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
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.