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Journal articles on the topic 'Amyloid beta-protein precursor'

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Published: 4 June 2021

Last updated: 26 July 2024

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1

Koo, E. H., S. L. Squazzo, D. J. Selkoe, and C. H. Koo. "Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody." Journal of Cell Science 109, no. 5 (May 1, 1996): 991–98. http://dx.doi.org/10.1242/jcs.109.5.991.

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Amyloid beta-protein, the principal constituent of amyloid fibrils found in senile plaques and blood vessels in Alzheimer's disease, is constitutively produced and released into medium of cultured cells. Amyloid beta-protein is derived by proteolysis of the beta-amyloid precursor protein by unclear mechanisms. Beta-amyloid precursor protein is a transmembrane protein which can be processed to release a large secretory product or processed in the endosomal/lysosomal pathway without secretion. Previous studies have shown that from the cell surface, beta-amyloid precursor protein may be released after cleavage or internalized without cleavage, the latter in a pathway that both produces amyloid beta-protein and also targets some molecules to the lysosomal compartment. Analysis of beta-amyloid precursor protein trafficking is confounded by the concomitant secretion and internalization of molecules from the cell surface. To address this issue, we developed an assay, based on the binding of radioiodinated monoclonal antibody, to measure the release and internalization of cell surface beta-amyloid precursor protein in transfected cells. With this approach, we showed that surface beta-amyloid precursor protein is either rapidly released or internalized, such that the duration at the cell surface is very short. Approximately 30% of cell surface beta-amyloid precursor protein molecules are released. Following internalization, a fraction of molecules are recycled while the majority of molecules are rapidly sorted to the lysosomal compartment for degradation When the C terminus of beta-amyloid precursor protein is deleted, secretion is increased by approximately 2.5-fold as compared to wild-type molecules. There is concomitant decrease in internalization in these mutant molecules as well as prolongation of the resident time on the cell surface. This observation is consistent with recent evidence that signals within the cytoplasmic domain mediate beta-amyloid precursor protein internalization.

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2

Naushad, Mehjabeen, Siva Sundara Kumar Durairajan, Amal Kanti Bera, Sanjib Senapati, and Min Li. "Natural Compounds with Anti-BACE1 Activity as Promising Therapeutic Drugs for Treating Alzheimerʼs Disease." Planta Medica 85, no. 17 (October 16, 2019): 1316–25. http://dx.doi.org/10.1055/a-1019-9819.

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AbstractAlzheimerʼs disease is a neurodegenerative disease that leads to irreversible neuronal damage. Senile plaques, composed of amyloid beta peptide, is the principal abnormal characteristic of the disease. Among the factors involved, the secretase enzymes, namely, α secretase, beta-site amyloid precursor protein-cleaving enzyme, β secretase, and γ secretase, hold consequential importance. Beta-site amyloid precursor protein-cleaving enzyme 1 is considered to be the rate-limiting factor in the production of amyloid beta peptide. Research supporting the concept of inhibition of beta-site amyloid precursor protein-cleaving enzyme activity as one of the effective therapeutic targets in the mitigation of Alzheimerʼs disease is well accepted. The identification of natural compounds, such as β-amyloid precursor protein-selective beta-site amyloid precursor protein-cleaving enzyme inhibitors, and the idea of compartmentalisation of the beta-site amyloid precursor protein-cleaving enzyme 1 action have caused a dire need to closely examine the natural compounds and their effectiveness in the disease mitigation. Many natural compounds have been reported to effectively modulate beta-site amyloid precursor protein-cleaving enzyme 1. At lower doses, compounds like 2,2′,4′-trihydroxychalcone acid, quercetin, and myricetin have been shown to effectively reduce beta-site amyloid precursor protein-cleaving enzyme 1 activity. The currently used five drugs that are marketed and used for the management of Alzheimerʼs disease have an increased risk of toxicity and restricted therapeutic efficiency, hence, the search for new anti-Alzheimerʼs disease drugs is of primary concern. A variety of natural compounds having pure pharmacological moieties showing multitargeting activity and others exhibiting specific beta-site amyloid precursor protein-cleaving enzyme 1 inhibition as discussed below have superior biosafety. Many of these compounds, which are isolated from medicinal herbs and marine flora, have been long used for the treatment of various ailments since ancient times in the Chinese and Ayurvedic medical systems. The aim of this article is to review the available data on the selected natural compounds, giving emphasis to the inhibition of beta-site amyloid precursor protein-cleaving enzyme 1 activity as a mode of Alzheimerʼs disease treatment.

