Gotowe bibliografie tematyczne / Amyloid beta-protein precursor

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Gotowa bibliografia na temat „Amyloid beta-protein precursor”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 26 lipca 2024

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Artykuły w czasopismach na temat "Amyloid beta-protein precursor"

Koo, E. H., S. L. Squazzo, D. J. Selkoe i 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, nr 5 (1.05.1996): 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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Naushad, Mehjabeen, Siva Sundara Kumar Durairajan, Amal Kanti Bera, Sanjib Senapati i Min Li. "Natural Compounds with Anti-BACE1 Activity as Promising Therapeutic Drugs for Treating Alzheimerʼs Disease". Planta Medica 85, nr 17 (16.10.2019): 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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Cai, X., T. Golde i S. Younkin. "Release of excess amyloid beta protein from a mutant amyloid beta protein precursor". Science 259, nr 5094 (22.01.1993): 514–16. http://dx.doi.org/10.1126/science.8424174.

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Nunan, Janelle, i David H. Small. "Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease". Essays in Biochemistry 38 (1.10.2002): 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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Parkin, Edward T., Jessica E. Hammond, Lauren Owens i 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, nr 1 (13.01.2022): 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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Wilquet, Valérie, i Bart De Strooper. "Amyloid-beta precursor protein processing in neurodegeneration". Current Opinion in Neurobiology 14, nr 5 (październik 2004): 582–88. http://dx.doi.org/10.1016/j.conb.2004.08.001.

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Schubert, David, Greg Cole, Tsunao Saitoh i Tilman Oltersdorf. "Amyloid beta protein precursor is a mitogen". Biochemical and Biophysical Research Communications 162, nr 1 (lipiec 1989): 83–88. http://dx.doi.org/10.1016/0006-291x(89)91965-7.

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Ling, Xie, R. N. Martins, M. Racchi, S. Craft i E. Helmerhorst. "Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor". Journal of Alzheimer's Disease 4, nr 5 (1.11.2002): 369–74. http://dx.doi.org/10.3233/jad-2002-4504.

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Ayoubi, Riham, Maryam Fotouhi, Donovan Worrall, Kathleen Southern i Carl Laflamme. "Identification of high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence". F1000Research 12 (9.08.2023): 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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Ghiso, J., E. Matsubara, A. Koudinov, N. H. Choi-Miura, M. Tomita, T. Wisniewski i 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, nr 1 (1.07.1993): 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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Rozprawy doktorskie na temat "Amyloid beta-protein precursor"

Dooley, Nora P. "Analysis of beta-amyloid precursor protein in Alzheimer's fibroblasts". Thesis, McGill University, 1992. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=56982.

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One of the hallmarks of Alzheimer's disease is the accumulation of beta-amyloid protein in the core of neuritic plaques. This 38-40 amino acid polypeptide is derived from a larger precursor known as beta-amyloid precursor protein (BAPP). In this thesis the expression of this precursor in cultured human fibroblasts obtained from Alzheimer's patients and age-matched controls is examined at the mRNA and protein level. Using the technique of reverse transcriptase-polymerase chain reaction, human fibroblasts were found to express BAPP transcripts encoding 770, 751, 714, and 695 amino acids. In immunocytochemical studies employing a monoclonal antibody to BAPP, this precursor was determined to be associated with the intermediate filament network. As well, on Western blots, aside from the bands of predicted molecular weights, a Triton-soluble 57 kDn band was detected. These findings lend support to the theory that aside from its putative extracellular functions, BAPP may play a vital intracellular role.

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Stephens, David John. "Intracellular processing of the Alzheimer's #beta#-amyloid precursor protein". Thesis, St George's, University of London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362427.

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Jung, Sonia Sun-Yung. "Expression and processing of the Alzheimer's beta-amyloid precursor protein". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0031/NQ64584.pdf.

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Jung, Sonia Sun-Yung 1968. "Expression and processing of the Alzheimer's beta-amyloid precursor protein". Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=36618.

