Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:Q9UIJ5 (
Rec
)
58,342
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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
The main and accessory olfactory systems of certain mammals (e.g., rodents, ungulates, and carnivores) have been investigated using lectin histochemistry to probe for sugar residues that may reflect physiological aspects of signal transduction or development. Morphologically, the vomeronasal organs (VNOs) of strepsirrhine primates (lemurs and lorises) are typical of functional VNOs in other mammals, whereas in humans and chimpanzees the VNOs appear vestigial. However, the human VNO is considered functional by some authors. To elucidate the cellular nature of the VNO in human and chimpanzees, a panel of six lectins (Con-A,
ECL
, PNA, RCA, s-WGA, and UEA-1) was applied to the VNO in eight species of primates, including humans and chimpanzees. The results indicated that there were few, if any, lectin-reactive cells in the human or chimpanzee VNO that resembled those seen in the vomeronasal neuroepithelium in other primates. The overall pattern of lectin reactivity in the human and chimpanzee VNO is unlike that seen in mammals with chemosensory VNOs, suggesting that the VNO of these hominoids does not function similarly to that of other primates.
Anat
Rec
A Discov Mol Cell Evol Biol 2005 Jun
PMID:Comparative study of lectin reactivity in the vomeronasal organ of human and nonhuman primates. 1588 Jul 83