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3

Cai, X., T. Golde, and S. Younkin. "Release of excess amyloid beta protein from a mutant amyloid beta protein precursor." Science 259, no. 5094 (January 22, 1993): 514–16. http://dx.doi.org/10.1126/science.8424174.

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4

Nunan, Janelle, and David H. Small. "Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease." Essays in Biochemistry 38 (October 1, 2002): 37–49. http://dx.doi.org/10.1042/bse0380037.

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The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.

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5

Parkin, Edward T., Jessica E. Hammond, Lauren Owens, and Matthew D. Hodges. "The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein." PLOS ONE 17, no. 1 (January 13, 2022): e0255715. http://dx.doi.org/10.1371/journal.pone.0255715.

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The amyloid cascade hypothesis proposes that excessive accumulation of amyloid beta-peptides is the initiating event in Alzheimer’s disease. These neurotoxic peptides are generated from the amyloid precursor protein via sequential cleavage by β- and γ-secretases in the ’amyloidogenic’ proteolytic pathway. Alternatively, the amyloid precursor protein can be processed via the ’non-amyloidogenic’ pathway which, through the action of the α-secretase a disintegrin and metalloproteinase (ADAM) 10, both precludes amyloid beta-peptide formation and has the additional benefit of generating a neuroprotective soluble amyloid precursor protein fragment, sAPPα. In the current study, we investigated whether the orphan drug, dichloroacetate, could alter amyloid precursor protein proteolysis. In SH-SY5Y neuroblastoma cells, dichloroacetate enhanced sAPPα generation whilst inhibiting β–secretase processing of endogenous amyloid precursor protein and the subsequent generation of amyloid beta-peptides. Over-expression of the amyloid precursor protein partly ablated the effect of dichloroacetate on amyloidogenic and non-amyloidogenic processing whilst over-expression of the β-secretase only ablated the effect on amyloidogenic processing. Similar enhancement of ADAM-mediated amyloid precursor protein processing by dichloroacetate was observed in unrelated cell lines and the effect was not exclusive to the amyloid precursor protein as an ADAM substrate, as indicated by dichloroacetate-enhanced proteolysis of the Notch ligand, Jagged1. Despite altering proteolysis of the amyloid precursor protein, dichloroacetate did not significantly affect the expression/activity of α-, β- or γ-secretases. In conclusion, dichloroacetate can inhibit amyloidogenic and promote non-amyloidogenic proteolysis of the amyloid precursor protein. Given the small size and blood-brain-barrier permeability of the drug, further research into its mechanism of action with respect to APP proteolysis may lead to the development of therapies for slowing the progression of Alzheimer’s disease.

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6

Wilquet, Valérie, and Bart De Strooper. "Amyloid-beta precursor protein processing in neurodegeneration." Current Opinion in Neurobiology 14, no. 5 (October 2004): 582–88. http://dx.doi.org/10.1016/j.conb.2004.08.001.

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7

Schubert, David, Greg Cole, Tsunao Saitoh, and Tilman Oltersdorf. "Amyloid beta protein precursor is a mitogen." Biochemical and Biophysical Research Communications 162, no. 1 (July 1989): 83–88. http://dx.doi.org/10.1016/0006-291x(89)91965-7.

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8

Ling, Xie, R. N. Martins, M. Racchi, S. Craft, and E. Helmerhorst. "Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor." Journal of Alzheimer's Disease 4, no. 5 (November 1, 2002): 369–74. http://dx.doi.org/10.3233/jad-2002-4504.

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9

Ayoubi, Riham, Maryam Fotouhi, Donovan Worrall, Kathleen Southern, and Carl Laflamme. "Identification of high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence." F1000Research 12 (August 9, 2023): 956. http://dx.doi.org/10.12688/f1000research.139867.1.

