Molecular association of two neural cell adhesion molecules within the surface membrane of cultured mouse neuroblastoma cells

Thor, G. Theander; Pollerberg, E G; Schachner, Melitta

doi:10.1016/0304-3940(86)90176-x

Cited by 31 publications

(27 citation statements)

References 13 publications

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“…The two larger-molecular-weight components of N-CAM in the brain (N-CAM 140 and N-CAM 180) are phosphorylated in situ on threonine and serine (Gennarini et al, 1984;Sorkin et al, 1984). Several observations indicate that the association of N-CAM 180 with brain spectrin (fodrin) stabilizes cell contacts (Pollerberg et al, 1985(Pollerberg et al, , 1986(Pollerberg et al, , 1987. Furthermore, N-CAM 180 and L1 are associated with each other in the plane of the surface membrane (Thor et al, 1986), and functional assays have suggested that this association could modulate cell adhesion (Faissner et al, 1984a).…”

Section: Discussionmentioning

confidence: 99%

“…Several observations indicate that the association of N-CAM 180 with brain spectrin (fodrin) stabilizes cell contacts (Pollerberg et al, 1985(Pollerberg et al, , 1986(Pollerberg et al, , 1987. Furthermore, N-CAM 180 and L1 are associated with each other in the plane of the surface membrane (Thor et al, 1986), and functional assays have suggested that this association could modulate cell adhesion (Faissner et al, 1984a). Therefore, it is possible that the phosphorylation of N-CAM 180 regulates its interaction with the cytoskeleton or with L 1, leading to a modification in adhesive properties.…”

Section: Discussionmentioning

confidence: 99%

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A Protein Kinase Activity Is Associated with and Specifically Phosphorylates the Neural Cell Adhesion Molecule LI

Sadoul

Kirchhoff

Schachner

1989

Journal of Neurochemistry

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The neural cell adhesion molecule L1 is a phosphorylated integral membrane glycoprotein that is recovered from adult mouse brain by immunoaffinity chromatography as a set of polypeptides with apparent molecular masses of 200, 180, 140, 80, and 50 kilodaltons (L1-200, L1-180, L1-140, L1-80, and L1-50, respectively). In the present study, we show that two kinase activities are associated with immunopurified L1: One specifically phosphorylates L1-200 and L1-80 but not L1-180, L1-140, or L1-50. This pattern of phosphorylation corresponds to the one described for L1 after metabolic phosphate incorporation into cultures of cerebellar cells. In both cases, serine is the main amino acid that is labeled by radioactive phosphate. The kinase activity is not activated by Ca2+, calmodulin, phosphatidylserine, diolein, cyclic AMP, or cyclic GMP, a result suggesting that the enzyme is distinct from Ca2+/calmodulin-dependent kinases, from protein kinase C, or from cyclic AMP/cyclic GMP-dependent kinases and may belong to the independent kinase group. The other kinase phosphorylates only casein but not L1, utilizes GTP as well as ATP, and is strongly inhibited by heparin. Because the primary structure of the L1 protein does not contain consensus sequences characteristic for known kinases, we believe that the catalytic activities detectable in immunopurified L1 are due to kinases that are strongly enough associated with L1 to withstand the stringent purification procedures.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

A Protein Kinase Activity Is Associated with and Specifically Phosphorylates the Neural Cell Adhesion Molecule LI

Sadoul

Kirchhoff

Schachner

1989

Journal of Neurochemistry

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“…The high molecular weight species (180 kD) was predominant in the cell homogenate (Fig. 2c) (Thor et al, 1986;Bhat and Silberberg, 1988). This is the form, however, that has been suggested to be associated with the neuronal cytoskeleton and to play a major role in the stabilisation of N-CAM-mediated adhesion (Pollerberg et al, 1987).…”

Section: Cam Expression In Metastatic Cell Linesmentioning

confidence: 94%

Beta amyloid precursor protein mediates neuronal cell‐cell and cell‐surface adhesion

