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 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.

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 Mapping of three carbohydrate attachment sites in embryonic and adult forms of the neural cell adhesion molecule.

1984 ◽  
Vol 99 (5) ◽  
pp. 1848-1855 ◽  
Author(s):  
K L Crossin ◽  
G M Edelman ◽  
B A Cunningham
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Sialic Acid ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Attachment Sites ◽  
Neural Cell Adhesion

The sialic-rich carbohydrate moiety of the neural cell adhesion molecule (N-CAM) undergoes major structural changes during development and plays a significant role in altering the homophilic binding of the molecule. In order to understand the mechanism of these changes, a cyanogen bromide (CNBr) fragment that contained 90% of the sialic acid of N-CAM was isolated and characterized according to the number of carbohydrate attachment sites and reactivity with specific monoclonal antibodies. The CNBr sialopeptide migrated on SDS PAGE as a broad zone of Mr 42,000-60,000. Upon treatment with neuraminidase, it was converted to a single component of Mr 42,000, and subsequent, limited treatment with endoglycosidase F gave four evenly spaced components of Mr 35,000-42,000, suggesting that it contained three attachment sites for N-linked oligosaccharides. The fragment reacted with monoclonal antibody 15G8, which detects the sialic acid in embryonic N-CAM, and with a monoclonal antibody, anti-(N-CAM) No. 2. Treatment with neuraminidase or with endoglycosidase F destroyed reactivity with 15G8 but not with anti-(N-CAM) No. 2. A similar CNBr sialopeptide was obtained from adult N-CAM; it contained sialic acid, had three N-linked oligosaccharides and reacted with anti-(N-CAM) No. 2 but not with 15G8 monoclonal antibodies. A peptide fragment, Fr2, comprising the NH2 terminal and middle regions of the molecule yielded a CNBr fragment closely similar to the fragment obtained from the whole molecule. The CNBr fragment from Fr2 reacted with monoclonal antibody anti-(N-CAM) No. 2. Fr1, comprising the NH2 terminal region alone, failed to react. These data confirm that the majority of the sialic acid is localized in the middle region of the N-CAM molecule and support the hypothesis that embryonic to adult conversion of N-CAM is the result of differences in sialidase or sialytransferase activity.

scholarly journals The Cell Adhesion Molecule “CAR” and Sialic Acid on Human Erythrocytes Influence Adenovirus In Vivo Biodistribution

2009 ◽  
Vol 5 (1) ◽  
pp. e1000277 ◽  
Author(s):  
Elena Seiradake ◽  
Daniel Henaff ◽  
Harald Wodrich ◽  
Olivier Billet ◽  
Matthieu Perreau ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Sialic Acid ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Human Erythrocytes ◽  
In Vivo Biodistribution

scholarly journals N-cadherin, NCAM, and integrins promote retinal neurite outgrowth on astrocytes in vitro.

1988 ◽  
Vol 107 (3) ◽  
pp. 1177-1187 ◽  
Author(s):  
K M Neugebauer ◽  
K J Tomaselli ◽  
J Lilien ◽  
L F Reichardt
Keyword(s):  
Cell Adhesion ◽  
Neurite Outgrowth ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neuronal Cell ◽  
Optic Pathway ◽  
Retinal Neurons ◽  
Inhibitory Effects ◽  
Axon Extension ◽  
Ganglion Neurons

Retinal ganglion neurons extend axons that grow along astroglial cell surfaces in the developing optic pathway. To identify the molecules that may mediate axon extension in vivo, antibodies to neuronal cell surface proteins were tested for their effects on neurite outgrowth by embryonic chick retinal neurons cultured on astrocyte monolayers. Neurite outgrowth by retinal neurons from embryonic day 7 (E7) and E11 chick embryos depended on the function of a calcium-dependent cell adhesion molecule (N-cadherin) and beta 1-class integrin extracellular matrix receptors. The inhibitory effects of either antibody on process extension could not be accounted for by a reduction in the attachment of neurons to astrocytes. The role of a third cell adhesion molecule, NCAM, changed during development. Anti-NCAM had no detectable inhibitory effects on neurite outgrowth by E7 retinal neurons. In contrast, E11 retinal neurite outgrowth was strongly dependent on NCAM function. Thus, N-cadherin, integrins, and NCAM are likely to regulate axon extension in the optic pathway, and their relative importance varies with developmental age.

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