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Article
Differential glycosylation of Tractin and LeechCAM, two novel Ig superfamily members, regulates neurite extension and fascicle formation
Journal of Cell Biology
  • Yueqiao Huang, Philadelphia College of Osteopathic Medicine
  • John Jellies
  • Kristen M. Johansen
  • Jørgen Johansen
Document Type
Article
Publication Date
1-1-1997
Abstract
By immunoaffinity purification with the mAb Lan3-2, we have identified two novel Ig super-family members. Tractin and LeechCAM. LeechCAM is an NCAM/FasII/ApCAM homologue, whereas Tractin is a cleaved protein with several unique features that include a PG/YG repeat domain that may be part of or interact with the extracellular matrix. Tractin and LeechCAM are widely expressed neural proteins that are differentially glycosylated in sets and subsets of peripheral sensory neurons that form specific fascicles in the central nervous system. In vivo antibody perturbation of the Lan3-2 glycoepitope demonstrates that it can selectively regulate extension of neurites and filopodia. Thus, these experiments provide evidence that differential glycosylation can confer functional diversity and specificity to widely expressed neural proteins.
Comments

This article was published in Journal of Cell Biology, Volume 138, Issue 1, Pages 143-157.

The published version is available at http://dx.doi.org/10.1083/jcb.138.1.143.

Copyright © 1997 Rockefeller U. Press.

Citation Information
Yueqiao Huang, John Jellies, Kristen M. Johansen and Jørgen Johansen. "Differential glycosylation of Tractin and LeechCAM, two novel Ig superfamily members, regulates neurite extension and fascicle formation" Journal of Cell Biology Vol. 138 Iss. 1 (1997) p. 143 - 157
Available at: http://works.bepress.com/yue-qiaogeorge_huang/9/