Pick's Disease
Introduction
Pick's disease (PiD) is a neurodegenerative disorder characterized by frontotemporal dementia (FTD), presenting distinct behavior, language, and motor function changes. PiD neuropathological phenotype is seen in patients presenting most often with clinical phenotypes of FTD. Cases of PiD have been described since the late 19th century, initially most comprehensively by Arnold Pick. He lent his name to the historical designation of the entire FTD spectrum as Pick's disease. In the past few decades, these diseases' clinical and pathological complexity and their unique status as examples of selective brain degeneration have been fully appreciated.
PiD is a rare cause of frontal lobe dementia that accounts for approximately 2% of all cases of dementia in the elderly. It is classically associated with circumscribed lobar atrophy. The distribution of focal cortical degeneration determines the clinical presentation. Clinical PiD, more recently referred to as frontotemporal lobar degeneration (FTLD), has a spectrum of underlying pathology, often considered heterogeneous. PiD is manifested by mainly progressive aphasia, disinhibition, apathy, language problems, memory deficits, apraxia, and behavior change associated with frontotemporal atrophy.
Fig.1 Histopathology of PiD. (Dickson, 2011)
PiD is a distinct tauopathy characterized by an accumulation of Pick bodies in the hippocampal region and cortex and the presence of three and four microtubule-binding repeat pathology in both cortical gray and white matter that distinguish this tauopathy from other neurodegenerative disorders. Neuropathologically, circumscribed cortical atrophy is associated with neuronal loss, mainly of the frontal and anterior temporal lobes, white matter degeneration, achromatic neurons (Pick cells), and intraneuronal lesions Pick bodies (PBs) in the hippocampus, cerebral cortex, and selected brainstem nuclei.
Key Factors of PiD
Tau is a significant component of the intracellular filamentous deposits that define several neurodegenerative diseases. Tau is a microtubule-associated protein (MAP) binding to microtubules and promoting their polymerization. It plays an essential role in maintaining axonal transport and neuronal integrity and is expressed at low levels in glial cells. Six tau isoforms are expressed in the average adult human brain, three isoforms with four microtubule-binding repeats each (4R tau) and three isoforms that lack the second repeat (3R tau).
PiD is one of the common FTLD-tau characterized by neuronal Pick bodies in a stereotypic neuroanatomical distribution. The observed tau fold in the filaments of patients with PiD explains the selective incorporation of 3R tau in Pick bodies and the differences in phosphorylation relative to the tau filaments of Alzheimer's disease. Mutations in the tau gene (such as MAPT) account for most pathologically confirmed cases of familial PiD. MAPT mutation carriers may have a prominent semantic impairment. Therefore, PiD has been classified as a significant tauopathy recently.
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Reference
- Dickson, D. W.; et al. Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau). Journal of Molecular Neuroscience. 2011, 45(3), 384-389.
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