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Cytoplasmic domain of NCAM 180 reduces NCAM‐mediated neurite outgrowth
Author(s) -
Büttner Bettina,
Reutter Werner,
Horstkorte Rüdiger
Publication year - 2004
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20049
Subject(s) - neurite , neural cell adhesion molecule , transmembrane protein , microbiology and biotechnology , intracellular , gene isoform , immunoglobulin superfamily , extracellular , biology , cell adhesion , cell adhesion molecule , chemistry , neuroscience , cell , in vitro , biochemistry , receptor , gene
The neural cell adhesion molecule (NCAM) is one of the best‐characterized cell adhesion molecules of the immunoglobulin superfamily. In the nervous system, NCAM is involved in cell migration, axon fasciculation and in neurite outgrowth. Neurite outgrowth is mediated by homophilic NCAM‐NCAM interactions. Alternative splicing generates three major isoforms of NCAM differing in their intracellular portion. Two of them, NCAM 180 and NCAM 140, are transmembrane proteins with large intracellular domains. The present study is concerned with novel details of the intracellular domains of NCAM 140 and NCAM 180. We expressed these NCAM isoforms consisting only of the transmembrane and intracellular domains (without extracellular domains) in PC12 cells and elaborated their function in neurite outgrowth assays. Our data demonstrate that membrane‐associated NCAM 180 interferes with neurite outgrowth, whereas membrane‐associated NCAM 140 promotes neurite outgrowth. © 2004 Wiley‐Liss, Inc.