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The amyloid-beta precursor protein is a transmembrane protein expressed in many tissues and highly concentrated in the brain. The protein is of significant interest due to its involvement in the generation of amyloidogenic β-amyloid peptides, prone to plaque formation that is characteristic of Alzheimer’s Disease. The scientific community would benefit from the availability of high-quality anti-amyloid-beta precursor protein antibodies to enhance reproducible research on this target. In this study, we characterized eleven amyloid-beta precursor protein commercial antibodies for Western blot, immunoprecipitation, and immunofluorescence using a standardized experimental protocol based on comparing read-outs in knockout cell lines and isogenic parental controls. We identified many high-performing antibodies and encourage readers to use this report as a guide to select the most appropriate antibody for their specific needs.

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10

Ghiso, J., E. Matsubara, A. Koudinov, N. H. Choi-Miura, M. Tomita, T. Wisniewski, and B. Frangione. "The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex." Biochemical Journal 293, no. 1 (July 1, 1993): 27–30. http://dx.doi.org/10.1042/bj2930027.

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The amyloid fibrils deposited in Alzheimer's neuritic plaque cores and cerebral blood vessels are mainly composed of aggregated forms of a unique peptide, 39-42 amino acids long, named amyloid beta (A beta). A similar, although soluble, A beta (‘sA beta’) has been identified in cerebrospinal fluid, plasma and cell supernatants, indicating that it is normally produced by proteolytic processing of its precursor protein, amyloid precursor protein (APP). Using direct binding experiments we have isolated and characterized an 80 kDa circulating protein that specifically interacts with a synthetic peptide identical with A beta. The protein was unmistakably identified as SP-40,40 or ApoJ, a cytolytic inhibitor and lipid carrier, by means of amino acid sequence and immunoreactivity with specific antibodies. Immunoprecipitation with anti-SP-40,40 retrieved soluble A beta from cerebrospinal fluid, indicating that the interaction occurs in vivo.

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11

Suzuki, N., T. Cheung, X. Cai, A. Odaka, L. Otvos, C. Eckman, T. Golde, and S. Younkin. "An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants." Science 264, no. 5163 (May 27, 1994): 1336–40. http://dx.doi.org/10.1126/science.8191290.

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12

Ayoubi, Riham, Maryam Fotouhi, Donovan Worrall, Kathleen Southern, and Carl Laflamme. "A guide to selecting high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence." F1000Research 12 (April 10, 2024): 956. http://dx.doi.org/10.12688/f1000research.139867.2.

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The amyloid-beta precursor protein is a transmembrane protein expressed in many tissues and highly concentrated in the brain. The protein is of significant interest due to its involvement in the generation of amyloidogenic β-amyloid peptides, prone to plaque formation that is characteristic of Alzheimer’s Disease. The scientific community would benefit from the availability of high-quality anti-amyloid-beta precursor protein antibodies to enhance reproducible research on this target. In this study, we characterized eleven amyloid-beta precursor protein commercial antibodies for Western blot, immunoprecipitation, and immunofluorescence using a standardized experimental protocol based on comparing read-outs in knockout cell lines and isogenic parental controls. These studies are part of a larger, collaborative initiative seeking to address antibody reproducibility issues by characterizing commercially available antibodies for human proteins and publishing the results openly as a resource for the scientific community. While use of antibodies and protocols vary between laboratories, we encourage readers to use this report as a guide to select the most appropriate antibodies for their specific needs.

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13

Younkin, S. G., X. H. Song, D. Scheuner, C. Eckman, C.-M. Prada, J. Jensen, L. Lannfelt, et al. "The effect of amyloid precursor protein and presenilin mutations on amyloid beta protein." Biological Psychiatry 39, no. 7 (April 1996): 562. http://dx.doi.org/10.1016/0006-3223(96)84161-8.

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14

Ambure, Pravin, and Kunal Roy. "Understanding the structural requirements of cyclic sulfone hydroxyethylamines as hBACE1 inhibitors against Aβ plaques in Alzheimer's disease: a predictive QSAR approach." RSC Advances 6, no. 34 (2016): 28171–86. http://dx.doi.org/10.1039/c6ra04104c.

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Beta (β)-site amyloid precursor protein cleaving enzyme 1 (BACE1) is one of the most important targets in Alzheimer's disease (AD), which is responsible for production and accumulation of beta amyloid (Aβ).

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15

Haass, C., E. H. Koo, D. B. Teplow, and D. J. Selkoe. "Polarized secretion of beta-amyloid precursor protein and amyloid beta-peptide in MDCK cells." Proceedings of the National Academy of Sciences 91, no. 4 (February 15, 1994): 1564–68. http://dx.doi.org/10.1073/pnas.91.4.1564.

