scholarly journals Specific asparagine-linked oligosaccharides are not required for certain neuron-neuron and neuron-Schwann cell interactions.

1986 ◽  
Vol 103 (1) ◽  
pp. 159-170 ◽  
Author(s):  
N Ratner ◽  
A Elbein ◽  
M B Bunge ◽  
S Porter ◽  
R P Bunge ◽  
...  
Keyword(s):  
Schwann Cell ◽  
Schwann Cells ◽  
Normal Structure ◽  
Cell Interactions ◽  
Dorsal Root Ganglion Neurons ◽  
Neuronal Cultures ◽  
Cellular Functions ◽  
Matrix Deposition ◽  
Neuronal Proteins ◽  
Ganglion Neurons

To determine whether specific asparagine-linked (N-linked) oligosaccharides present in cell surface glycoproteins are required for cell-cell interactions within the peripheral nervous system, we have used castanospermine to inhibit maturation of N-linked sugars in cell cultures of neurons or neurons plus Schwann cells. Maximally 10-15% of the N-linked oligosaccharides on neuronal proteins have normal structure when cells are cultured in the presence of 250 micrograms/ml castanospermine; the remaining oligosaccharides are present as immature carbohydrate chains not normally found in these glycoproteins. Although cultures were treated for 2 wk with castanospermine, cells always remained viable and appeared healthy. We have analyzed several biological responses of embryonic dorsal root ganglion neurons, with or without added purified populations of Schwann cells, in the presence of castanospermine. We have observed that a normal complement of mature, N-linked sugars are not required for neurite outgrowth, neuron-Schwann cell adhesion, neuron-induced Schwann cell proliferation, or ensheathment of neurites by Schwann cells. Treatment of neuronal cultures with castanospermine increases the propensity of neurites to fasciculate. Extracellular matrix deposition by Schwann cells and myelination of neurons by Schwann cells are greatly diminished in the presence of castanospermine as assayed by electron microscopy and immunocytochemistry, suggesting that specific N-linked oligosaccharides are required for the expression of these cellular functions.

scholarly journals Studies of adhesion molecules mediating interactions between cells of peripheral nervous system indicate a major role for L1 in mediating sensory neuron growth on Schwann cells in culture.

1988 ◽  
Vol 107 (1) ◽  
pp. 341-351 ◽  
Author(s):  
B Seilheimer ◽  
M Schachner
Keyword(s):  
Nervous System ◽  
Dorsal Root Ganglion ◽  
Schwann Cell ◽  
Neurite Outgrowth ◽  
Adhesion Molecules ◽  
Schwann Cells ◽  
Dorsal Root ◽  
Dorsal Root Ganglion Neurons ◽  
Ganglion Neurons ◽  
Large Neurons

The involvement of the adhesion molecules L1, N-CAM, and J1 in adhesion and neurite outgrowth in the peripheral nervous system was investigated. We prepared Schwann cells and fibroblasts (from sciatic nerves) and neurons (from dorsal root ganglia) from 1-d mice. These cells were allowed to interact with each other in a short-term adhesion assay. We also measured outgrowth of dorsal root ganglion neurons on Schwann cell and fibroblast monolayers. Schwann cells (which express L1, N-CAM, and J1) adhered most strongly to dorsal root ganglion neurons by an L1-dependent mechanism and less by N-CAM and J1. Schwann cell-Schwann cell adhesion was mediated by L1 and N-CAM, but not J1. Adhesion of fibroblasts (which express N-CAM, but not L1 or J1) to neurons or Schwann cells was mediated by L1 and N-CAM and not J1. However, inhibition by L1 and N-CAM antibodies was found to be less pronounced with fibroblasts than with Schwann cells. N-CAM was also strongly involved in fibroblast-fibroblast adhesion. Neurite outgrowth was most extensive on Schwann cells and less on fibroblasts. A difference in extent of neurite elongation was seen between small- (10-20 microns) and large- (20-35 microns) diameter neurons, with the larger neurons tending to exhibit longer neurites. Fab fragments of polyclonal L1, N-CAM, and J1 antibodies exerted slightly different inhibitory effects on neurite outgrowth, depending on whether the neurites were derived from small or large neurons. L1 antibodies interfered most strikingly with neurite outgrowth on Schwann cells (inhibition of 88% for small and 76% for large neurons), while no inhibition was detectable on fibroblasts. Similarly, although to a smaller extent than L1, N-CAM appeared to be involved in neurite outgrowth on Schwann cells and not on fibroblasts. Antibodies to J1 only showed a very small effect on neurite outgrowth of large neurons on Schwann cells. These observations show for the first time that identified adhesion molecules are potent mediators of glia-dependent neurite formation and attribute to L1 a predominant role in neurite outgrowth on Schwann cells which may be instrumental in regeneration.

scholarly journals A neuronal cell surface heparan sulfate proteoglycan is required for dorsal root ganglion neuron stimulation of Schwann cell proliferation.

