scholarly journals Neural cell adhesion molecule expression is regulated by Schwann cell-neuron interactions in culture.

1989 ◽  
Vol 108 (5) ◽  
pp. 1909-1915 ◽  
Author(s):  
B Seilheimer ◽  
E Persohn ◽  
M Schachner
Keyword(s):  
Cell Adhesion ◽  
Schwann Cell ◽  
Schwann Cells ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dorsal Root Ganglion Neurons ◽  
Adhesion Molecule Expression ◽  
Cell Surfaces ◽  
Cell Surface Antigens ◽  
Ganglion Neurons

To investigate the cellular and molecular signals underlying regulation of cell adhesion molecule expression, the influence of interactions between dorsal root ganglion neurons and Schwann cells on their expression of L1 and N-CAM was quantitated by immunogold electronmicroscopy. The numbers of antibody binding sites on cell surfaces of neurons and glia were compared between pure populations and co-cultures. After 3 d of co-culture, expression of L1 was reduced by 91% on Schwann cells and 36% on neurons, with expression in pure cultures being taken as 100%. N-CAM expression was unchanged on neurons and reduced by 43% on Schwann cells. Within 3 d after removal of neurons from Schwann cell-neuron co-cultures by immunocytolysis, expression of L1 and N-CAM on Schwann cell surfaces increased by 69 and 84%, respectively. Cell surface antigens recognized by an antibody to mouse liver membranes were unchanged in co-cultures. Furthermore, in co-cultures of neurons and sciatic nerve fibroblasts neither of the three antibodies detected any changes in expression of antigens when pure and co-cultures were compared. These observations suggest that adhesion molecules are not only involved in neuron-Schwann cell recognition and neurite outgrowth on Schwann cells (Seilheimer, B., and M. Schachner. 1988. J. Cell Biol. 107: 341-351), but that cell interactions, in turn, modulate the extent of adhesion molecule expression.

scholarly journals A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth

1992 ◽  
Vol 117 (4) ◽  
pp. 877-887 ◽  
Author(s):  
P Durbec ◽  
G Gennarini ◽  
C Goridis ◽  
G Rougon
Keyword(s):  
Cell Adhesion ◽  
Neurite Outgrowth ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dorsal Root Ganglion Neurons ◽  
Soluble Form ◽  
Dependent Manner ◽  
Neurite Initiation ◽  
Ganglion Neurons ◽  
Adhesive Proteins

The F3 molecule is a member of the immunoglobulin superfamily anchored to membranes by a glycane-phosphatidylinositol, and is predominantly expressed on subsets of axons of the central and peripheral nervous system. In a previous paper (Gennarini, G., P. Durbec, A. Boned, G. Rougon, and C. Goridis. 1991. Neuron. 6:595-606), we have established that F3 fulfills the operational definition of a cell adhesion molecule and that it stimulates neurite outgrowth when presented to sensory neurons as a surface component of transfected CHO cells. In the present study the question as to whether soluble forms of F3 would be functionally active was addressed in vitro on cultures of mouse dorsal root ganglion neurons. We observed that preparations enriched in soluble F3 had no effect on neuron attachment but enhanced neurite initiation and neurite outgrowth in a dose-dependent manner. By contrast, soluble NCAM-120 does not have any measurable effect on these phenomena. Addition of anti-F3 monovalent antibodies reduced the number of process-bearing neurons and the neuritic output per neuron to control values. Addition of cerebrospinal fluid, a natural source of soluble F3, also stimulated neurite extension, and this effect was partially blocked by anti-F3 antibodies. Our results suggest that the soluble forms of adhesive proteins with neurite outgrowth-promoting properties could act at a distance from their site of release in a way reminiscent of growth and trophic factors.

O-glycosylation pattern of CD24 from mouse brain

2009 ◽  
Vol 390 (7) ◽  
Author(s):  
Christina Bleckmann ◽  
Hildegard Geyer ◽  
Annika Lieberoth ◽  
Frauke Splittstoesser ◽  
Yan Liu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Sialic Acid ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Ion Trap ◽  
Biological Activities ◽  
Tumor Biology ◽  
Dorsal Root Ganglion Neurons ◽  
Glycosylation Pattern ◽  
Ganglion Neurons

AbstractThe cell adhesion molecule CD24 is a highly glycosylated glycoprotein that plays important roles in the central nervous system, the immune system and in tumor biology. Since CD24 comprises only a short protein core of approximately 30 amino acids and low conservation among species, it has been proposed that the functions of CD24 are mediated by its glycosylation pattern. Our present study provides evidence that interaction of CD24 with the cell adhesion molecule L1 is mediated by O-linked glycans carrying α2,3-linked sialic acid. Furthermore, de-N-glycosylated CD24 was shown to promote or inhibit neurite outgrowth of cerebellar neurons or dorsal root ganglion neurons, respectively, to the same extent as untreated CD24. Therefore, this study is focused on the structural elucidation of the chemically released, permethylated CD24 O-glycans by electrospray ionization ion trap mass spectrometry. Our analyses revealed the occurrence of a diverse mixture of mucin-type and O-mannosyl glycans carrying, in part, functionally relevant epitopes, such as 3-linked sialic acid, disialyl motifs, LeX, sialyl-LeXor HNK-1 units. Hence, our data provide the basis for further studies on the contribution of carbohydrate determinants to CD24-mediated biological activities.

scholarly journals Antibodies to the L1 adhesion molecule inhibit Schwann cell ensheathment of neurons in vitro.

1989 ◽  
Vol 109 (6) ◽  
pp. 3095-3103 ◽  
Author(s):  
B Seilheimer ◽  
E Persohn ◽  
M Schachner
Keyword(s):  
Cell Differentiation ◽  
Schwann Cell ◽  
Schwann Cells ◽  
Adhesion Molecule ◽  
Neuronal Cell ◽  
Dorsal Root Ganglion Neurons ◽  
Neural Adhesion Molecule ◽  
Ganglion Neurons ◽  
Schwann Cell Differentiation

To investigate whether neural adhesion molecules are involved in neuron-induced Schwann cell differentiation, cocultures of pure dorsal root ganglion neurons, and Schwann cells were maintained in the presence of antibodies to evaluate possible perturbing effects. Several parameters characteristic of differentiating Schwann cells were studied, such as transition of spindle-shaped to flattened, i.e., more epithelioid morphology, association with neuronal cell bodies, ensheathment of neurites, production of basal lamina and collagen fibrils, and expression of the myelin associated glycoprotein (MAG). A complete ablation of Schwann cell differentiation in all features studied was seen with antibodies to the neural adhesion molecule L1. Antibodies to N-CAM did not reduce the association of Schwann cells with neurites but abolished the interdigitation of Schwann cell processes into neurite bundles, while leaving the other parameters studied unaffected. Fab fragments of antibodies to J1, MAG, and mouse liver membranes did not interfere with the manifestation of any of these parameters. None of the antibodies changed incorporation of [3H]thymidine into Schwann cells.

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