DIFFERENTIAL GLYCOSYLATION OF TRACTIN AND LEECHCAM, 2 NOVEL IG SUPERFAMILY MEMBERS, REGULATES NEURITE EXTENSION AND FASCICLE FORMATION

Citation
Yq. Huang et al., DIFFERENTIAL GLYCOSYLATION OF TRACTIN AND LEECHCAM, 2 NOVEL IG SUPERFAMILY MEMBERS, REGULATES NEURITE EXTENSION AND FASCICLE FORMATION, The Journal of cell biology, 138(1), 1997, pp. 143-157
Citations number
82
Categorie Soggetti
Cell Biology
Journal title
ISSN journal
00219525
Volume
138
Issue
1
Year of publication
1997
Pages
143 - 157
Database
ISI
SICI code
0021-9525(1997)138:1<143:DGOTAL>2.0.ZU;2-Q
Abstract
By immunoaffinity purification with the mAb Lan3-2, we have identified two novel Ig superfamily members, Tractin and LeechCAM. LeechCAM is a n NCAM/FasII/ApCAM homologue, whereas Tractin is a cleaved protein wit h several unique features that include a PG/YG repeat domain that may be part of or interact with the extracellular matrix. Tractin and Leec hCAM are widely expressed neural proteins that are differentially glyc osylated in sets and subsets of peripheral sensory neurons that form s pecific fascicles in the central nervous system. In vivo antibody pert urbation of the Lan3-2 glycoepitope demonstrates that it can selective ly regulate extension of neurites and filopodia. Thus, these experimen ts provide evidence that differential glycosylation can confer functio nal diversity and specificity to widely expressed neural proteins.