Alzheimer's amyloid-beta (A beta) is an essential synaptic protein, not neurotoxic junk.
Despite a decade long universal publication in favor of the view on amyloid-beta (A beta) as Alzheimer's disease culprit (solely neurotoxic for neurons and brain tissue), current scientific evidence leaves little doubt that A beta serves an essential role at synapse and in synaptic structure-functional plasticity that underlie learning and memory. Therefore, the change of A beta biology in Alzheimer's disease (as well as in a number of other human pathologies, including cardiovascular disease, neuromuscular junction disorders, NPC and Down's syndrome) may represent a physiological mechanism to compensate for impaired brain structure or function. In our own recent study A beta 1-40 rescued long term potentiation (LTP, a major model for activity-dependent CNS plasticity), while cholesterol synthesis inhibition abolished the restorative action of the A beta peptide. This study confirms that A beta protein is a functional player in synaptic structure-functional plasticity and in cholesterol neurochemical pathways. The article also calls for a need to critically re-evaluate a universal belief that transgenic mice with a transgene for amyloid-beta protein precursor (A beta PP) are a true model for Alzheimer's type neurodegeneration.
Koudinov
Alexei R
AR
Russian Academy of Medical Sciences, Moscow, Russia. P.O. Box 1665, Rehovot 76100, Israel. koudinov@neurobiologyoflipids.org.
Berezov
Temirbolat T
TT
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D006801:Humans; D009474:Neurons / Q000378:metabolism*; D013569:Synapses / Q000378:metabolism*
D016229:Amyloid beta-Peptides