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.
Original language | American English |
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Journal | Journal of Cell Biology |
Volume | 138 |
State | Published - Jan 1 1997 |
Keywords
- Afferent
- Affinity
- Amino Acid
- Amino Acid Sequence
- Animalia
- Animals
- Antibodies
- Cell Adhesion Molecules
- Chromatography
- Cloning
- Fluorescent Antibody Technique
- Glycosylation
- Hirudinida
- Indirect
- Leeches
- Molecular
- Molecular Sequence Data
- Monoclonal
- Nerve Fibers
- Neurites
- Neuronal
- Neurons
- Sequence Homology
- animal cell
- article
- cell adhesion molecule
- controlled study
- leech
- nerve cell adhesion molecule
- nerve cell differentiation
- nerve fiber growth
- nonhuman
- priority journal
- protein glycosylation
- sensory nerve cell
- signal transduction
Disciplines
- Neuroscience and Neurobiology