Monoclonal antibody that recognizes the carbohydrate portion of cell adhesion molecule L1 influences calcium current in cultured neurons
✍ Scribed by Hiroaki Asou
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 796 KB
- Volume
- 153
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
A monoclonal antibody (mAb), 2E12, against the neural cell adhesion molecule L1 recognized the 200 kDa component of L1. The epitope of L1 reacting with mAb 2E12 was localized in its carbohydrate chain, judging from the results o C experiments on glycopeptidase F treatment. The physiological effect of adding mAbLl (ZE1Z) to cultured mouse dorsal root ganglion neurons was studied using patchclamp techniques. The binding of mAbLl (2E12) to the neurons expressing L1 molecule induced an inward current inhibited by calcium channel blockers such as nifedipine and Lanthanum. It was also found that the mAbLl (2E12) leads to a rise in the intracellular Ca'+ concentration ([Ca'+],) in cultured neurons. This rise seems to be due to an influx of extracellular CaLt, since treatment with ECTA abolished those phenomena. L-type calcium channel blockers such as nifedipine and cadmium, as well as inward current, blocked the effect of mAbLl(2E12). These results suggest that the carbohydrate chain of L I glycoprotein is directly involved in the induction of calcium current, and that the L. 1 molecule may play a prominent role in regulation of the Ca2+ channel.