PEP-19 immunohistochemistry defines the basal ganglia and associated structures in the adult human brain, and is dramatically reduced in Huntington's disease

Add time:08/02/2019    Source:sciencedirect.com

We have investigated the distribution of PEP-19, a neuron-specific protein, in the adult human brain. Immunohistochemistry for PEP-19 appears to define the basal ganglia and related structures. The strongest immunoreactivity is seen in the caudate nucleus and putamen, each of which showed both cell body and neuropil PEP-19 immunoreactivity The substantia nigra and both segments of the globus pallidus showed PEP-19 immunoreactivity only in the neuropil. Cell bodies and dendrites of the thalamic nuclei ventralis lateralis and ventralis anterioralis were less strongly immunoreactive. Cerebellar Purkinje cells and their dendrites were immunoreactive, as were the presubiculum/subiculum regions and dentate gyrus granule cells of the hippocampus. The CA zones of the hippocampus were not immunoreactive. Preliminary data from immunoblotting experiments indicate that PEP-19 immunoreactivity is significantly reduced in cerebellum in Alzheimer's disease. While there were no apparent alterations of immunoreactivity in Down's syndrome or in Parkinson's disease, immunohistochemical analysis showed a massive loss of PEP-19 immunoreactivity in the caudate nucleus, putamen, globus pallidus and substantia nigra in Huntington's disease.These results show that PEP-19, a neuron-specific, calmodulin-binding protein, is distributed in specific areas of the adult human brain. The reduction in PEP-19 immunoreactivity in Alzheimer's disease and Huntington's disease suggests that PEP-19 may play a role in the pathophysiology of these diseases through a mechanism of calcium/calmodulin disregulation. This may be especially apparent in Huntington's disease where the distribution of the product of the abnormal gene, huntingtin, alone is not sufficient to explain the pattern of pathology. Abnormal huntingtin associates more strongly with calmodulin than does normal huntingtin (Bao et al., 1996, Proc. natn. Acad. Sci. U.S.A., 93, 5037–5042) suggesting a disruption of calmodulin-mediated intracellular mechanism(s), very likely involving PEP-19.

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