Evidence for cis interaction and cooperative signalling by the heat-stable antigen nectadrin (murine CD24) and the cell adhesion molecule L1 in neurons.

@article{Kadmon1995EvidenceFC,
  title={Evidence for cis interaction and cooperative signalling by the heat-stable antigen nectadrin (murine CD24) and the cell adhesion molecule L1 in neurons.},
  author={Guni Kadmon and Friedrich Von Bohlen Und Halbach and Ruediger Horstkorte and Martine Eckert and Peter Altevogt and Melitta Schachner},
  journal={The European journal of neuroscience},
  year={1995},
  volume={7 5},
  pages={993-1004}
}
L1 is a transmembranal homophilic cell adhesion molecule of the immunoglobulin superfamily expressed by neural and lymphoid cells. The heat-stable antigen (HSA, murine CD24) nectadrin is a highly and heterogeneously glycosylated glycophosphatidylinositol-linked differentiation antigen of haematopoietic and neural cells. L1 and nectadrin have been shown to mediate cell adhesion and intracellular Ca2+ signals in neurons and B lymphoblasts, respectively. Here we show that nectadrin is co-expressed… CONTINUE READING

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Both the weak Ca2 + signal mediated by L1 alone and the enhanced signal jointly triggered by antibodies to L1 and nectadrin were inhibited by phorbol 12-myristate 13-acetate and were not significantly affected by Ni2 + and Cd2 + cations , suggesting that they are related to one another and involve recruitment of intracellular Ca2 + .
Both the weak Ca2 + signal mediated by L1 alone and the enhanced signal jointly triggered by antibodies to L1 and nectadrin were inhibited by phorbol 12-myristate 13-acetate and were not significantly affected by Ni2 + and Cd2 + cations , suggesting that they are related to one another and involve recruitment of intracellular Ca2 + .
Both the weak Ca2 + signal mediated by L1 alone and the enhanced signal jointly triggered by antibodies to L1 and nectadrin were inhibited by phorbol 12-myristate 13-acetate and were not significantly affected by Ni2 + and Cd2 + cations , suggesting that they are related to one another and involve recruitment of intracellular Ca2 + .
Both the weak Ca2 + signal mediated by L1 alone and the enhanced signal jointly triggered by antibodies to L1 and nectadrin were inhibited by phorbol 12-myristate 13-acetate and were not significantly affected by Ni2 + and Cd2 + cations , suggesting that they are related to one another and involve recruitment of intracellular Ca2 + .
In co - capping experiments nectadrin co - redistributed with L1 and N - CAM .
Evidence for cis interaction and cooperative signalling by the heat - stable antigen nectadrin ( murine CD24 ) and the cell adhesion molecule L1 in neurons .
Evidence for cis interaction and cooperative signalling by the heat - stable antigen nectadrin ( murine CD24 ) and the cell adhesion molecule L1 in neurons .
Binding between nectadrin and purified N - CAM was not observed .
Since in these cells N - CAM and L1 cohere by cis - binding nectadrin appears to join the L1-N - CAM complex through binding to L1 .
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