Amyloid Precursor Protein, or APP, is a large, transmembrane protein expressed in numerous tissues, but it is particularly concentrated at the synapses of neurons in the brain. The protein’s primary function remains a subject of ongoing research, though it is understood to be essential for neuronal growth, survival, and post-injury repair mechanisms. Proper processing of APP is vital for maintaining neurophysiological homeostasis and cognitive function throughout the lifespan.
Origin
The protein was first identified in the context of neurological research, specifically due to its role as the source molecule for the amyloid-beta peptide, which forms the characteristic plaques found in the brains of individuals with Alzheimer’s disease. The term itself is purely descriptive, combining the Greek word amylo (starch) with precursor (something that precedes) to describe the protein that precedes the pathological amyloid material.
Mechanism
APP is metabolized through two primary pathways: the non-amyloidogenic pathway and the amyloidogenic pathway. In the non-amyloidogenic process, the protein is cleaved by alpha-secretase and gamma-secretase, producing soluble fragments that are generally considered neuroprotective. Conversely, the amyloidogenic pathway involves cleavage by beta-secretase and gamma-secretase, leading to the generation of the neurotoxic amyloid-beta peptides, which can aggregate and disrupt synaptic signaling and cellular communication.
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