140-180 KDA NCAM SPECIFIC INMUNOREACTIVITY IN THE CHICKEN EMBRYO OPTIC DISK

Abstract

During embryonic development of chicken retina and retinotectal proyection, neural cells showed spatiotemporal patterns in the glycosidic residues located in the plasmatic membranes. Those glycidic components are related with adhesion and recognition cellular behaviours during the generation of nervous system cytoarchitecture. Thus those sugars are included both in usual glycoproteins as in a group of molecules called as cell adhesion molecules (CAM). The first isolated molecule in this group was the neural cell adhesion molecule (NCAM). This glycoprotein has a proteic core with diverse isoforms and it has a variable sialic acids chain. It was able to determine that 120 kDa NCAM isoform shows scarcely sialized chains in intermediate stages by using conventional techniques, lectins and immunohistochemistry. Meanwhile 140-180 kDa NCAM isoforms possess high content in sialic acid and they are present both in early and final stages. Other authors reported that human 120 kDa NCAM isoform was similar to that observed in the Gallus domesticus retina. Our results showed that 140- 180kDa isoforms were only presented in the nerve optic fibers when they were left the optic disc.