Functional characterization of chondroitin sulfate proteoglycans of brain: interactions with neurons and neural cell adhesion molecules.

Grumet, Martin; Flaccus, Andrea; Margolis, Richard U.

doi:10.1083/jcb.120.3.815

Cited by 311 publications

(221 citation statements)

References 58 publications

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“…For example, Chaudhry et al (2006) found that co-expression of L1 with nerve growth factor reduced CGRP-positive sprouting within the spinal cord, and that this reduction did not occur with other cell adhesion molecules. Furthermore, this finding (Chaudhry et al, 2006) is supported by the growth-cone collapsing interaction of L1 with neuropilin-1 and sema3A (Castellani et al, 2000) and the neurite growth inhibition due to interactions with the proteoglycans neurocan and phosphocan (Friedlander et al, 1994;Grumet et al, 1996). If L1 is playing a role in growth inhibition after rhizotomy, we would expect to see an increase in the CGRP-positive sprouting into the center of the denervated dorsal horn in the L1 mutant compared to wild-type mice.…”

Section: L1 Is Not Required For Cgrp-positive Afferent Sproutingmentioning

confidence: 51%

L1 cell adhesion molecule is not required for small-diameter primary afferent sprouting after deafferentation

Runyan

Roy²,

Zhong³

et al. 2007

Neuroscience

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L1 is a cell adhesion molecule associated with axonal outgrowth and fasciculation during spinal cord development and may reiterate its developmental role in adults following injury; L1 is upregulated on certain sprouting and regenerating axons in adults, but it is unclear if L1 expression is necessary for, or contributes to, regrowth of axons. This study asks if L1 is required for small-diameter primary afferents to sprout by conducting unilateral dorsal rhizotomies (6 segments; T10-L2) on both wildtype and L1 mutant mice. First we determined that L1 co-localizes substantially with the peptidergic (calcitonin gene-related peptide; CGRP) but minimally with the nonpeptidergic (isolectin B4; IB4) primary afferents in intact wild-type and L1 mutant mice. However, we encountered a complication using IB4 to identify primary afferents post-rhizotomy; we detected extensive abnormal IB4 expression in the dorsal horn and dorsal columns. Much of this aberrant IB4 labeling is associated with fibrous astrocytes and microglia. Five days after dorsal rhizotomy a large decrease in peptidergic and nonpeptidergic afferents is evident on the deafferented side in both wild-type and L1 mutants. Three months after surgery the peptidergic primary afferents sprouted into the center of the denervated dorsal horn in both wild-type and mutant mice, and quantitative analyses confirmed a sprouting density of similar magnitude in both genotypes. In contrast, we did not detect sprouting in the nonpeptidergic primary afferents in either genotype. These results suggest that the absence of L1 neither diminishes nor enhances sprouting of peptidergic small-diameter primary afferent axons following a dorsal rhizotomy. Keywordscell adhesion molecule; denervated; IB4; CGRP; nociceptors; rhizotomy The cell adhesion molecule L1 (L1 CAM) is an axonal glycoprotein and a member of the immunoglobulin superfamily (Kamiguchi et al., 1997). L1 plays a role in axonal outgrowth, fasciculation, and guidance during spinal cord development (Stallcup et al., 1985;Jessell, 1988;Stoeckli and Landmesser, 1995;Orlino et al., 2000;Tran and Phelps, 2000;Akopians et al., 2003) through homophilic and various heterophilic binding partners such as integrins (αVβ3 and α5β1) and the fibroblast growth factor receptor (Kamiguchi and Lemmon, 1997 Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Lemmon, 1997;Castellani et al., 2000). NIH Public AccessMutations in X-linked L1 in humans cause major developmental errors and result in a group of symptoms that include corpus callosum hypoplasia, spastic paraplegia and hydrocephalus (Fran...

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Section: L1 Is Not Required For Cgrp-positive Afferent Sproutingmentioning

confidence: 51%

L1 cell adhesion molecule is not required for small-diameter primary afferent sprouting after deafferentation

Runyan

Roy²,

Zhong³

et al. 2007

Neuroscience

View full text Add to dashboard Cite

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“…17 Mechanisms by which astrocytes could dynamically modulate the entry of leukocytes into normal or injured CNS parenchyma in addition to, and perhaps independently of, their influence on the tight junctional complexes of the BBB include their ability to produce: (i) both pro-and anti-inflammatory cytokines; 1,18 and (ii) extracellularly deposited molecules that positively and negatively influence the migration of many cell types and nerve fibers. [19][20][21] These findings suggest that dysfunction of astrocyte regulation of leukocyte trafficking in CNS parenchyma represents a novel potential pathogenic mechanism for inflammatory disturbances in the CNS.…”

Section: Astrocytes and Leukocyte Traffickingmentioning

confidence: 91%

Astrocyte failure as a cause of CNS dysfunction

Sofroniew¹

2000

Mol Psychiatry

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“…In parallel, the chondroitin sulfate proteoglycans neurocan and phosphacan block the homophilic interaction of NgCAM and NCAM, resulting in a competitive inhibition of NgCAM-and NCAM-mediated neuron and glia cell adhesion and neurite outgrowth (61)(62)(63). However, phosphacan probably interferes with NgCAM-mediated neurite outgrowth by binding directly to the cell surface.…”

Section: Discussionmentioning

confidence: 99%

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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Functional characterization of chondroitin sulfate proteoglycans of brain: interactions with neurons and neural cell adhesion molecules.

Cited by 311 publications

References 58 publications

L1 cell adhesion molecule is not required for small-diameter primary afferent sprouting after deafferentation

L1 cell adhesion molecule is not required for small-diameter primary afferent sprouting after deafferentation

Astrocyte failure as a cause of CNS dysfunction

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

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