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

Hall, Heike; Carbonetto, Salvatore; Schachner, Melitta

doi:10.1046/j.1471-4159.1997.68020544.x

Cited by 72 publications

(40 citation statements)

References 43 publications

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“…Our studies with cyclic RGD peptide pretreatment showed reduction in SCN attachment and neurite outgrowth when plated onto L1-Fc/ PA/PDL and L1-Fc/PA treated thin films, suggesting that this domain was also exposed and available for a v b 3 integrin binding. Thus, we propose that the PA-based treatment of the polymers not only facilitated oriented display of L1-Fc, but also engendered a display of L1-Fc molecules in close proximity to one another, which may mirror the close apposition of highly organized and clustered L1 molecules on the cell surface [43,64]. Using AFM imaging of substrate counterstained with L1 antibodies, we established that L1-Fc/PA substrates showed adsorbed L1-Fc.…”

Section: Discussionmentioning

confidence: 83%

Oriented, Multimeric Biointerfaces of the L1 Cell Adhesion Molecule: An Approach to Enhance Neuronal and Neural Stem Cell Functions on 2-D and 3-D Polymer Substrates

et al. 2012

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This article focuses on elucidating the key presentation features of neurotrophic ligands at polymer interfaces. Different biointerfacial configurations of the human neural cell adhesion molecule L1 were established on two-dimensional films and three-dimensional fibrous scaffolds of synthetic tyrosine-derived polycarbonate polymers and probed for surface concentrations, microscale organization, and effects on cultured primary neurons and neural stem cells. Underlying polymer substrates were modified with varying combinations of protein A and poly-d-lysine to modulate the immobilization and presentation of the Fc fusion fragment of the extracellular domain of L1 (L1-Fc). When presented as an oriented and multimeric configuration from protein A-pretreated polymers, L1-Fc significantly increased neurite outgrowth of rodent spinal cord neurons and cerebellar neurons as early as 24 h compared to the traditional presentation via adsorption onto surfaces treated with poly-d-lysine. Cultures of human neural progenitor cells screened on the L1-Fc/polymer biointerfaces showed significantly enhanced neuronal differentiation and neuritogenesis on all protein A oriented substrates. Notably, the highest degree of βIII-tubulin expression for cells in 3-D fibrous scaffolds were observed in protein A oriented substrates with PDL pretreatment, suggesting combined effects of cell attachment to polycationic charged substrates with subcellular topography along with L1-mediated adhesion mediating neuronal differentiation. Together, these findings highlight the promise of displays of multimeric neural adhesion ligands via biointerfacially engineered substrates to “cooperatively” enhance neuronal phenotypes on polymers of relevance to tissue engineering.

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Section: Discussionmentioning

confidence: 83%

Oriented, Multimeric Biointerfaces of the L1 Cell Adhesion Molecule: An Approach to Enhance Neuronal and Neural Stem Cell Functions on 2-D and 3-D Polymer Substrates

et al. 2012

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“…PC12 cells express mainly ␣1 ␤1, and ␣3 ␤1 integrins, which are receptors for both laminin and collagen (Tomaselli et al, 1990). In contrast, cerebellar neurons express ␣1 ␤1 as a collagen/laminin receptor and ␣6 ␤1 as receptor for laminin (Hall et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Biochemical Engineering of Cell Surface Sialic Acids Stimulates Axonal Growth

et al. 2002

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Sialylation is essential for development and regeneration in mammals. Using N-propanoylmannosamine, a novel precursor of sialic acid, we were able to incorporate unnatural sialic acids with a prolonged N-acyl side chain (e.g., N-propanoylneuraminic acid) into cell surface glycoconjugates. Here we report that this biochemical engineering of sialic acid leads to a stimulation of neuronal cells. Both PC12 cells and cerebellar neurons showed a significant increase in neurite outgrowth after treatment with this novel sialic acid precursor. Furthermore, also the reestablishment of the perforant pathway was stimulated in brain slices. In addition, we surprisingly identified several cytosolic proteins with regulatory functions, which are differentially expressed after treatment with N-propanoylmannosamine. Because sialic acid is the only monosaccharide that is activated in the nucleus, we hypothesize that transcription could be modulated by the unnatural CMP-Npropanoylneuraminic acid and that sialic acid activation might be a general tool to regulate cellular functions, such as neurite outgrowth.

