The Ca2+-dependent intercellular adhesion molecule cadherin is known t
o be linked to the cytoskeleton by the protein catenin, an association
of which appears to be important for the cell-adhesion function of ca
dherin. Catenin consists of three subtypes-alpha, beta, and gamma. In
our previous study, N-cadherin was shown to be localized on the plasma
lemma of normal and regenerating chick peripheral nerve. Thus, as alph
a N-catenin is a subtype of alpha-catenin (which is specifically assoc
iated with N-cadherin), we investigated the immunolocalization of alph
a N-catenin in normal and regenerating chick sciatic nerve. In normal
nerve, unmyelinated axons exhibited either intense or weak alpha N-cat
enin immunoreactivity throughout the axoplasm, whereas myelinated axon
s were completely immunonegative. Regenerating axons, including those
derived from parent myelinated axons, showed alpha N-catenin immunorea
ctivity of variable intensities in growth cones and axon shafts. Schwa
nn cells were invariably devoid of immunoreactivity. Thus alpha N-cate
nin is not necessarily bound to the surface plasmalemma, but is distri
buted throughout the cytoplasm, suggesting that most alpha N-catenin m
olecules are dissociated from N-cadherin.