αN-catenin expression in the normal and regenerating chick sciatic nerve
| Autor: | Chizuka Ide, Keikichi Shimada, Masaki Tomatsuri, Akira Mizoguchi, Yasuyuki Shibuya, Masatoshi Takeichi, Hisashi Yasuda |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Cytoplasm
Histology Nerve Crush Gene Expression Schwann cell Nerve Tissue Proteins Biology Nerve Fibers Myelinated medicine Animals Axon Growth cone Cytoskeleton Cadherin General Neuroscience Cell Biology Anatomy Cadherins Immunohistochemistry Sciatic Nerve Axons Nerve Regeneration Cell biology Cytoskeletal Proteins Microscopy Electron medicine.anatomical_structure nervous system Axoplasm Catenin Female Schwann Cells Sciatic nerve Chickens alpha Catenin |
| Zdroj: | Journal of Neurocytology. 25:615-624 |
| ISSN: | 1573-7381 0300-4864 |
| DOI: | 10.1007/bf02284828 |
| Popis: | The Ca(2+)-dependent intercellular adhesion molecule cadherin is known to be linked to the cytoskeleton by the protein catenin, an association of which appears to be important for the cell-adhesion function of cadherin. Catenin consists of three subtypes-alpha, beta, and gamma. In our previous study, N-cadherin was shown to be localized on the plasmalemma of normal and regenerating chick peripheral nerve. Thus, as alpha N-catenin is a subtype of alpha-catenin (which is specifically associated with N-cadherin), we investigated the immunolocalization of alpha N-catenin in normal and regenerating chick sciatic nerve. In normal nerve, unmyelinated axons exhibited either intense or weak alpha N-catenin immunoreactivity throughout the axoplasm, whereas myelinated axons were completely immunonegative. Regenerating axons, including those derived from parent myelinated axons, showed alpha N-catenin immunoreactivity of variable intensities in growth cones and axon shafts. Schwann cells were invariably devoid of immunoreactivity. Thus alpha N-catenin is not necessarily bound to the surface plasmalemma, but is distributed throughout the cytoplasm, suggesting that most alpha N-catenin molecules are dissociated from N-cadherin. |
| Databáze: | OpenAIRE |
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