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16

Jin, Lee-Way, and Hyun-seok Hong. "P1-450: Tomoregulin-2 binds beta-amyloid precursor protein and intracellular beta-amyloid (Aβ)." Alzheimer's & Dementia 4 (July 2008): T351—T352. http://dx.doi.org/10.1016/j.jalz.2008.05.1032.

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17

Mattson, M. P. "Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives." Physiological Reviews 77, no. 4 (October 1, 1997): 1081–132. http://dx.doi.org/10.1152/physrev.1997.77.4.1081.

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beta-Amyloid precursor protein (beta-APP), the source of the fibrillogenic amyloid beta-peptide (A beta) that accumulates in the brain of victims of Alzheimer's disease, is a multifunctional protein that is widely expressed in the nervous system. beta-Amyloid precursor protein is axonally transported and accumulates in presynaptic terminals and growth cones. A secreted form of beta-APP (sAPP alpha) is released from neurons in response to electrical activity and may function in modulation of neuronal excitability, synaptic plasticity, neurite outgrowth, synaptogenesis, and cell survival. A signaling pathway involving guanosine 3',5'-cyclic monophosphate is activated by sAPP alpha and modulates the activities of potassium channels, N-methyl-D-aspartate receptors, and the transcription factor NF kappa B. Additional functions of beta-APP may include modulation of cell adhesion and regulation of proliferation of nonneuronal cells. Alternative enzymatic processing of beta-APP liberates A beta, which has a propensity to form amyloid fibrils; A beta can damage and kill neurons and increase their vulnerability to excitotoxicity. The mechanism involves generation of oxyradicals and impairment of membrane transport systems (e.g., ion-motive ATPases and glutamate and glucose transporters). Genetic mutations or age-related metabolic changes may promote neuronal degeneration in Alzheimer's disease by increasing production of A beta and/or decreasing levels of neuroprotective sAPP alpha.

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18

Mönning, U., G. König, R. B. Banati, H. Mechler, C. Czech, J. Gehrmann, U. Schreiter-Gasser, C. L. Masters, and K. Beyreuther. "Alzheimer beta A4-amyloid protein precursor in immunocompetent cells." Journal of Biological Chemistry 267, no. 33 (November 1992): 23950–56. http://dx.doi.org/10.1016/s0021-9258(18)35929-5.

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19

Jaffe, A. B., C. D. Toran-Allerand, P. Greengard, and S. E. Gandy. "Estrogen regulates metabolism of Alzheimer amyloid beta precursor protein." Journal of Biological Chemistry 269, no. 18 (May 1994): 13065–68. http://dx.doi.org/10.1016/s0021-9258(17)36796-0.

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20

Schmaier, Alvin H. "The amyloid beta-precursor protein—The unappreciated cerebral anticoagulant." Thrombosis Research 155 (July 2017): 149–51. http://dx.doi.org/10.1016/j.thromres.2017.05.037.

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21

Donnelly, Robert J., Arnold J. Friedhoff, Bernard Beer, Arthur J. Blume, and Michael P. Vitek. "Interleukin-1 stimulates the beta-amyloid precursor protein promoter." Cellular and Molecular Neurobiology 10, no. 4 (December 1990): 485–95. http://dx.doi.org/10.1007/bf00712843.

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22

Orobets, Kseniia S., and Andrey L. Karamyshev. "Amyloid Precursor Protein and Alzheimer’s Disease." International Journal of Molecular Sciences 24, no. 19 (September 30, 2023): 14794. http://dx.doi.org/10.3390/ijms241914794.

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Alzheimer’s disease (AD) is one of the most common neurodegenerative disorders associated with age or inherited mutations. It is characterized by severe dementia in the late stages that affect memory, cognitive functions, and daily life overall. AD progression is linked to the accumulation of cytotoxic amyloid beta (Aβ) and hyperphosphorylated tau protein combined with other pathological features such as synaptic loss, defective energy metabolism, imbalances in protein, and metal homeostasis. Several treatment options for AD are under investigation, including antibody-based therapy and stem cell transplantation. Amyloid precursor protein (APP) is a membrane protein considered to play a main role in AD pathology. It is known that APP in physiological conditions follows a non-amyloidogenic pathway; however, it can proceed to an amyloidogenic scenario, which leads to the generation of extracellular deleterious Aβ plaques. Not all steps of APP biogenesis are clear so far, and these questions should be addressed in future studies. AD is a complex chronic disease with many factors that contribute to disease progression.

