The laminin-alpha 2 chain is a component of brain capillary basement m
embranes and appears also to be present in neurons of rat, rabbit, pig
and non-human primate brain as evidenced by immunohistochemistry. In
the present study, we have further characterized this very distinct ne
uronal laminin-alpha 2 chain-like immunoreactivity in the hippocampus
of various species. Immunoelectron microscopy with poly- and monoclona
l antibodies to the laminin-alpha 2 chain G-domain localized laminin-a
lpha 2 chain immunoreactivity in adult rat and rabbit hippocampus to d
endritic processes, primarily to dendritic spines. In the developing r
at hippocampus, spine-associated laminin-alpha 2 chain-like immunoreac
tivity first appeared at a time corresponding to that of active synapt
ogenesis. After an entorhinal cortex lesion in adult rats, the time co
urse of denervation-induced loss and reactive reappearance of spines i
n the molecular layer of the dentate gyrus was correlated closely to t
he loss and reappearance of laminin-alpha 2 chain immunoreactivity. Im
munoblot analysis of normal adult rat, rabbit and pig brain revealed a
protein similar in size to the reported 80-kDa laminin-alpha 2 chain
fragment of human placenta as well as 140/160-kDa proteins. These resu
lts suggest the presence of proteins with antigenic homology to the la
minin-alpha 2 chain and/or laminin-alpha 2 isoforms in dendrites and d
endritic spines in selected areas of the brain, predominately in the h
ippocampus and other limbic structures. Given the adhesion and neurite
promoting functions of laminins, it is possible that neuronal laminin
-alpha 2 chain-like proteins play a role in synaptic function and plas
ticity in the CNS. (C) 1997 Elsevier Science B.V.