Breen

Bruce

Anderton

1991

J of Neuroscience Research

232

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The beta-amyloid precursor protein (APP) is a membrane-bound glycoprotein which has been proposed to play a role both as a growth factor and a mediator of cell adhesion. Using the Neuro-2A neuroblastoma cell line, we have investigated the capacity of APP to mediate neural cell adhesion. The cells express the protein at a high level, the immunohistochemical staining pattern at the level of the membrane having a punctate pattern. Fab' fragments of antibodies to the extracellular portion of the molecule were found to inhibit cell binding to a collagen substrate, but not to laminin, fibronectin, or poly-l-lysine. Fab' fragments of antibodies to the nerve cell adhesion molecule N-CAM also inhibited binding of Neuro-2A cells specifically to collagen. This inhibition of cell-surface binding was accompanied by a repression of neurite outgrowth in differentiating cells in the presence of antibodies. APP antibodies also inhibited neuron-neuron and neuron-glial binding, but not glial-glial cell adhesion. These data suggest that the APP, which is expressed primarily on differentiated neuronal cells, may play a role in the mediation of both cell-cell and cell-substrate adhesion.

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“…Recognition molecules exposed at the cell surface may engage in lock-and-key interactions with their respective ligands individually, but can interact also with several other cell surface components in a cooperative manner. It has been found that the neural adhesion molecules L l and NCAM associate with each other in the plane of the surface membrane (Thor et al, 1986;Simon et al, 1991;Horstkorte et al, 1993) to enhance the avidity of their interaction with L1 on the opposing cell surface (Kadmon et al, 1990a,b). Whether this molecular association also leads to different modes of signal transduction than those given by the individual molecules (Schuch et al, 1989;von Bohlen et al, 1992;Williams et al, 1992) is presently unknown.…”

Section: Introductionmentioning

confidence: 99%

CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1

Schmidt

Künemund

Wintergerst

et al. 1996

J of Neuroscience Research

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We describe here a novel monoclonal antibody (mab H6) which recognizes CD9, an integral cell surface constituent previously described in cells of the hematopoietic lineage and involved in the aggregation of platelets. Mab H6 was raised against membranes of immature mouse astrocytes and reacted with a protein of 25-27 kD in detergent extracts of adult mouse brain membranes. Sequence analysis of the N-terminal amino acids revealed an identity of 96% with CD9 from mouse kidney. CD9 was localized in the central and peripheral mouse nervous systems: in the spinal cord of 11-day-old mouse embryos, CD9 was strongly expressed in the floor and roof plates. In the adult mouse sciatic nerve, myelin sheaths were highly CD9-immunoreactive. Mab H6 reacted with the cell surfaces of both glial cells and neurons in culture and inhibited migration of neuronal cell bodies, neurite fasciculation and outgrowth of astrocytic processes from cerebellar microexplants. Neurite outgrowth from isolated small cerebellar neurons was increased in the presence of mab H6 on substrate-coated laminin, but not on substrate-coated poly-L-lysine. Addition of mab H6 elicited an increase in intracellular Ca2+ concentration in these cells on substrate-coated laminin. Immunoprecipitates of CD9 from cultured mouse neuroblastoma N2A cells contained the alpha 6/beta 1 integrin. Moreover, preparations of CD9 immunoaffinity-purified from adult mouse brain using a mab H6 column contained the neural adhesion molecule L1, but not other neural adhesion molecules. CD9 bound to L1, but not to NCAM or MAG. Both the alpha 6/beta 1 integrin and L1 could be induced to coredistribute with CD9 on the surface of cultured neuroblastoma N2A cells. The combined observations suggest that CD9 can associate with L1 and alpha 6/beta 1 integrin to influence neural cell interactions in vitro.

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Molecular association of two neural cell adhesion molecules within the surface membrane of cultured mouse neuroblastoma cells

Cited by 31 publications

References 13 publications

A Protein Kinase Activity Is Associated with and Specifically Phosphorylates the Neural Cell Adhesion Molecule LI

A Protein Kinase Activity Is Associated with and Specifically Phosphorylates the Neural Cell Adhesion Molecule LI

Beta amyloid precursor protein mediates neuronal cell‐cell and cell‐surface adhesion

CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1

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