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Alzheimer's disease (AD) is the most common neurodegenerative disease affecting the elderly. One of the main pathological hallmarks of AD is abundant senile plaques found in brain parenchyma and in the meningovasculature. The core of these senile plaques is predominantly composed of the 40--43 amino acid beta-amyloid (Abeta) peptide which arises from proteolytic cleavage of the beta-amyloid precursor protein (betaAPP), a glycoprotein with a predicted structure of a transmembrane protein. Most studies of betaAPP expression and processing have focused on cultured cell systems. Previously, our laboratory reported that immediately ex vivo human peripheral blood lymphocytes did not express cell surface betaAPP. Here, we investigated expression of betaAPP in various immediately ex vivo cell types from rodent and human species to determine whether or not our previous findings extended to different cell types and species. Cell surface expression of betaAPP was detected on immediately ex vivo rodent and human adult brain cells, and human peripheral blood monocytes by using various anti-betaAPP antibodies and flow cytometry; however, peripheral cells such as rodent lymphoid cells, hepatocytes, and kidney cells or human lymphoid cells did not display cell surface immunoreactivity, although all cells expressed abundant betaAPP intracellularly. This suggests cell-specific processing of the betaAPP molecule. We extended our studies with human peripheral blood monocytes to examine any differences between different age groups and AD patients. We demonstrate that cell surface betaAPP decreases with aging; however, it is significantly increased in AD patients compared to healthy age-matched controls. Our data suggest that a proportion of peripheral Abeta may be derived from monocyte/macrophages, and that defects in brain cell processing of betaAPP in AD may be shared by this readily accessible peripheral cell. Investigation of immediately ex vivo human adult brain cells demonstrat

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Kim, Joung-Hun. "Electrophysiological and biochemical studies of #beta#-amyloid precursor protein fragments". Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394383.

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Sultana, Joynab. "Behavioral Effects of Amyloid Precursor Protein beta Mutation in zebrafish". Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-421155.

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Amyloid precursor protein beta (βAPP) plays an important role in the pathogenesis of Alzheimer’s disease. An appb mutant strain of zebrafish has been previously generated and has shown increased boldness. Here we tested boldness by Novel Tank Diving Test and compared the results between the wildtype AB strain controls (WT) (N=16) and appb mutant strain (N=28), as well as between two Swedish testing institutions that use different protocols. Fish were tracked by automated video tracking in Ethovision. Compared with the wild type fish, using both the Uppsala and Gothenburg protocols, the mutant fish have a higher cumulative duration in the top area suggesting increased boldness. Greater boldness in mutants appears specifically context dependent and only expressed when the test fish is taken from a larger group of fish.

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Selivanova, Alexandra. "Intracellular dynamics of Alzheimer disease-related proteins /". Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-234-7/.

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Heuvel, Corinna van den. "Studies on upregulation of amyloid precursor protein in response to traumatic brain injury /". Title page, contents and abstract only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phv22723.pdf.

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Ly, Philip T. T. "Glycogen synthase kinase-3 signaling in Alzheimer's disease : regulation of beta-amyloid precursor protein processing and amyloid beta protein production". Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/42848.

