Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions

The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts... N-CAM 180 , the molecular form of the three neural cell adhesion molecules (N-CAM) with the largest cytoplasmic domain, is accumulated at sites of cell-cell contact (cell bodies, neurites, growth cones) in cultures of neuroblastoma and cerebellum. At these sites the cytoskeletonmembrane linker protein brain spectrin and actin are also accumulated. Brain spectrin copurifies with N-CAM 180 by immunoaffinity chromatography and binds specifically to N-CAM 180 but not to N-CAM 140 or N-CAM 120 in a solid-phase binding test. These observations indicate an association of N-CAM 180 with the cytoskeleton in vivo. This association may underlie the reduced lateral mobility of N-CAM 180 in the surface membrane compared to N-CAM 140 (Pollerberg et al. 1986). Together with the fact that N-CAM 180 is only expressed after termination of neuron migration in vivo (Persohn and Schachner, unpublished) these results suggest a role for N-CAM 180 in stabilization of cell contacts. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cell and Tissue Research Springer Journals

The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions

Download PDF
10 pages

Loading next page...
 
/lp/springer-journals/the-180-kd-component-of-the-neural-cell-adhesion-molecule-n-cam-is-VCe7AjyB3x

References (48)

Publisher
Springer Journals
Copyright
Copyright © 1987 by Springer-Verlag
Subject
Biomedicine; Human Genetics; Proteomics; Molecular Medicine
ISSN
0302-766X
eISSN
1432-0878
DOI
10.1007/BF00214676
Publisher site
See Article on Publisher Site

Abstract

N-CAM 180 , the molecular form of the three neural cell adhesion molecules (N-CAM) with the largest cytoplasmic domain, is accumulated at sites of cell-cell contact (cell bodies, neurites, growth cones) in cultures of neuroblastoma and cerebellum. At these sites the cytoskeletonmembrane linker protein brain spectrin and actin are also accumulated. Brain spectrin copurifies with N-CAM 180 by immunoaffinity chromatography and binds specifically to N-CAM 180 but not to N-CAM 140 or N-CAM 120 in a solid-phase binding test. These observations indicate an association of N-CAM 180 with the cytoskeleton in vivo. This association may underlie the reduced lateral mobility of N-CAM 180 in the surface membrane compared to N-CAM 140 (Pollerberg et al. 1986). Together with the fact that N-CAM 180 is only expressed after termination of neuron migration in vivo (Persohn and Schachner, unpublished) these results suggest a role for N-CAM 180 in stabilization of cell contacts.

Journal

Cell and Tissue Research – Springer Journals

Published: Oct 1, 1987

There are no references for this article.