Differential immunoreactivity for alpha-actinin-2, an N-methyl- d-aspartate-receptor/actin binding protein, in hippocampal interneurons

Recent studies have demonstrated that hippocampal interneurons possess distinct cytoskeletal and cell-signaling proteins in comparison to hippocampal principal cells; however, little is known about the differences in the actin cytoskeleton between these two populations. This study examined the immunoreactivity of α-actinin-2, an actin binding/ N-methyl- d-aspartate-receptor linking protein, in the rat hippocampal formation using double-labelling immunofluorescence. Alpha-actinin-2 immunoreactivity is seen throughout the hippocampus with heavy labeling observed in the dendrites of granule cells, in CA2 pyramidal cells and in presumed interneuronal somata throughout the dentate gyrus and CA1. All the cells with heavy somatic α-actinin-2 immunoreactivity in the dentate gyrus and CA1 were GABAergic interneurons labeled by glutamate decarboxylase (99%). Examination of the neurochemical marker content of the α-actinin-2 immunoreactive interneurons revealed that the majority of this population was neuropeptide-Y-positive and a minority was positive for calretinin. Fluid percussion head trauma did not result in significant alterations of α-actinin-2 immunoreactivity in hippocampal interneurons. The developmental profile of α-actinin-2 immunoreactivity showed the presence of α-actinin-2 in the hippocampus at P1, labeling of interneurons by P7 and the adult staining pattern seen by P21. This study demonstrates that principal cells and interneurons are differentially immunoreactive for α-actinin-2, and that α-actinin-2 staining is restricted to a subpopulation of interneurons. Each of the three classes of cytoskeletal elements have been shown to be differentially expressed in hippocampal interneurons and principal cells, suggesting that the cytoskeleton is a defining feature of neuronal populations. Additionally, the limited expression of α-actinin-2 could have important functional implications in N-methyl- d-aspartate receptor localization and modulation.