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Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase that plays a part in a number of physiological processes ranging from glycogen metabolism to gene transcription. Recent studies indicated that GSK3 also involved in the formation of Alzheimer’s disease (AD) pathologies: neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles develop when abnormal tau proteins accumulate inside neurons and form insoluble filaments, and amyloid plaques develop when the amyloid β protein (Aβ) accumulates in increasingly insoluble forms. The Aβ peptide is generated through sequential cleavages of the β-amyloid precursor protein by β-secretase (BACE1) and γ-secretase. Accumulation of insoluble Aβ is believed to trigger the initial series of neurodegenerative events leading to AD. Therefore, inhibition of the pathways that lead to Aβ generation will have therapeutic implications for AD treatment. The mechanism by which GSK3 affects APP processing and Aβ production has been controversial. Previous published reports have found differential effects on GSK3-mediated APP processing. This thesis entails a thorough investigation of GSK3’s role in APP processing and Aβ production. First, the therapeutic effects of the anti-convulsant drug, valproic acid (VPA) were tested in AD modeled mice. VPA, a known GSK3 inhibitor could interfere with Aβ production, and rescued memory deficits. In addition to inhibiting GSK3 activity, VPA also stimulate a plethora of signaling cascades. To further our understanding of GSK3’s effect on APP processing, a GSK3 specific pharmacological inhibitor (AR-A014418) and siRNA technologies were used in our systems. With specific GSK3β inhibition, we showed that BACE1-mediated cleavage of APP and Aβ production were reduced. Moreover, GSK3β induced BACE1 gene expression depends on NFκB activity. Additionally, specific inhibition of GSK3 also reduced Aβ production and neuritic plaque formation in AD modeled mice, as well as improved memory functions. Finally, this thesis examined in detail the role of GSK3 in AD pathogenesis. This study demonstrated for the first time that the GSK3β signaling pathway regulates BACE1 transcription and facilitates Aβ production. These findings reinforced the notion that specific GSK3 inhibition is a safe and effective approach for treating AD.

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Leutz, Steffen. "Neuronaler Zelltod bei der Alzheimer-Demenz : Einfluss von b-Amyloid [Beta-Amyloid] und Amyloid-precursor-Protein /". Aachen : Shaker, 2002. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=009735379&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Książki na temat "Amyloid beta-protein precursor"

Weiming, Xia, i Xu Huaxi, red. Amyloid precursor protein: A practical approach. Boca Raton, Fla: CRC Press, 2005.

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L, Masters Colin, i Colloque médecine et recherche (9th : 1993 : Lyon, France), red. Amyloid protein precursor in development, aging, and Alzheimer's disease. Berlin: Springer-Verlag, 1994.

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1924-, Kameyama Masakuni, red. [Beta]-amyloid precursor proteins and neurotransmitter function: Proeedings of the eighth Workshop on Neurotransmitters and Diseases, Tokyo, June 1, 1991. Amsterdam, The Netherlands: Excerpta Medica, 1991.

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M, Nitsch Roger, i International Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, red. Alzheimer's disease: Amyloid precursor proteins, signal transduction, and neuronal transplantation. New York, N.Y: New York Academy of Sciences, 1993.

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Christian, Haass, red. Molecular biology of Alzheimer's disease: Genes and mechanisms involved in amyloid generation. Amsterdam: Harwood Academic Publishers, 1998.

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1936-, Wurtman Richard J., i New York Academy of Sciences., red. The neurobiology of Alzheimer's disease: Edited by Richard J. Wurtman ... [et al.]. New York: New York Academy of Sciences, 1996.

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1936-, Wurtman Richard J., i Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, red. The Neurobiology of Alzheimer's disease. New York, N.Y: New York Academy of Sciences, 1996.

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A, Nixon Ralph, Banner Carl D. B i New York Academy of Sciences., red. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York: NewYork Academy of Sciences, 1992.

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B, Banner Carl D., i Nixon Ralph A, red. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York, N.Y: New York Academy of Sciences, 1992.

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M, Hooper N., red. Alzheimer's disease: Methods and protocols. Totowa, N.J: Humana Press, 2000.

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Części książek na temat "Amyloid beta-protein precursor"

Caporaso, G. L., S. E. Gandy, J. D. Buxbaum, T. Suzuki, C. Nordstedt, K. Iverfeldt, T. V. Ramabhadran, A. J. Czernik, A. C. Nairn i P. Greengard. "Protein Phosphorylation Regulates the Cellular Trafficking and Processing of the Alzheimer Beta/A4 Amyloid Precursor Protein". W Molecular Mechanisms of Membrane Traffic, 201–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_42.

