha-GalNAc terminated O-linked side chains on the cell surface. The distribution of DBA- and MPA-binding sites over the follicular epithelium changed during the different stages of oocyte growth. DBA- and MPA-binding sites first appeared at the beginning of folliculogenesis within the zona pellucida (ZP) and on the surface of small cells, i.e., the stem cells of pyriform cells. Afterward, labeling was evident on the cell surfaces of intermediate cells and, later on, also of pyriform cells. On the other hand, no labeling was detected on the small cells located under the basal lamina, which, reportedly, do not differentiate into pyriform cells (Filosa et al. J. Embryol. Exp. Morphol., 1979; 15:297-316). Once pyriform cells were differentiated, the distribution of DBA- and MPA-binding sites over the follicular epithelium remained unchanged until intermediate and pyriform cells underwent apoptosis (Motta et al. J. Exp. Zool., 1996; 276:233-241) and the follicular epithelium transformed into a monolayer composed of small follicle cells only (Filosa Mon. Zool. Ital., 1973; 7:151-165). During this stage of oocyte growth, DBA and MPA labeling gradually decreased to completely disappear in the follicular epithelium of vitellogenic follicles. It is noteworthy that the observed changes in the distribution of DBA- and MPA-binding sites represent the first evidence recognized by lectins of a gradual modification of surface glycoprotein distribution over the follicular epithelium in the ovarian follicles of nonmammalian vertebrates so far studied. Finally, the zona pellucida (ZP), characterized by the presence of GalNAc, GluNAc, Man, and Gal, was demonstrated to be first synthetized by the oocyte and later on by the follicle cells.
Anat Rec 2001 05 01
PMID:Pyriform cell differentiation in Podarcis sicula is accompanied by the appearance of surface glycoproteins bearing alpha-galNAc terminated chains. 1133 65

During development, different epithelial cells in the mouse cochlea express different cell surface glycoconjugates, which may reflect membrane specialization. Some of the lectins tested in this study (SBA, succ-WGA, and PSA) labeled the sensory cells of the cochlea around birth. Other lectins (WGA, Con A, RCA-II, and PHA-E) labeled surfaces of the sensory cells, particularly the stereocilia, from early stages of development (gestation day (GD) 16) through 21 days after birth. These may be adhesion molecules needed to attach the newly forming tectorial membrane (TM) to the stereocilia. Lectin staining of the developing TM revealed that the substructures of the TM are biochemically distinct. Lectin staining also showed the temporal sequence of the expression of cytoplasmic glycoconjugates of the cochlear epithelium during development. Biochemical changes during development are probably the result of different cells being involved in the production of glycoconjugates, and may have functional significance, specifically with regard to the expression of adhesion and/or signaling molecules.
Anat Rec A Discov Mol Cell Evol Biol 2003 Oct
PMID:Distribution of glycoconjugates during cochlea development in mice: light microscopic lectin study. 1297 16