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APP

Official Full Name
amyloid beta precursor protein
Organism
Homo sapiens
GeneID
351
Background
This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Aug 2014]
Synonyms
AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; preA4; CTFgamma; alpha-sAPP;
Bio Chemical Class
mRNA target
Protein Sequence
MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN
Open
Disease
Alzheimer disease
Approved Drug
3 +
Clinical Trial Drug
41 +
Discontinued Drug
3 +

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Detailed Information

Particularly because of its critical function in Alzheimer's disease (AD), the Amyloid Beta Precursor Protein (APP) gene has become a prominent actor in neurobiology. This transmembrane protein shows how one gene may significantly affect cellular health and disease etiology by means of its sophisticated processing and many roles.

Discovery and Structural Insights

Little revelations that eventually exposed APP's function as both a cell surface receptor and a precursor of many bioactive peptides have defined the path to knowledge about this molecule. By means of alternative splicing, the APP gene generates many isoforms that enable intricate interactions and varied cellular roles. Especially, the amyloid-beta (Aβ) peptide of APP is well-known as it provides the protein foundation of the amyloid plaques unique to Alzheimer's disease. This historical background emphasizes the need of APP in clinical research as well as in basic neuroscience.

Functional Complexity and Cellular Roles

The use of Apps goes well beyond their function in AD pathogenesis. Being a cell surface receptor, it is essential for physiology in neurons especially in neurite development and neuronal adhesion. By improving connections between APP molecules on adjacent cells and therefore strengthening communication and connectivity among neurons, the protein helps to generate synapses. Moreover, APP is a kinesin I membrane receptor that is essential for axonal movement, hence preserving neural health and function.

Apart from these duties, APP controls oxidative stress by means of copper ion reduction and supports copper homeostasis. Fascinatingly, some splice isoforms of APP show protease inhibitor activity, underlining even more the complex character of the protein. Many protein-protein interactions help the APP to be involved in cell motility and transcription control. Especially, it highlights its complicated regulating power by inducing transcription activation by binding to APBB1-KAT5 and blocking Notch signaling via contact with Numb.

Pathological Mechanisms and Disease Association

Particularly in Alzheimer's, the link between app and illness is complex and involves several important mechanisms:

1. Amyloid-Beta Formation and Toxicity

Two main routes of app processing are the amyloidogenic pathway including β- and γ-secretases and the non-amyloidogenic pathway driven by α- and γ-secretases. The latter route generates Aβ peptides mostly Aβ1-40 and more insoluble Aβ1-42. These peptides tend to gather into oligomers, protofibrils, and finally the distinctive amyloid plaques seen in the brains of AD patients.

2. Prion-Like Properties

Fascinatingly, Aβ has prion-like properties that enable it to spread disease by self-replicating. Time- and dose-dependent cerebral amyloidosis in APP transgenic mice is induced by administering diluted Aβ-containing brain extracts, studies show. This feature has great consequences for possible therapy approaches and the course of a disease.

3. Direct and Indirect Toxicity Mechanisms

Aβ's toxicity shows up as direct mitochondrial damage from contact with alcohol dehydrogenase, disturbance of the endosomal-lysosomal system, and malfunction of cellular transport systems. Indirect toxicity mostly caused by immunological activation and inflammation involves microglial activation and many vascular elements compromising blood-brain barrier integrity.

Figure 1 illustrates the distinct differences in APP cleavage mechanisms, highlighting the accumulation of amyloid-beta (Aβ) peptides in the Alzheimer brain, which contributes to neurodegeneration.Figure 1. Comparison of the amyloid beta precursor protein (APP) processing pathways between a healthy individual (left) and an Alzheimer's disease patient (right).

Therapeutic Implications and Future Directions

Different treatment approaches for Alzheimer's disease have evolved from the thorough knowledge of APP. These methods target molecules like LRP1 by means of immunotherapy, inhibition of β- and γ-secretases to lower Aβ generation, and use of new technologies like nanotechnology.

Promising recent developments include Lecanemab, the first FDA-approved medication aiming against Aβ. Still, reaching cognitive recovery is a multifaceted difficulty that calls for a comprehensive therapy strategy addressing the complexity of neurodegeneration. With an increasing focus on advanced microscopy techniques for observing Aβ structure and distribution, the impact of environmental factors and exercise on modulating APP-related pathology, and multidisciplinary approaches combining several therapeutic strategies, research in this area keeps changing.

References:

  1. Cho Y, Bae HG, Okun E, et al. Physiology and pharmacology of amyloid precursor protein. Pharmacol Ther. 2022 Jul;235:108122.
  2. Shinohara M, Ono K. Anti-Amyloid Antibody Therapy for Alzheimer's Disease. Brain Nerve. 2024;76(10):1119-1125.
  3. Bahk YY, Ahsan-Ul-Bari M, Kim YJ. Biomedical application of phosphoproteomics in neurodegenerative diseases. J Microbiol Biotechnol. 2013 Mar;23(3):279-88.
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