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“…The antigen has been found to be one of the factors responsible for the precise cell adhesion and recognition processes that underlie the interaction of neural cells (42). It has also been implicated in interactions with laminin and peripheral nerve regeneration (43,(72)(73)(74)(75)(76)(77). This carbohydrate antigen, also found in the retina and on HNK cells, is the main target of IgM molecules from patients with peripheral demyelination neuropathies (44,78).…”

Section: Characterization Of N-glycans Of Bovine Peripheral Myelin P0mentioning

confidence: 99%

Epitope Diversity of N-Glycans from Bovine Peripheral Myelin Glycoprotein P0 Revealed by Mass Spectrometry and Nano Probe Magic Angle Spinning 1H NMR Spectroscopy

Gallego¹,

Blanco²,

Zuylen³

et al. 2001

Journal of Biological Chemistry

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The carbohydrate structures present on the glycoproteins in the central and peripheral nerve systems are essential in many cell adhesion processes. The P0 glycoprotein, expressed by myelinating Schwann cells, plays an important role during the formation and maintenance of myelin, and it is the most abundant constituent of myelin. Using monoclonal antibodies, the homophilic binding of the P0 glycoprotein was shown to be mediated via the human natural keller cell (HNK)-1 epitope (3-O-SO 3 H-GlcUA(␤1-3)Gal(␤1-4)GlcNAc) present on the N-glycans. We recently described the structure of the N-glycan carrying the HNK-1 epitope, present on bovine peripheral myelin P0 (Voshol, H., van Zuylen, C. W. E. M., Orberger, G., Vliegenthart, J. F. G., and Schachner, M. (1996) J. Biol. Chem. 271, 22957-22960). In this study, we report on the structural characterization of the detectable glycoforms, present on the single N-glycosylation site, using state-of-the-art NMR and mass spectrometry techniques. Even though all structures belong to the hybrid-or biantennary complex-type structures, the variety of epitopes is remarkable. In addition to the 3-Osulfate present on the HNK-1-carrying structures, most of the glycans contain a 6-O-sulfated N-acetylglucosamine residue. This indicates the activity of a 6-Osulfo-GlcNAc-transferase, which has not been described before in peripheral nervous tissue. The presence of the disialo-, galactosyl-, and 6-O-sulfosialyl-Lewis X epitopes provides evidence for glycosyltransferase activities not detected until now. The finding of such an epitope diversity triggers questions related to their function and whether events, previously attributed merely to the HNK-1 epitope, could be mediated by the structures described here.The P0 glycoprotein consists of a single immunoglobulin-like domain in its extracellular part, a transmembranous domain, and a cytoplasmic tail. It is the most abundant protein constituent of peripheral myelin. P0 contains a single N-glycosylation site and heterogeneity in its glycosylation pattern that originates from variable contents of fucose, galactose, and sialic acid residues; sulfate; and the HNK-1 carbohydrate epitope (1-4). P0 appears at the initial stage of myelination and contributes to the formation and maintenance of myelin compaction as an adhesion molecule (5). The essential functional role of P0 in the processes of myelination has been demonstrated by creating P0 knockout mice, which show severe hypomyelination and myelin degeneration (5, 6). In humans, several neurological disorders such as Charcot-Marie-Tooth disease, Dejerine-Sottas disease, and congenital hypomyelination have been associated with mutations in the P0 gene (7).It has been reported that the glycan moiety of P0 plays an important role in cell-cell adhesion via homophilic binding. This homophilic binding has been mapped to the SDNGT sequence composing amino acids 91-95, which harbors the single N-glycosylation site on P0 (8). Thus, it was observed that this glycopeptide fragment inhibits cell adhesion t...

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

Cited by 72 publications

References 43 publications

Oriented, Multimeric Biointerfaces of the L1 Cell Adhesion Molecule: An Approach to Enhance Neuronal and Neural Stem Cell Functions on 2-D and 3-D Polymer Substrates

Oriented, Multimeric Biointerfaces of the L1 Cell Adhesion Molecule: An Approach to Enhance Neuronal and Neural Stem Cell Functions on 2-D and 3-D Polymer Substrates

Biochemical Engineering of Cell Surface Sialic Acids Stimulates Axonal Growth

Epitope Diversity of N-Glycans from Bovine Peripheral Myelin Glycoprotein P0 Revealed by Mass Spectrometry and Nano Probe Magic Angle Spinning 1H NMR Spectroscopy

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