J1/tenascin is a repulsive substrate for central nervous system neurons

Faissner, Andréas; Kruse, Jan

doi:10.1016/0896-6273(90)90217-4

Cited by 364 publications

(272 citation statements)

References 54 publications

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“…One week later, 50 g of the antigen in PBS (137 mM NaCl, 3 mM KCl, 6.5 mM Na 2 HPO 4 , 1.5 mM KH 2 PO 4 ), pH 7.4, was injected into the tail vein, and fusions were carried out 4 days thereafter by using the mouse myeloma line X-Ag8 -653 as described (10,24). Supernatants reactive with the antigen were detected with an enzyme-linked immunosorbent assay and further characterized by immunocytology on mouse postnatal cerebellar cultures.…”

Section: Methodsmentioning

confidence: 99%

Structurally Distinct LewisX Glycans Distinguish Subpopulations of Neural Stem/Progenitor Cells

Hennen

Czopka

Faissner

2011

Journal of Biological Chemistry

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There is increasing evidence that the stem and progenitor cell population that builds the central nervous system is very heterogeneous. Stem cell markers with the potential to divide this cell pool into subpopulations with distinct characteristics are sparse. We were looking for new cell type-specific antigens to further subdivide the progenitor pool. Here, we introduce the novel monoclonal antibody clone 5750. We show that it specifically labels cell surfaces of neural stem and progenitor cells. When 5750-expressing cells were isolated by fluorescence-activated cell sorting from embryonic mouse brains, the sorted population showed increased neurosphere forming capacity and multipotency. Neurospheres generated from 5750-positive cells could self-renew and remained multipotent even after prolonged passaging. Carbohydrate binding assays revealed that the 5750 antibody specifically binds to LewisX-related carbohydrates. Interestingly, we found that the LewisX epitope recognized by clone 5750 differs from those detected by other antiLewisX antibody clones like 487LeX , SSEA-1 LeX , and MMA LeX . Our data further reveal that individual anti-LewisX clones can be successfully used to label and deplete different subpopulations of neural cells in vivo and in vitro. In conclusion, we present a new tool for the isolation and characterization of neural subpopulations and provide insights into the complexity of cell surface glycosylation.

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Section: Methodsmentioning

confidence: 99%

Structurally Distinct LewisX Glycans Distinguish Subpopulations of Neural Stem/Progenitor Cells

Hennen

Czopka

Faissner

2011

Journal of Biological Chemistry

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“…The supernatant was dialyzed against 50 mM imidazole/HCl, pH 7.4, lyophilized, resuspended in PBS, and precleared for 5 min at 5000 ϫ g. BALB/c mice were injected four times intraperitoneally with 50 g of the protein fraction at intervals of 3-4 weeks. 4 days after the final injection, spleens were removed, and the splenocytes were fused with the myeloma line X63Ag8.653 as described previously (24). A second immunization was performed with the PBS-insoluble material after solubilization with 8 M urea and diluted to a final concentration of 0.85 M urea in PBS.…”

Section: Methodsmentioning

confidence: 99%

Differential and Regulated Binding of cAMP-dependent Protein Kinase and Protein Kinase C Isoenzymes to Gravin in Human Model Neurons

Piontek

Brandt

2003

Journal of Biological Chemistry

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The membrane cortex has an important role in generating and maintaining spatially and functionally distinct domains in neurons. As a tool to functionally characterize molecules of the membrane cortex, we generated novel monoclonal antibodies against a fraction enriched for components of the neuronal membrane skeleton. We obtained two antibodies against the kinase-anchoring protein gravin. Gravin was strongly up-regulated during differentiation of human model neurons (NT2-N neurons) and was enriched at the inner peripheral cortex in close proximity to the plasma membrane where its localization primarily depended on association with membranes. In differentiated neurons, gravin colocalized in putative signaling complexes with protein kinase C (PKC␤II) and partially with PKC␣ and cAMP-dependent protein kinase (PKA). Colocalization with PKC⑀ was not observed. PKC␤II, PKC␣, and PKA but not PKC⑀ coprecipitated with gravin indicating physical interaction. Binding of gravin to PKC␣ required the presence of Ca 2؉ and was increased after inhibition of PKC. In contrast, binding of PKC␤II and PKA were independent of Ca 2؉ and PKC inhibition. Activation of PKC decreased binding of PKC␣ to gravin, decreased its association with the plasma membrane, and reduced the mean size of gravin particles. Taken together the data suggest that gravin provides a dynamic platform to localize kinases in an isoenzyme-specific and activation-dependent manner at specific sites in neurons.During development, many neurons establish a complex morphology that is characterized by the formation of multiple and in many cases highly branched neurites. Within the neurites, many organelles and proteins exhibit a nonuniform distribution that is thought to provide the basis for the formation of structurally and functionally distinct domains. For example, mitochondria are clustered at sites of high energy consumption, and several cytoskeleton-associated proteins are enriched at positions where active process outgrowth occurs. Some kinases and phosphatases also show a nonuniform distribution in neurons and are enriched at specific regions. In many cases this is achieved by locally anchoring them to cytosolic filament systems or to components of the cortical membrane skeleton.

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“…according to Faissner and Kruse (1990). Positive clones were selected by surface staining of cells of the Oli-neu cell line and primary oligodendrocytes, followed by Western blot analysis.…”

Section: Methodsmentioning

confidence: 99%

“…The inhibition of neural cell attachment test was performed as described in Faissner and Kruse (1990). In brief, glass coverslips were coated with poly-L-ornithine (PORN), which was allowed to dry.…”

Section: Methodsmentioning

confidence: 99%

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

et al. 1999

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Myelination by oligodendrocytes in the CNS involves the migration to and recognition and ensheathment of axons. These distinct developmental phases of myelination are assumed to involve the interplay of a precisely regulated set of cell adhesion molecules expressed by both neurons and glial cells. These molecules remain largely unelucidated. In this paper we have identified a large (330 kDa) glycoprotein expressed by murine oligodendrocyte progenitor cells in vitro and in vivo that is downregulated as oligodendrocytes mature. Antigen-positive oligodendrocyte progenitor cells purified by panning develop into myelin-associated glycoprotein-positive oligodendrocytes and also adhere to cultured neurons. Polyclonal antibodies directed against the protein reduce the migration of oligodendrocyte progenitor cells. The observations suggest that the AN2 antigen may play a role in early stages of myelination.

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J1/tenascin is a repulsive substrate for central nervous system neurons

Cited by 364 publications

References 54 publications

Structurally Distinct LewisX Glycans Distinguish Subpopulations of Neural Stem/Progenitor Cells

Structurally Distinct LewisX Glycans Distinguish Subpopulations of Neural Stem/Progenitor Cells

Differential and Regulated Binding of cAMP-dependent Protein Kinase and Protein Kinase C Isoenzymes to Gravin in Human Model Neurons

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

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