The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180

Pesheva, Penka; Gennarini, Gianfranco; Goridis, Christo; Schachner, Melitta

doi:10.1016/0896-6273(93)90243-k

Cited by 235 publications

(151 citation statements)

References 61 publications

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“…Immunohistochemistry and in situ hybridization reveal that F11 shows a significant overlap in its expression pattern with TN-R or TN-C, but there are also spatial and temporal differences (14,16,39). This is consistent with the possibility of interactions between these proteins as well as competition between them for ligands.…”

supporting

confidence: 69%

“…One explanation for the functional effect of TN-R described here might be that the interaction between TN-R and F11 induces a conformation in TN-R that is suitable for the induction of neurite outgrowth. Alternatively, inhibitory sites on TN-R could be masked by interaction with F11 (14). Similar mechanisms might be discussed for the interaction between TN-C and F11.…”

Section: Discussionmentioning

confidence: 77%

“…Interactions with the cell surface proteins NgCAM, NrCAM, neurofascin, Caspr, and RPTP␤/ and the ECM glycoproteins tenascin-R (TN-R) and tenascin-C (TN-C) have been revealed by in vitro assays (7)(8)(9)(10)(11)(12)(13)(14)(15)(16). The N-terminal Ig domains 1-4 of the F11 polypeptide are sufficient for interactions with NgCAM, NrCAM, TN-R, and TN-C, although binding assays with domain-specific anti-F11 monoclonal antibodies and with F11 domain deletion mutants suggest that individual domains of the four N-terminal domains might be more important for specific bindings (8 -10, 15).…”

mentioning

confidence: 99%

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Functional Interactions of the Immunoglobulin Superfamily Member F11 Are Differentially Regulated by the Extracellular Matrix Proteins Tenascin-R and Tenascin-C

Zacharias

Nörenberg

Rathjen

1999

Journal of Biological Chemistry

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The axon-associated protein F11 is a GPI-anchored member of the immunoglobulin superfamily that promotes axon outgrowth and that shows a complex binding pattern toward multiple cell surface and extracellular matrix proteins including tenascin-R and tenascin-C. In this study, we demonstrate that tenascin-R and tenascin-C differentially modulate cell adhesion and neurite outgrowth of tectal cells on F11. While soluble tenascin-R increases the number of attached cells and the percentage of cells with neurites on immobilized F11, tenascin-C stimulates cell attachment to a similar extent but decreases neurite outgrowth. The cellular receptor interacting with F11 has been previously identified as NrCAM; however, in the presence of tenascin-R or tenascin-C cell attachment and neurite extension are independent of NrCAM. Antibody perturbation experiments indicate that ␤ 1 integrins instead of NrCAM function as receptor for neurite outgrowth of tectal cells on an F11⅐TN-R complex. Cellular binding assays support the possibility that the interaction of F11 to NrCAM is blocked in the presence of tenascin-R and tenascin-C. Furthermore, a sandwich binding assay demonstrates that tenascin-R and tenascin-C are able to form larger molecular complexes and to link F11 polypeptides by forming a molecular bridge.These results suggest that the molecular interactions of F11 might be regulated by the presence of tenascin-R and tenascin-C. Cell adhesion molecules (CAMs)1 of the immunoglobulin superfamily (IgSF) act in concert with other cell surface molecules and extracellular matrix (ECM) proteins to regulate cell migration, axonal growth, and guidance during development of the nervous system. IgSF members coexist on many extending axons and show a transient expression pattern during early stages of development. The multidomain nature of glycoproteins of the IgSF suggest that they regulate axonal pathfinding by multiple complex interactions with other axonal and ECM molecules (1).The axon-associated F11 glycoprotein is composed of six Nterminal Ig domains followed by four fibronectin type III (FNIII) domains and a glycosylphosphatidylinositol anchor and has been implicated in axonal growth and fasciculation (2-6).As found for other axonal members of the IgSF, the F11 polypeptide shows a broad binding activity. Interactions with the cell surface proteins NgCAM, NrCAM, neurofascin, Caspr, and RPTP␤/ and the ECM glycoproteins tenascin-R (TN-R) and tenascin-C (TN-C) have been revealed by in vitro assays (7-16). The N-terminal Ig domains 1-4 of the F11 polypeptide are sufficient for interactions with NgCAM, NrCAM, TN-R, and TN-C, although binding assays with domain-specific anti-F11 monoclonal antibodies and with F11 domain deletion mutants suggest that individual domains of the four N-terminal domains might be more important for specific bindings (8 -10, 15). The interaction between immobilized F11 and neuronal NrCAM induces neurite outgrowth of tectal cells (10). TN-R and TN-C are two major members of the tenascin family of ECM glycoprote...