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23

Oestereich, Felix, Heiko J. Bittner, Christoph Weise, Lisa Grohmann, Lisa-Kristin Janke, Peter W. Hildebrand, Gerhard Multhaup, and Lisa-Marie Munter. "Impact of Amyloid Precursor Protein Hydrophilic Transmembrane Residues on Amyloid-Beta Generation." Biochemistry 54, no. 17 (April 23, 2015): 2777–84. http://dx.doi.org/10.1021/acs.biochem.5b00217.

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24

Arbor, Sage. "Targeting amyloid precursor protein shuttling and processing - long before amyloid beta formation." Neural Regeneration Research 12, no. 2 (2017): 207. http://dx.doi.org/10.4103/1673-5374.200800.

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25

Caporaso, G. L., S. E. Gandy, J. D. Buxbaum, T. V. Ramabhadran, and P. Greengard. "Protein phosphorylation regulates secretion of Alzheimer beta/A4 amyloid precursor protein." Proceedings of the National Academy of Sciences 89, no. 7 (April 1, 1992): 3055–59. http://dx.doi.org/10.1073/pnas.89.7.3055.

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26

Itoh, Naohiro, Masayasu Okochi, Shinji Tagami, Kouhei Nishitomi, Taisuke Nakayama, Kanta Yanagida, Akio Fukumori, et al. "Destruxin E Decreases Beta-Amyloid Generation by Reducing Colocalization of Beta-Amyloid-Cleaving Enzyme 1 and Beta-Amyloid Protein Precursor." Neurodegenerative Diseases 6, no. 5-6 (2009): 230–39. http://dx.doi.org/10.1159/000236902.

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27

Alasmari, Fawaz, Musaad A. Alshammari, Abdullah F. Alasmari, Wael A. Alanazi, and Khalid Alhazzani. "Neuroinflammatory Cytokines Induce Amyloid Beta Neurotoxicity through Modulating Amyloid Precursor Protein Levels/Metabolism." BioMed Research International 2018 (October 25, 2018): 1–8. http://dx.doi.org/10.1155/2018/3087475.

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Neuroinflammation has been observed in association with neurodegenerative diseases including Alzheimer’s disease (AD). In particular, a positive correlation has been documented between neuroinflammatory cytokine release and the progression of the AD, which suggests these cytokines are involved in AD pathophysiology. A histological hallmark of the AD is the presence of beta-amyloid (Aβ) plaques and tau neurofibrillary tangles. Beta-amyloid is generated by the sequential cleavage of beta (β) and gamma (γ) sites in the amyloid precursor protein (APP) by β- and γ-secretase enzymes and its accumulation can result from either a decreased Aβ clearance or increased metabolism of APP. Previous studies reported that neuroinflammatory cytokines reduce the efflux transport of Aβ, leading to elevated Aβ concentrations in the brain. However, less is known about the effects of neuroinflammatory mediators on APP expression and metabolism. In this article, we review the modulatory role of neuroinflammatory cytokines on APP expression and metabolism, including their effects on β- and γ-secretase enzymes.

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28

Shah, Hirak, Ashish Patel, Vruti Parikh, Afzal Nagani, Bhargav Bhimani, Umang Shah, and Tushar Bambharoliya. "The β-Secretase Enzyme BACE1: A Biochemical Enigma for Alzheimer’s Disease." CNS & Neurological Disorders - Drug Targets 19, no. 3 (August 17, 2020): 184–94. http://dx.doi.org/10.2174/1871527319666200526144141.

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Beta site amyloid precursor protein cleaving enzyme 1 (BACE1) is a rational target in Alzheimer’s Disease (AD) drug development due to its role in amyloidogenic cleavage of Amyloid Precursor Protein (APP) in generating Amyloid β (Aβ). This β-secretase cleaves not only Amyloid Precursor Protein (APP) and its homologues, but also small series of substrates including neuregulin and β subunit of voltage-gated sodium channel that play a very important role in the development and normal function of the brain. Moreover, BACE1 is modulated at the post-translational level by several factors that are associated with both physiological and pathological functions. Since the discovery of BACE1 over a decade ago, medicinal chemistry and pharmacokinetics of BACE1 small molecule inhibitors have proven challenging for the treatment of Alzheimer’s disease.

