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EN
Amyloid Precursor Protein (APP) Intracellular Domain (AICD) is the product of APP processing realized by alpha- or beta-secretases and gamma-secretase. It was shown that AICD is able to interact with several proteins which regulate its stability and cellular localization. The Fe65 adaptor protein translocates AICD into nucleus where the APP-Fe65-Tip60 ternary complex may activate transcription of target genes. In the light of recent studies AICD seems to be another product of APP proteolysis endowed with important biological functions that may contribute to Alzheimer's disease pathology.
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Dysregulation of calcium in Alzheimer's disease

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EN
Multiple efforts has underlined importance of calcium dependent cellular processes in the biochemical characterisation of Alzheimer?s disease (AD), suggesting that abnormalities in calcium (Ca2+) homeostasis might be involved in the pathophysiology of the disease. Studies of the pathogenic mutations in presenilins 1 and 2 (PS1 and PS2) and amyloid precursor protein (APP) responsible for early onset familial AD have estabilished central roles for perturbed cellular Ca2+ homeostasis. Studies of apolipoprotein E (ApoE) neurotoxic effects in AD confirmed involvement of Ca2+-mediated mechanisms. Futher consequences of Ca2+ alterations in AD underline the importance of the ER and mitochondria as the regulatory sites involved in the pathogenesis of neuronal degeneration. Alterations of Ca2+ homeostasis include cells from peripheral tissues, including lymphocytes and fibroblasts from AD donors.
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