L1-mediated axon outgrowth occurs via a homophilic binding mechanism

Lemmon, Vance; Farr, Kathryn L.; Lagenaur, Carl F.

doi:10.1016/0896-6273(89)90048-2

Cited by 418 publications

(308 citation statements)

References 23 publications

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“…This was one reason why L1, TAG-1, and SC-1 were selected for tests of CAM synthesis by axon-regenerating rat RGCs. Moreover, related proteins and direct homologs in various species have been demonstrated to be involved in axon elongation, recognition, fasciculation, and contact stabilization (i.e., TAG-1 in mouse: Furley et al, 1990; axonin-1 in chick: Ruegg et al, 1989;Stoeckli et al, 1991; L1 in mouse and rat: Bartsch et al, 1989;Mohajeri et al, 1996;; NgCAM in chick: Lemmon et al, 1989;Chang et al, 1987;Rathjen et al, 1987;Yamagata et al, 1995;E587 antigen in goldfish: Bastmeyer et al, 1995; SC-1/DM-GRASP in chick: Burns et al, 1991;Tanaka et al, 1991;Pollerberg and Mack, 1994;Yamagata et al, 1995;neurolin in goldfish: Bastmeyer et al, 1996). Moreover, CAMs activate signal transduction pathways which effect and modulate axon growth (Doherty and Walsh, 1994;Kunz et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Axon-Regenerating Retinal Ganglion Cells in Adult Rats Synthesize the Cell Adhesion Molecule L1 but Not TAG-1 or SC-1

Jung

Petrausch

Stuermer

1997

Molecular and Cellular Neuroscience

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Retinal ganglion cells (RGCs) in rats regenerate axons in the presence of a PNS nerve graft. To determine if axonregenerating RGCs synthesize cell adhesion/recognition molecules which they possessed during development, retinae were subjected to in situ hybridization with antisense cRNA probes of L1, TAG-1, and SC-1 (and GAP-43 for comparison). L1 and TAG-1 (and GAP-43) proteins on axons were detected with antibodies. L1, TAG-1, and SC-1 (and Gap-43) mRNAs and L1 and TAG-1 (and Gap-43) proteins were expressed by RGCs in embryonic, postnatal, and adult rats. After optic nerve lesion (ONL), the surviving RGCs between 2 and 28 days after ONL continue to express L1. TAG-1 and SC-1 expression, however, is lost. In grafted rats, axon-regenerating RGCs express L1 (together with GAP-43) but neither TAG-1 nor SC-1. Thus, axonal regeneration in grafted rats occurs in the presence of L1 (and GAP-43) but in the absence of TAG-1 and SC-1.

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Section: Discussionmentioning

confidence: 99%

Axon-Regenerating Retinal Ganglion Cells in Adult Rats Synthesize the Cell Adhesion Molecule L1 but Not TAG-1 or SC-1

Jung

Petrausch

Stuermer

1997

Molecular and Cellular Neuroscience

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“…In brief, features in common to both proteins include (a) their gross domain structural organization (Moos et al, 1988;Burgoon et al, 1991); (b) their appearance as a pattern of polypeptides probably originated by partial proteolytic cleavage of a single precursor molecule (Grumet et al, 1984;Wolffet al, 1987;Sadoul et al, 1988); (c) the occurrence of a phosphorylation site on the cytoplasmic domain (Grumet et al, 1984;Faissner et al, 1985;Sadoul et al, 1989); (d) the tissue expression patterns in most areas of the nervous system on which data are available for corresponding developmental stages (Rathjen and Schachner, 1984;Stalleup et al, 1985;Daniloff et al, 1986;but ef. Shiga et al, 1990, for an exception); and (e) involvement in biological functions, such as neuronal migration (Lindner et al, 1983;Hoffman et al, 1986), promotion of neurite outgrowth (Lagenaur and Lemmon, 1987;Lemmon et al, 1989;Chang et al, 1990;Kadmon et al, 1990), and fasciculation (Hoffman et al, 1986;Fischer et al, 1986;Rathjen et al, 1987a). The argumentation that L1 and Ng-CAM may not be species homologues but relatives derived main has a three-dimensional structure similar to that of the immunoglobulin fold of the C2 subcategory.…”

Section: Structural Features Of Ig/fniii-like Proteins Concentrated Omentioning

confidence: 99%

“…Such procedures have become popular in the past years because they represent the most readily applicable assays for the identification of weak macromolecular interactions. To determine whether L1/Ng-CAM of the neuronal membrane is part of the neurite growthpromoting machinery as a receptor binding to LUNg-CAM substratum in a homophilic interaction, Lemmon et al (1989) used a cross-species approach based on the finding that both LUNg-CAM from mouse and from chick each promote neurite extension from neurons of both species. When they cultured chick neurons on mouse LUNg-CAM they found that antibodies specific for chick LUNg-CAM inhibited neurite outgrowth.…”

Section: L1/ng-cam a Neuronal Receptor For Substratum-induced Neuritmentioning

confidence: 99%

Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily.

Sonderegger

Rathjen

1992

The Journal of Cell Biology

152

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“…Spinal cord sections throughout the six segment deafferentation were processed with L1 polyclonal antisera (1:30,000; rabbit anti-rat L1; Lemmon et al, 1989; gift from Dr. Vance Lemmon, University of Miami, Miami, Florida), CGRP (AB1971; 1:30,000; Chemicon; Temecula, CA), IB4 (1:400; Vector; Burlingame, CA), and an additional marker for a subgroup of nonpeptidergic axons, P2X 3 (1:4,000; Chemicon), a receptor subunit in the P2X family of ATP-gated ion channels (Vulchanova et al, 1998). Immunocytochemical protocols for CGRP and IB4 are detailed in Runyan et al (2005) and L1 labeling was performed according to the CGRP protocol.…”

Section: Immunocytochemical Proceduresmentioning

confidence: 99%

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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L1-mediated axon outgrowth occurs via a homophilic binding mechanism

Cited by 418 publications

References 23 publications

Axon-Regenerating Retinal Ganglion Cells in Adult Rats Synthesize the Cell Adhesion Molecule L1 but Not TAG-1 or SC-1

Axon-Regenerating Retinal Ganglion Cells in Adult Rats Synthesize the Cell Adhesion Molecule L1 but Not TAG-1 or SC-1

Regulation of axonal growth in the vertebrate nervous system by interactions between glycoproteins belonging to two subgroups of the immunoglobulin superfamily.

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

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