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29

Godara, Amandeep, Andy Y. Wang, Knarik Arkun, Teresa Fogaren, Adnan S. Qamar, Ellen D. McPhail, James Kryzanski, Ron Riesenburger, and Raymond Comenzo. "Unraveling a rare cause of spinal stenosis: Coexistent AL and ATTR amyloidosis involving the ligamentum flavum." Surgical Neurology International 13 (January 12, 2022): 12. http://dx.doi.org/10.25259/sni_1235_2021.

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Background: Amyloidosis is a protein misfolding disorder that leads to the deposition of beta-pleated sheets of a fibrillar derivative of various protein precursors. Identification of the type of precursor protein is integral in treatment decision-making. The presence of two different types of amyloid in the same patient is unusually rare, and there are no previous reports of two different types of amyloid deposition in the ligamentum flavum (LF) in the same patient. Case Description: Here, we describe two patients with spinal stenosis who underwent laminectomies and were found to have AL and ATTR amyloid deposits in the LF. Conclusion: As the spine is becoming recognized as a site for ATTRwt amyloid deposition, patients undergoing spinal decompression surgery may potentially benefit from evaluation for amyloidosis in the LF.

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30

De Strooper, B., and W. Annaert. "Proteolytic processing and cell biological functions of the amyloid precursor protein." Journal of Cell Science 113, no. 11 (June 1, 2000): 1857–70. http://dx.doi.org/10.1242/jcs.113.11.1857.

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Recent research has identified some key players involved in the proteolytic processing of amyloid precursor protein (APP) to amyloid beta-peptide, the principal component of the amyloid plaques in Alzheimer patients. Interesting parallels exists with the proteolysis of other proteins involved in cell differentiation, cholesterol homeostasis and stress responses. Since the cytoplasmic domain of APP is anchored to a complex protein network that might function in axonal elongation, dendritic arborisation and neuronal cell migration, the proteolysis of APP might be critically involved in intracellular signalling events.

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31

Tienari, P. J., B. De Strooper, E. Ikonen, M. Simons, A. Weidemann, C. Czech, T. Hartmann, et al. "The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein." EMBO Journal 15, no. 19 (October 1996): 5218–29. http://dx.doi.org/10.1002/j.1460-2075.1996.tb00907.x.

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32

Uhm, Kyung-Ok, Hirofumi Horike, Makoto Michikawa, and Cha-Gyun Jung. "P1-227: ATBF1 interacts with amyloid precursor protein and enhances amyloid-beta production." Alzheimer's & Dementia 6 (July 2010): S239—S240. http://dx.doi.org/10.1016/j.jalz.2010.05.778.

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33

Selkoe, D. J. "Normal and Abnormal Biology of the beta-Amyloid Precursor Protein." Annual Review of Neuroscience 17, no. 1 (March 1994): 489–517. http://dx.doi.org/10.1146/annurev.ne.17.030194.002421.

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34

McMeekin, S., C. H. Williams, J. Cummings, J. Law, B. Greer, and J. A. Johnston. "A beta-site amyloid precursor protein cleaving enzyme (BACE) assay." Biochemical Society Transactions 30, no. 3 (June 1, 2002): A81. http://dx.doi.org/10.1042/bst030a081b.

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35

Narlawar, Rajeshwar, Karlheinz Baumann, Robert Schubenel, and Boris Schmidt. "Curcumin Derivatives Inhibit or Modulate Beta-Amyloid Precursor Protein Metabolism." Neurodegenerative Diseases 4, no. 2-3 (2007): 88–93. http://dx.doi.org/10.1159/000101832.

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36

Zhong, Z., J. Higaki, K. Murakami, Y. Wang, R. Catalano, D. Quon, and B. Cordell. "Secretion of beta-amyloid precursor protein involves multiple cleavage sites." Journal of Biological Chemistry 269, no. 1 (January 1994): 627–32. http://dx.doi.org/10.1016/s0021-9258(17)42395-7.

