ISSN:
1573-7381
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary The Ca2+-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-α, β, and γ. In our previous study, N-cadherin was shown to be localized on the plasmalemma of normal and regenerating chick peripheral nerve. Thus, as αN-catenin is a subtype of α-catenin (which is specifically associated with N-cadherin), we investigated the immunolocalization of αN-catenin in normal and regenerating chick sciatic nerve. In normal nerve, unmyelinated axons exhibited either intense or weak αN-catenin immunoreactivity throughout the axoplasm, whereas myelinated axons were completely immunonegative. Regenerating axons, including those derived from parent myelinated axons, showed αN-catenin immunoreactivity of variable intensities in growth cones and axon shafts. Schwann cells were invariably devoid of immunoreactivity. Thus αN-catenin is not necessarily bound to the surface plasmalemma, but is distributed throughout the cytoplasm, suggesting that most αN-catenin molecules are dissociated from N-cadherin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02284828
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