Carbohydrate recognition in neuronal development: structure and expression of surface oligosaccharides and beta-galactoside-binding lectins.

Publication Type:

Journal Article

Source:

Ciba Foundation symposium, Volume 145, p.189-210; discussion 210-8 (1989)

Keywords:

Aging, Amino Acid Sequence, Animals, Carbohydrate Conformation, Carbohydrate Sequence, Cell Membrane, Galactosides, Galectins, Ganglia, Spinal, Glycosides, Hemagglutinins, Molecular Sequence Data, NEURONS, Oligosaccharides, Rats, Sequence Homology, Nucleic Acid

Abstract:

The differentiation and development of vertebrate neurons is controlled in part by interactions with cell surface and extracellular matrix molecules, many of which are glycoproteins that mediate their developmental actions by homophilic or heterophilic binding to other glycoproteins. In addition there is increasing evidence that cell recognition and adhesion in some embryonic cell types involve interactions between cell surface oligosaccharides and complementary carbohydrate-binding proteins. Although a role for carbohydrate recognition in neuronal development has been proposed, the precise function of complex carbohydrate structures on neural cells has not been defined. To approach this problem, we have examined the structure and expression of cell surface oligosaccharides and carbohydrate-binding proteins by primary sensory neurons in the rat dorsal root ganglion (DRG). There are several functionally distinct subsets of DRG neurons, each of which conveys a different sensory modality to distinct target domains in the spinal cord. Monoclonal antibodies against defined oligosaccharide structures identify each of the major subsets of DRG neurons on the basis of their expression of a distinct set of complex oligosaccharides, derived from lacto-, globo- and ganglioseries backbone structures. In particular, small diameter DRG neurons involved in pain processing express beta-galactoside-based lactoseries oligosaccharides. DRG and spinal cord neurons also express two soluble beta-galactoside-binding proteins of relative molecular masses 14,500 and 29,000, termed RL-14.5 and RL-29, which represent potential ligands for lactoseries oligosaccharides. RL-14.5 is expressed by the majority of DRG neurons whereas RL-29 is restricted to the subset of small DRG neurons that express surface N-acetyllactosamine structures. RL-14.5 and RL-29 are expressed soon after the differentiation of DRG neurons and appear to be released from cultured DRG neurons. Rat brain cDNA clones encoding RL-14.5 have been isolated. The nucleotide and predicted amino acid sequence of RL-14.5 has confirmed that this lectin is highly homologous to soluble beta-galactoside-binding proteins in other vertebrate species. Northern blot analysis and in situ hybridization indicate that RL-14.5 mRNA is selectively expressed in sensory and motor neurons in the rat nervous system. The selective expression of lactoseries oligosaccharides and complementary beta-galactoside-binding lectins may contribute to the differentiation and/or development of these two classes of neurons.