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supporting

confidence: 69%

Section: Discussionmentioning

confidence: 77%

mentioning

confidence: 99%

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Functional Interactions of the Immunoglobulin Superfamily Member F11 Are Differentially Regulated by the Extracellular Matrix Proteins Tenascin-R and Tenascin-C

Zacharias

Nörenberg

Rathjen

1999

Journal of Biological Chemistry

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“…Soluble CSs promote the growth of optic axons of goldfish (Challacombe and Elam, 1997). This underscores that the axonal reaction to CSs (Snow and Letourneau, 1992;Snow et al, 1996;Hynds and Snow, 1999) and also to other matrix molecules, such as tenascins (Lochter et al, 1991Lochter and Schachner, 1993;Pesheva et al, 1993;Taylor et al, 1993), depends on the way the molecules are presented to the axons (as a homogeneous or step gradient substrate or soluble in the culture medium). The complex reactions of developing optic axons in slice cultures of the optic chiasm of mice (Chung et al, 2000) to the removal of CSs may be related to the potential role of the spatial configuration in which the molecules are encountered in a specific CNS structure.…”

Section: Discussionmentioning

confidence: 79%

Repellent Guidance of Regenerating Optic Axons by Chondroitin Sulfate Glycosaminoglycans in Zebrafish

Becker

2002

J. Neurosci.

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We analyzed the role of chondroitin sulfate (CS) glycosaminoglycans, putative inhibitors of axonal regeneration in mammals, in the regenerating visual pathway of adult zebrafish. In the adult, CS immunoreactivity was not detectable before or after an optic nerve crush in the optic nerve and tract but was constitutively present in developing and adult nonretinorecipient pretectal brain nuclei, where CSs may form a boundary preventing regenerating optic fibers from growing into these inappropriate locations. Enzymatic removal of CSs by chondroitinase ABC after optic nerve crush significantly increased the number of animals showing erroneous growth of optic axons into the nonretinorecipient magnocellular superficial/ posterior pretectal nucleus (83% vs 42% in controls). In vitro, a substrate border of CSs, but not heparan sulfates, strongly repelled regenerating retinal axons from adult zebrafish. We conclude that CSs contribute to repellent axon guidance during regeneration of the optic projection in zebrafish.

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“…However, each also has distinct binding capabilities (e.g. F3/contactin-tenascin R, TAG-1-neurocan) (Pesheva et al, 1993;Milev et al, 1996) and, in some contexts, F3/contactin may inhibit neurite outgrowth (Buttiglione et al, 1996;Buttiglione et al, 1998). In the cerebellum, TAG-1 is predominantly expressed on premigratory granule neurons in the external granular layer (EGL) whereas F3/contactin peaks on postmitotic migrating neurons (Faivre-Sarrailh et al, 1992;Wolfer et al, 1994;Wolfer et al, 1998;Stottmann et al, 1998;Virgintino et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Transgenic mice expressing F3/contactin from the TAG-1 promoter exhibit developmentally regulated changes in the differentiation of cerebellar neurons

Virgintino²,

et al. 2003

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F3/contactin (CNTN1) and TAG-1 (CNTN2) are closely related axonal glycoproteins that are differentially regulated during development. In the cerebellar cortex TAG-1 is expressed first as granule cell progenitors differentiate in the premigratory zone of the external germinal layer. However, as these cells begin radial migration, TAG-1 is replaced by F3/contactin. To address the significance of this differential regulation, we have generated transgenic mice in which F3/contactin expression is driven byTAG-1 gene regulatory sequences, which results in premature expression of F3/contactin in granule cells. These animals (TAG/F3mice) display a developmentally regulated cerebellar phenotype in which the size of the cerebellum is markedly reduced during the first two postnatal weeks but subsequently recovers. This is due in part to a reduction in the number of granule cells, most evident in the external germinal layer at postnatal day 3 and in the inner granular layer between postnatal days 8 and 11. The reduction in granule cell number is accompanied by a decrease in precursor granule cell proliferation at postnatal day 3, followed by an increase in the number of cycling cells at postnatal day 8. In the same developmental window the size of the molecular layer is markedly reduced and Purkinje cell dendrites fail to elaborate normally. These data are consistent with a model in which deployment of F3/contactin on granule cells affects proliferation and differentiation of these neurons as well as the differentiation of their synaptic partners, the Purkinje cells. Together,these findings indicate that precise spatio-temporal regulation of TAG-1 and F3/contactin expression is critical for normal cerebellar morphogenesis.

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The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180

Cited by 235 publications

References 61 publications

Functional Interactions of the Immunoglobulin Superfamily Member F11 Are Differentially Regulated by the Extracellular Matrix Proteins Tenascin-R and Tenascin-C

Functional Interactions of the Immunoglobulin Superfamily Member F11 Are Differentially Regulated by the Extracellular Matrix Proteins Tenascin-R and Tenascin-C

Repellent Guidance of Regenerating Optic Axons by Chondroitin Sulfate Glycosaminoglycans in Zebrafish

Transgenic mice expressing F3/contactin from the TAG-1 promoter exhibit developmentally regulated changes in the differentiation of cerebellar neurons

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