TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins

Felsenfeld, Dan P.; Hynes, Mary; Skoler, Karen M.; Furley, Andrew J.; Jessell, Thomas M.

doi:10.1016/0896-6273(94)90222-4

Cited by 180 publications

(144 citation statements)

References 66 publications

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“…6). An increase over this number in the adhesion of L1 probe cells to vector target cells or vector probe cells to LI target cells provides an indication of the heterophilic binding of L1 to other molecules expressed by NIH/3T3 ceils, such as 131 integrins (16,81). The adhesion of vector probe cells to L1 target cells was only slightly greater than that of vector probe cells to vector target cells.…”

Section: Ethanol Inhibition Of Homophilic Interactions Mediated By L1mentioning

confidence: 92%

Alcohol inhibits cell-cell adhesion mediated by human L1 [published erratum appears in J Cell Biol 1996 Jun;133(5):1139-40]

Ramanathan

Wilkemeyer

Mittal

et al. 1996

The Journal of Cell Biology

166

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Abstract. Mental retardation, hydrocephalus, and agenesis of the corpus callosum are observed both in fetal alcohol syndrome (FAS) and in children with mutations in the gene for the cell adhesion molecule L1. We studied the effects of ethanol on cell-cell adhesion in mouse fibroblasts transfected with human L1. Ll-transfected fibroblasts exhibited increased cell-cell adhesion compared with wild-type or vector-transfected controls. Ethanol potently and completely inhibited Ll-mediated adhesion both in transfected L cells and NIH/3T3 cells. Half-maximal inhibition was observed at 7 mM ethanol, a concentration achieved in blood and brain after ingesting one alcoholic beverage. In contrast, ethanol did not inhibit the adhesion of fibroblasts transfected with vector alone or with N-CAM-140. Ll-mediated cell-cell adhesion was inhibited with increasing potency by n-propanol and n-butanol, but was not inhibited at all by n-alcohols of 5 to 8 carbons, acetaldehyde, or acetate, suggesting that ethanol interacts directly with a small hydrophobic pocket within L1. Phenylalanine, teratogenic anticonvulsants, and high concentrations of glucose did not inhibit Ll-mediated cell-cell adhesion. Ethanol also inhibited potently the heterotypic adhesion of rat cerebellar granule cells to a monolayer of Ll-transfected NIH/3T3 cells, but had no effect on their adhesion to N-CAM-140 or vector-transfected NIH/3T3 cells. Because L1 plays a role in both neural development and learning, ethanol inhibition of Ll-mediated cell-cell interactions could contribute to FAS and ethanol-associated memory disorders. FETAL alcohol syndrome (FAS) 1 is one of the most common recognizable syndromes associated with mental retardation in the Western world (1). The full syndrome, characterized by growth retardation, neurological abnormalities, and facial malformations, occurs in N5% of the offspring of alcoholic women (1, 72). Neuropathological examination and neuroimaging of children with FAS have disclosed a spectrum of neurodevelopmental abnormalities, including hydrocephalus, agenesis of the corpus callosum, neuronal-glial heterotopias, cerebellar dysplasia, and microcephaly (8,27,62). Some of these lesions arise from disordered migration of neural cells, which has also been demonstrated experimentally in animal models of FAS (45,46 X-linked syndrome associated with mutations in the gene encoding L1, an immunoglobulin cell adhesion molecule (IgCAM) (4,20,28,31,66,74,83). Three overlapping syndromes, X-linked hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait, and adducted thumbs), and X-linked complicated spastic paraplegia, were each mapped to the same region (Xq28) of the X chromosome (32,76,82). A large number of different missense mutations, short deletions, and defects of alternative splicing within the L1 gene have been identified in individuals with these X-linked disorders (83); similar mutations have never been encountered in large numbers of control subjects. A single point mutation in L1 can cause either X-linked hydro...

