APP

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APP

amyloid precursor protein.

APP

abbr.
amyloid precursor protein

amyloid precursor protein (APP)

a large transmembrane glycoprotein expressed on the cell surface and of uncertain function; it may be cleaved on the cell surface to a soluble form. Alternatively, cleavage may follow endocytosis and in some cases then yields 40 to 43 abnormal amino acid peptides, which aggregate to form Ab amyloid, associated with Alzheimer's disease.

APP

A gene on chromosome 21q21.3 that encodes a cell surface receptor and transmembrane precursor protein which is cleaved by secretases to form various peptides.

Molecular pathology
APP mutations are implicated in autosomal dominant Alzheimer’s disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy).

APP

Amyloid β protein precursor A membrane-spanning glycoprotein of unknown function, which is expressed in many mammalian tissues, the gene for which maps to chromosome 21. See Alzheimer's disease, β-amyloid.
References in periodicals archive ?
Abnormal cleavage, or failure to dear beta-amyloid peptides, causes them to accumulate into oligomers (two to 12 peptide strands joined together), fibrils and plaques.
Two of the identified mutations are responsible for an under-expression of SORL1, resulting in an increase in the production of the beta-amyloid peptide.
Protection against beta-amyloid peptide toxicity in vivo with long-term administration of ferulic acid.
Gamma-secretase cleaves APP at the other end of the beta-amyloid peptide, releasing it into the space outside the neuron.
It identifies another pathway that's important in regulating levels of beta-amyloid peptide," reports Dwain Thiele, chief of hepatology.
The Alzheimer's patients had significantly less beta-amyloid peptide and more tau protein in their spinal fluid than people in the other three groups did, says study coauthor Christoph Hock of the University of Zurich.
In research so far, a synthetic form of the beta-amyloid peptide, called AN-1792, was injected into six-week-old mice.
Alpha2-macroglobulin associates with beta-amyloid peptide and prevents fibril formation.
today announced data from a laboratory study demonstrating natural antibodies contained in GAMMAGARD LIQUID [Immune Globulin Intravenous (Human)] (IGIV), marketed as KIOVIG in the European Union, a plasma-derived antibody replacement therapy indicated for primary immunodeficiency disorders and being studied in Alzheimer's disease, binds directly to multiple aggregated, or clustered, forms of the beta-amyloid peptide molecule.
In addition, unpublished work by this team suggests that apo E-IV leads to denser deposits of the beta-amyloid peptide implicated in Alzheimer's disease.
Caprospinol binds to the Beta-Amyloid peptide, preventing its aggregation into more neurotoxic entities and entry into neurons, as well as protecting neuronal mitochondria from Beta-Amyloid induced damage, and maintaining neuronal cell energy levels.
Like the beta-amyloid peptide, this 37-amino-acid particle, called amylin, aggregates; but instead of forming plaques in the brain, as beta-amyloid does, amylin accumulates near insulin-producing beta cells located in the pancreas.