1985 ◽  
Vol 101 (3) ◽  
pp. 744-754 ◽  
Author(s):  
N Ratner ◽  
R P Bunge ◽  
L Glaser
Keyword(s):  
Dorsal Root Ganglion ◽  
Schwann Cell ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Schwann Cells ◽  
Dorsal Root ◽  
Dorsal Root Ganglion Neurons ◽  
Sulfate Proteoglycan ◽  
Mitogenic Response ◽  
Ganglion Neurons

Axons of dorsal root ganglion neurons express on their surfaces one or more proteins which are mitogenic for Schwann cells (Salzer, J., R. P. Bunge, and L. Glaser, 1980, J. Cell Biol., 84:767-778). Incubation of co-cultures of dorsal root ganglion neurons and Schwann cells with 4-methylumbelliferyl-beta-D-xyloside, an inhibitor of proteoglycan biosynthesis, decreases the mitogenic response of the Schwann cell by over 95%. The effect of the beta-D-xyloside has been localized to the neurons; pretreatment of neurons but not of Schwann cells with the inhibitor causes a marked reduction of the mitogenic response. In addition, Schwann cells treated with beta-D-xyloside are still mitogenically responsive to soluble Schwann cell mitogens (cholera toxin and glial growth factor). Neurons treated with heparitinase and membrane vesicles prepared from heparitinase-treated neurons show diminished mitogenicity for Schwann cells, while other proteoglycan lyases have no effect. We conclude that a cell surface heparan sulfate proteoglycan is a component of the Schwann cell mitogen present on the surface of dorsal root ganglion neurons.

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.

scholarly journals Expression of P30, a protein with adhesive properties, in Schwann cells and neurons of the developing and regenerating peripheral nerve.

1991 ◽  
Vol 112 (6) ◽  
pp. 1229-1239 ◽  
Author(s):  
M M Daston ◽  
N Ratner
Keyword(s):  
Nervous System ◽  
Schwann Cell ◽  
Schwann Cells ◽  
Dorsal Root Ganglion Neurons ◽  
Cell Contact ◽  
Heparin Binding ◽  
Adhesive Properties ◽  
Ganglion Neurons ◽  
Developing Rat

P30 is a heparin-binding protein with adhesive and neurite outgrowth-promoting properties present at high levels in the developing rat central nervous system (Rauvala, H., and R. Pihlaskari. 1987 J. Biol. Chem. 262:16625-16635). Partial sequencing of p30 has revealed homology or identity with HMG-1 (Rauvala, H., J. Merenmies, R. Pihlaskari, M. Korkolainen, M.-L. Huhtala, and P. Panula. 1988. J. Cell Biol. 107:2292-2305), a 28-kD protein that was originally purified from the thymus (Goodwin, G.H., C. Sanders, and E. W. Johns. 1973. Eur. J. Biochem. 38:14-19) which binds DNA in vitro. We have analyzed the distribution of p30 in the developing rat peripheral nervous system (PNS). P30 was detected by immunohistochemistry and Western blot analysis using antibodies raised against intact p30 and against a synthetic peptide corresponding to the amino terminus of the p30 molecule. P30 was localized to nonnuclear compartments of neurons and peripheral glial cells (Schwann cells). P30 immunoreactivity of PNS neurons persisted into adulthood. In contrast, Schwann cell staining decreased after the second postnatal week and was not detectable in adult animals. Neuron-Schwann cell contact was correlated with diminished p30 levels in Schwann cells. Schwann cells of the normal adult sciatic nerve did not express p30; however, when deprived of axonal contact by nerve transection, the Schwann cells of the distal nerve stained intensely for p30. In addition, when Schwann cells and dorsal root ganglion neurons were grown in coculture, Schwann cells that were associated with neurites were not as intensely stained by anti-p30 as Schwann cells that were not in contact with neurons. The pattern of p30 expression during development and regeneration, and its apparent regulation by cell-cell contact suggests that p30 plays a role in the interaction between neurons and Schwann cells during morphogenesis of peripheral nerves.

