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Monoclonal antibody that recognizes the carbohydrate portion of cell adhesion molecule L1 influences calcium current in cultured neurons
Author(s) -
Asou Hiroaki
Publication year - 1992
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041530211
Subject(s) - chemistry , dorsal root ganglion , monoclonal antibody , calcium channel , calcium , egta , extracellular , intracellular , cell adhesion molecule , biochemistry , epitope , biophysics , microbiology and biotechnology , nifedipine , calcium in biology , biology , antibody , immunology , anatomy , dorsum , organic chemistry
Abstract 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 of experiments on glycopeptidase F treatment. The physiological effect of adding mAbL1 (2E12) to cultured mouse dorsal root ganglion neurons was studied using patch‐clamp techniques. The binding of mAbL1 (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 mAbL1 (2E12) leads to a rise in the intracellular Ca 2+ concentration ([Ca 2+ ] i ) in cultured neurons. This rise seems to be due to an influx of extracellular Ca 2+ , since treatment with EGTA abolished those phenomena. L‐type calcium channel blockers such as nifedipine and cadmium, as well as inward current, blocked the effect of mAbL1 (2E12). These results suggest that the carbohydrate chain of L1 glycoprotein is directly involved in the induction of calcium current, and that the L1 molecule may play a prominent role in regulation of the Ca 2+ channel. © 1992 Wiley‐Liss, Inc.