scholarly journals The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules.

1987 ◽  
Vol 104 (6) ◽  
pp. 1597-1602 ◽  
Author(s):  
A Kücherer ◽  
A Faissner ◽  
M Schachner

The monoclonal L3 antibody reacts with an N-glycosidically linked carbohydrate structure on at least nine glycoproteins of adult mouse brain. Three out of the L3 epitope-carrying glycoproteins could be identified as the neural cell adhesion molecules L1 and myelin-associated glycoprotein, and the novel adhesion molecule on glia. Expression of the L3 carbohydrate epitope is regulated independently of the protein backbone of these three glycoproteins. Based on the observation that out of three functionally characterized L3 epitope-carrying glycoproteins three fulfill the operational definition of an adhesion molecule, we would like to suggest that they form a new family of adhesion molecules that is distinct from the L2/HNK-1 carbohydrate epitope family of neural cell adhesion molecules. Interestingly, some members in each family appear to be unique to one family while other members belong to the two families.

1987 ◽  
Vol 105 (1) ◽  
pp. 569-576 ◽  
Author(s):  
E Persohn ◽  
M Schachner

The cellular and subcellular localization of the neural cell adhesion molecules L1 and N-CAM was studied by pre- and postembedding immunoelectron microscopic labeling procedures in the developing mouse cerebellar cortex. The salient features of the study are: L1 displays a previously unrecognized restricted expression by particular neuronal cell types (i.e., it is expressed by granule cells but not by stellate and basket cells) and by particular subcellular compartments (i.e., it is expressed on axons but not on dendrites or cell bodies of Purkinje cells). L1 is always expressed on fasciculating axons and on postmitotic, premigratory, and migrating granule cells at sites of neuron-neuron contact, but never at contact sites between neuron and glia, thus strengthening the view that L1 is not involved in granule cell migration as a neuron-glia adhesion molecule. While N-CAM antibodies reacting with the three major components of N-CAM (180, 140, and 120 kD) show a rather uniform labeling of all cell types, antibodies to the 180-kD component (N-CAM180) stain only the postmigratory granule cell bodies supporting the notion that N-CAM180, the N-CAM component with the longest cytoplasmic domain, is not expressed before stable cell contacts are formed. Furthermore, N-CAM180 is only transiently expressed on Purkinje cell dendrites. N-CAM is present in synapses on both pre- and post-synaptic membranes. L1 is expressed only preterminally and not in the subsynaptic membranes. These observations indicate an exquisite degree of fine tuning in adhesion molecule expression during neural development and suggest a rich combinatorial repertoire in the specification of cell surface contacts.


1998 ◽  
Vol 19 (4) ◽  
pp. 269-277
Author(s):  
YOSHIHIRO YAYOI ◽  
SUMIO TAKAHASHI ◽  
SAKAE TAKEUCHI ◽  
MAKOTO TAKEUCHI ◽  
TATSUNORI SEKI ◽  
...  

Development ◽  
1988 ◽  
Vol 102 (4) ◽  
pp. 749-761 ◽  
Author(s):  
G. Klein ◽  
M. Langegger ◽  
C. Goridis ◽  
P. Ekblom

The neural cell adhesion molecules (N-CAM) are a family of related glycoproteins with Mr of 180, 140 and 120 × 10(3) (180K etc.). In the embryo, they are often highly sialylated and migrate as a diffuse band of 170–250K. N-CAM are found in non-neural tissues and we have now studied the expression of N-CAM in the developing mouse kidney. During kidney development, a unique conversion of a mesenchyme to an epithelium occurs and it is thought that this is mediated by an increase in cell adhesivity. By immunofluorescence, we show that N-CAM is present already at onset of kidney development on the cells of the uninduced nephrogenic mesenchyme. After induction, when the cells convert into an epithelium, they lose N-CAM gradually and instead begin to express uvomorulin, another primary CAM. By using an organ culture model, we could rather precisely show that N-CAM and uvomorulin are coexpressed for a short period, but, when epithelial cell polarization is evident, only uvomorulin is present on the epithelium, whereas N-CAM is confined to the surrounding mesenchyme. Immunoblotting for N-CAM revealed that the ‘embryonic’ form of N-CAM, the broad 170–250K band was not present in the embryonic kidney, which instead expressed the three distinct 180K, 140K and 120K bands typical of adult neurones. The 180K and 140K bands were gradually lost during development and were no longer detectable in adult kidneys. By using an N-CAM cDNA, we detected three different mRNAs of 7.4, 6.7 and 4.3 kb in the developing kidney, but this expression was restricted to the embryonic and early postnatal stages. No transcripts were detectable in adult kidneys. The studies do not support the hypothesis that N-CAM expression in the kidney is turned on by embryonic induction. Rather, we suggest that N-CAM are important adhesives for the predetermined, but not yet induced, nephrogenic mesenchyme.


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