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Section: Ethanol Inhibition Of Homophilic Interactions Mediated By L1mentioning

confidence: 92%

Alcohol inhibits cell-cell adhesion mediated by human L1 [published erratum appears in J Cell Biol 1996 Jun;133(5):1139-40]

Ramanathan

Wilkemeyer

Mittal

et al. 1996

The Journal of Cell Biology

166

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“…SC-1/DM-GRASP and TAG-1/axonin-1 were reported to interact homophilically (Burns et al, 1991;Rader et al, 1993) as well as heterophilically with L1/NgCAM (De Bernado and Chang, 1996;Felsenfeld et al, 1994;Kuhn et al, 1991). Such and further interactions mediated by rat L1, SC-1, and TAG-1 could conceivably enhance rat RGC axon regeneration.…”

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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“…Alternatively, homo- We investigated the possibility of heterophilic cis interactions between Li and~3 i integrin in small cerebellar neurons, which have been suggested to occur in neurobiastoma N2A cells in conjunction with the calcium-dependent signal transducer molecule CD9 (Schmidt et al, 1996). Furthermore, cis interactions between an Li-like molecule in the chicken and~3i integrin, both of which show trans interactions with the immunoglobulin superfamily molecule TAG-i (Felsenfeld et al, 1994) and trans interactions between Li and av/33-or VLA-5 integrins, have been shown (Kadmon et a!., 1995;Ruppert et al, 1995;Montgomery et al, 1996). The possibility of a cis interaction between Li and /3 1 integrin was investigated by antibody-induced patching and copatching at the membrane surface of live cells.…”

Section: Discussionmentioning

confidence: 99%

L1/HNK‐1 Carbohydrate‐ and β1 Integrin‐Dependent Neural Cell Adhesion to Laminin‐1

Hall

Carbonetto

Schachner

1997

Journal of Neurochemistry

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Abstract:We have shown recently that mouse small cerebellar neurons adhere to a short amino acid sequence of the G2 domain of the laminin al chain via the cell surface-expressed HNK-i carbohydrate. Therefore, we were interested in identifying glycoproteins carrying the HNK-1 carbohydrate at the cell surface of these neurons. Adhesion of small cerebellar neurons to laminin is partially dependent on Ca 2~,Mn2-, and Mg2~,indicating the involvement of integrins, which were identified as~3i,a3, and a6. They could be shown to bind to laminin by a /31 -dependent adhesion mechanism. None of these subunits was found to carry the HNK-1 carbohydrate. HNK-1-immunoreactive glycoproteins were immunoprecipitated and shown to consist of predominantly one molecular species, which was identified as the neural cell recognition molecule Li. Li was demonstrated to bind in a concentration-dependent and saturating manner to laminin. The binding could be partially inhibited by Fab fragments of monoclonal antibodies against the HNK-1 carbohydrate and against the Ig-like domains of Li. Furthermore, antibodies to the Ig-like domains of Li and~31integrin inhibited partially cell adhesion to laminin. Determination of the association of Li,~31integrin, and the HNK-i carbohydrate on the cell surface of live cerebellar neurons by antibody-induced patching and copatching revealed HNK-i to be linked to Li, but less so to /31 integrin. However, only negligible association was found between Li and /31 integrin. Furthermore, it could be shown that adhesion to laminin is mediated by Li/HNK-i-and /3i integrin-dependent mechanisms that act at least partially independent of each other. Key Words: HNK-i carbohydrate-Laminin-lntegrins-L1 -Cell adhesion.

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TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and β1 integrins

Cited by 180 publications

References 66 publications

Alcohol inhibits cell-cell adhesion mediated by human L1 [published erratum appears in J Cell Biol 1996 Jun;133(5):1139-40]

Alcohol inhibits cell-cell adhesion mediated by human L1 [published erratum appears in J Cell Biol 1996 Jun;133(5):1139-40]

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

L1/HNK‐1 Carbohydrate‐ and β1 Integrin‐Dependent Neural Cell Adhesion to Laminin‐1

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