Amyloid precursor protein (APP) and acetylcholinesterase (AChE) are membrane-bound proteins possessing a variety of roles in brain development and functioning. While APP is mostly known as a protein producing amyloid β peptide (Aβ) both AChE and butyrylcholinesterase (BuChE) are generally linked to cholinergic neurotransmission. All three proteins have soluble forms which, despite their different origin, are believed to play a role in neurogenesis, synaptogenesis and neuroprotection. There is evidence that APP and AChE can form complexes in the membrane and both AChE and BuChE are found in tight association with Aβ in senile plaques characteristic for Alzheimer’s disease. Under certain circumstances AChE is shed from the neuronal membrane by an enzymatic process similar to that involved in the non-amyloidogenic shedding of APP. Our data demonstrated that the content of membrane bound and soluble forms of APP, AChE and BuChE signifi cantly increase in various brain structures of rats during the fi rst month of postnatal life suggesting their role in brain development and synaptogenesis. The levels of soluble and membrane-bound forms of these proteins were affected by prenatal hypoxia with subsequent developmental defi cit observed in these animals. The molecular mechanisms of the APP and AChE shedding and their involvement in the pathogenesis of AD will also be discussed. Supported: the UK MRC, RAS “Fundamental sciences to medicine
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