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© The Rockefeller University Press, 0021-9525/1997//143 $5.00
The Journal of Cell Biology, Volume 138, Number 1, , 1997 143-157

Article

Differential Glycosylation of Tractin and LeechCAM, Two Novel Ig Superfamily Members, Regulates Neurite Extension and Fascicle Formation



Yueqiao Huang*, John Jellies{ddagger}, Kristen M. Johansen*, and Jørgen Johansen*

* Department of Zoology and Genetics, Iowa State University, Ames, Iowa 50011; and {ddagger} Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008

By immunoaffinity purification with the mAb Lan3-2, we have identified two novel Ig superfamily 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.

1. Abbreviations used in this paper: CAM, cellular adhesion molecule; CNS, central nervous system; FNIII, fibronectin type III.

Please address all correspondence to Jørgen Johansen, Department of Zoology and Genetics, 3156 Molecular Biology Building, Iowa State University, Ames, IA 50011. Tel.: (515) 294-2358. Fax: (515) 294-0345. e-mail: jorgen{at}iastate.edu


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