Calcium-binding protein immunoreactivity delineates the intralaminar nuclei of the thalamus in the human brain.

Immunohistochemical studies have shown that the three calcium-binding proteins (calbindin-D28k, calretinin and parvalbumin) are heterogeneously distributed in the mammalian brain and are useful for delineating nuclear boundaries. We have investigated the distribution of the three calcium-binding proteins in the human thalamus in order to assist in the delineation of the equivocal nuclear boundaries of the intralaminar nuclei of the thalamus. The results show that each of the "functional" nuclear complexes in the human thalamus demonstrates a characteristic pattern of calcium-binding protein immunoreactivity. In particular, the intralaminar nuclei are characterized by a unique combination of calcium-binding protein staining which clearly delineates the component nuclei in this complex from the other nuclei of the human thalamus. The anterior group of intralaminar nuclei (central lateral nucleus, paracentral nucleus and central medial nucleus) showed intense staining for both calbindin-D28k and calretinin. By contrast, the posterior group of intralaminar nuclei (centre median nucleus and parafascicular nucleus) showed a complementary pattern of staining; the centre median nucleus showed immunoreactivity only for one calcium-binding protein, parvalbumin, while the parafascicular nucleus showed immunoreactivity for both calbindin-D28k and calretinin. No other nucleus in the human thalamus showed these particular combinations of calcium-binding protein staining. Since the intralaminar nuclei also have unique topographically organized connectional affiliations with both the cerebral cortex and the basal ganglia, these results suggest that the calcium-binding proteins may play an important role in the influence of the intralaminar nuclei on interactions between the cerebral cortex and the basal ganglia.