Expressing antisense P0 RNA in Schwann cells perturbs myelination

Development ◽  
1991 ◽  
Vol 112 (2) ◽  
pp. 639-649
Author(s):  
G.C. Owens ◽  
C.J. Boyd
Keyword(s):  
Schwann Cell ◽  
Schwann Cells ◽  
Dorsal Root Ganglion Neurons ◽  
Beta Actin ◽  
Actin Promoter ◽  
Dominant Selectable Marker ◽  
Myelin Associated Glycoprotein ◽  
Ganglion Neurons ◽  
Schwann Cell Differentiation

Primary Schwann cells were infected in vitro with a recombinant retrovirus expressing a dominant selectable marker, neomycin phosphotransferase (conferring resistance to the drug G418), and antisense P0 RNA under the control of the human beta-actin promoter. A proportion of the G418-resistant cells failed to form myelin when cocultured with dorsal root ganglion neurons under conditions that promote Schwann cell differentiation. These cells expressed high levels of P0 antisense RNA. Among the impaired cells, the majority had segregated and ensheathed individual axon but had not differentiated further. They did not express P0 but did express myelin- associated glycoprotein and galactocerebroside. A minority of partially inhibited Schwann cells were also observed that elaborated thin myelin sheaths containing variable numbers of compacted and noncompacted lamellae. These data indicate that restricting the level of P0 expression inhibits spiralling of the Schwann cell membrane and subsequent compaction.

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 Promoting Neuronal Outgrowth Using Ridged Scaffolds Coated with Extracellular Matrix Proteins

Biomedicines ◽  
2021 ◽  
Vol 9 (5) ◽  
pp. 479
Author(s):  
Ahad M. Siddiqui ◽  
Rosa Brunner ◽  
Gregory M. Harris ◽  
Alan Lee Miller ◽  
Brian E. Waletzki ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Extracellular Matrix ◽  
Schwann Cells ◽  
Cell Attachment ◽  
Dorsal Root Ganglion Neurons ◽  
Neurologic Recovery ◽  
Cord Injury ◽  
Biodegradable Hydrogel ◽  
Ganglion Neurons ◽  
Novel Scaffold

Spinal cord injury (SCI) results in cell death, demyelination, and axonal loss. The spinal cord has a limited ability to regenerate, and current clinical therapies for SCI are not effective in helping promote neurologic recovery. We have developed a novel scaffold biomaterial that is fabricated from the biodegradable hydrogel oligo(poly(ethylene glycol)fumarate) (OPF). We have previously shown that positively charged OPF scaffolds (OPF+) in an open spaced, multichannel design can be loaded with Schwann cells to support axonal generation and functional recovery following SCI. We have now developed a hybrid OPF+ biomaterial that increases the surface area available for cell attachment and that contains an aligned microarchitecture and extracellular matrix (ECM) proteins to better support axonal regeneration. OPF+ was fabricated as 0.08 mm thick sheets containing 100 μm high polymer ridges that self-assemble into a spiral shape when hydrated. Laminin, fibronectin, or collagen I coating promoted neuron attachment and axonal outgrowth on the scaffold surface. In addition, the ridges aligned axons in a longitudinal bipolar orientation. Decreasing the space between the ridges increased the number of cells and neurites aligned in the direction of the ridge. Schwann cells seeded on laminin coated OPF+ sheets aligned along the ridges over a 6-day period and could myelinate dorsal root ganglion neurons over 4 weeks. This novel scaffold design, with closer spaced ridges and Schwann cells, is a novel biomaterial construct to promote regeneration after SCI.

Axon-Schwann cell interactions regulate the expression of c-jun in Schwann cells

1996 ◽  
Vol 43 (5) ◽  
pp. 511-525 ◽  
Author(s):  
M.E. Shy ◽  
Y. Shi ◽  
L. Wrabetz ◽  
J. Kamholz ◽  
S.S. Scherer
Keyword(s):  
Schwann Cell ◽  
Schwann Cells ◽  
Cell Interactions
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