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37

Davies, T. A., H. J. Long, K. Sgro, W. H. Rathbun, M. E. McMenamin, K. Seetoo, H. Tibbles, et al. "Activated Alzheimer Disease Platelets Retain More Beta Amyloid Precursor Protein." Neurobiology of Aging 18, no. 2 (March 1997): 147–53. http://dx.doi.org/10.1016/s0197-4580(97)00013-4.

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38

Okuda, R., K. Uchida, S. Tateyama, R. Yamaguchi, H. Nakayama, and N. Goto. "The distribution of amyloid beta precursor protein in canine brain." Acta Neuropathologica 87, no. 2 (February 1994): 161–67. http://dx.doi.org/10.1007/bf00296186.

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39

Xu, Huaxi. "Cellular and molecular basis of beta-amyloid precursor protein metabolism." Frontiers in Bioscience 3, no. 4 (1998): d399–407. http://dx.doi.org/10.2741/a283.

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40

Farber, SA, RM Nitsch, JG Schulz, and RJ Wurtman. "Regulated secretion of beta-amyloid precursor protein in rat brain." Journal of Neuroscience 15, no. 11 (November 1, 1995): 7442–51. http://dx.doi.org/10.1523/jneurosci.15-11-07442.1995.

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41

Reichard, R. Ross, Charles L. White, Christa L. Hladik, and David Dolinak. "Beta-Amyloid Precursor Protein Staining in Nonhomicidal Pediatric Medicolegal Autopsies." Journal of Neuropathology & Experimental Neurology 62, no. 3 (March 2003): 237–47. http://dx.doi.org/10.1093/jnen/62.3.237.

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42

Cunningham, D. D. "Protease nexin-2/amyloid beta-protein precursor: a cerebral anticoagulant?" Journal of Clinical Investigation 92, no. 5 (November 1, 1993): 2090. http://dx.doi.org/10.1172/jci116807.

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Sisodia, S. S. "Beta-amyloid precursor protein cleavage by a membrane-bound protease." Proceedings of the National Academy of Sciences 89, no. 13 (July 1, 1992): 6075–79. http://dx.doi.org/10.1073/pnas.89.13.6075.

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Yoshikai, Shun-ichi, Hiroyuki Sasaki, Katsumi Doh-ura, Hirokazu Furuya, and Yoshiyuki Sakaki. "Genomic organization of the human amyloid beta-protein precursor gene." Gene 87, no. 2 (March 1990): 257–63. http://dx.doi.org/10.1016/0378-1119(90)90310-n.

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Yoshikai, Shun-ichi, Hiroyuki Sasaki, Katsumi Doh-ura, Hirokazu Furuya, and Yoshiyuki Sakaki. "Genomic organization of the human-amyloid beta-protein precursor gene." Gene 102, no. 2 (June 1991): 291–92. http://dx.doi.org/10.1016/0378-1119(91)90093-q.

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Ishiura, Shoichi, Kazuhiko Tagawa, Kei Maruyama, and Koichi Suzuki. "Proteolytic cleavage of the Alzheimer's disease amyloid beta precursor protein." Neuroscience Research Supplements 17 (January 1992): 19. http://dx.doi.org/10.1016/0921-8696(92)90671-m.

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Altstiel, Larry D., and Nikolaos K. Robakis. "Expression of beta-amyloid precursor protein on neuron plasma membranes." Biological Psychiatry 25, no. 7 (April 1989): A118—A119. http://dx.doi.org/10.1016/0006-3223(89)91725-3.

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Okuda, R., K. Uchida, S. Tateyama, R. Yamaguchi, H. Nakayama, and N. Goto. "The distribution of amyloid beta precursor protein in canine brain." Acta Neuropathologica 87, no. 2 (February 1, 1994): 161–67. http://dx.doi.org/10.1007/s004010050071.

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Van Nostrand, W., A. Schmaier, J. Farrow, and D. Cunningham. "Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein." Science 248, no. 4956 (May 11, 1990): 745–48. http://dx.doi.org/10.1126/science.2110384.

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Schubert, D., R. Schroeder, M. LaCorbiere, T. Saitoh, and G. Cole. "Amyloid beta protein precursor is possibly a heparan sulfate proteoglycan core protein." Science 241, no. 4862 (July 8, 1988): 223–26. http://dx.doi.org/10.1126/science.2968652.

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