Proline-rich synapse-associated protein-1 (ProSAP1) is a neuronal PDZ domai
n-containing protein that has recently been identified as an essential elem
ent of the postsynaptic density. Via its interaction with the actin-binding
protein cortactin and its integrative function in the organization of neur
otransmitter receptors, ProSAP1 is believed to be involved in the linkage o
f the postsynaptic signaling machinery to the actin-based cytoskeleton, and
may play a role in the cytoskeletal rearrangements that underlie synaptic
plasticity. As a result of our ongoing studies on the distribution and func
tion of this novel PDZ domain protein, we now report that the expression of
ProSAP1 is restricted neither to neurons and interneuronal junctions nor t
o the nervous system. Using immunohistochemical technniques in conjunction
with specific antibodies, we found that, in the CNS, ProSAP1 can be detecte
d in certain glial cells, such as ependymal cells, tanycytes, subpial/radia
l astrocytes, and in the choroid plexus epithelium. Moreover, our immunohis
tochemical analyses revealed the presence of ProSAP1 in endocrine cells of
the adenohypophysis and of the pancreas, as well as in non-neuronal cell ty
pes of other organs. In the pancreas, ProSAP1 immunoreactivity was also loc
alized in the duct system of the exocrine parenchyma. Our findings demonstr
ate that, in addition to neurons, ProSAP1 is present in various non-neurona
l cells, in which it may play a crucial role in the dynamics of the actin-b
ased cytoskeleton.