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Yamada, Takeshi, Ryutaro Izumi, Hiroyuki Sasaki, Hirokazu Furuya, Ikuo Goto i Yoshiyuki Sasaki. "Structure and Expression of mRNA for the Mouse Homolog of Alzheimer Amyloid Beta Protein Precursor". W Basic, Clinical, and Therapeutic Aspects of Alzheimer’s and Parkinson’s Diseases, 47–50. Boston, MA: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4684-5844-2_9.

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El-Hachem, Nehme, Benjamin Haibe-Kains, Athar Khalil, Firas H. Kobeissy i Georges Nemer. "AutoDock and AutoDockTools for Protein-Ligand Docking: Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1(BACE1) as a Case Study". W Methods in Molecular Biology, 391–403. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6952-4_20.

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Kosik, K. S., i D. J. Selkoe. "Studies of the Beta-Amyloid Precursor Protein in Brain and the Pathological Transformation of Tau into the Neurofibrillary Tangle". W Genetics and Alzheimer’s Disease, 164–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73647-6_18.

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Anand, Abhinav, Neha Sharma, Monica Gulati i Navneet Khurana. "Amyloid Beta". W Research Anthology on Diagnosing and Treating Neurocognitive Disorders, 1–17. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-3441-0.ch001.

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Alzheimer's disease (AD), exhibiting accumulation of amyloid beta (Aβ) peptide as a foremost protagonist, is one of the top five causes of deaths. It is a neurodegenerative disorder (ND) that causes a progressive decline in memory and cognitive abilities. It is characterized by deposition of Aβ plaques and neurofibrillary tangles (NFTs) in the neurons, which in turn causes a decline in the brain acetylcholine levels. Aβ hypothesis is the most accepted hypothesis pertaining to the pathogenesis of AD. Amyloid Precursor Protein (APP) is constitutively present in brain and it is cleaved by three proteolytic enzymes (i.e., alpha, beta, and gamma secretases). Beta and gamma secretases cleave APP to form Aβ. Ubiquitin Proteasome System (UPS) is involved in the clearing of Aβ plaques. AD also involves impairment in UPS. The novel disease-modifying approaches involve inhibition of beta and gamma secretases. A number of clinical trials are going on worldwide with moieties targeting beta and gamma secretases. This chapter deals with an overview of APP and its enzymatic cleavage leading to AD.

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Anand, Abhinav, Neha Sharma, Monica Gulati i Navneet Khurana. "Amyloid Beta". W Advances in Medical Diagnosis, Treatment, and Care, 235–51. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch011.

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Penke, B., i T. Harkány. "Physiological role of amyloid precursor protein (APP) and beta-amyloid peptides". W Molecular Pathomechanisms and New Trends in Drug Research, 402–10. CRC Press, 2002. http://dx.doi.org/10.1201/9780203219973.ch33.

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Obici, L., G. De Rosa, G. Palladini, S. Marciano, S. Donadei, E. Arbustini, L. Verga, M. Concardi, G. Ferrari i G. Merlini. "Hereditary Cerebral Amyloid Angiopathy Associated with a Novel Amyloid Beta Precursor Protein Mutation". W Amyloid and Amyloidosis, 396–98. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494-141.

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Palladini, G., L. Obici, G. Merlini, S. Marciano, L. Verga, G. Ferrari, G. De Rosa, E. Arbustini, S. Donadei i M. Concardi. "Hereditary Cerebral Amyloid Angiopathy Associated with a Novel Amyloid Beta Precursor Protein Mutation". W Amyloid and Amyloidosis, 396–98. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494.ch136.

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"Amyloid Beta (A4) Precursor Protein-Binding, Family B, Member 1 Interacting Protein (APBB1IP)". W Encyclopedia of Signaling Molecules, 312. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_100202.

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Streszczenia konferencji na temat "Amyloid beta-protein precursor"

RajaRajeswari, P., S. Viswanadha Raju, Amira S. Ashour, Nilanjan Dey i Valentina E. Balas. "Active site cavities identification of amyloid beta precursor protein: Alzheimer disease study". W 2016 IEEE 20th Jubilee International Conference on Intelligent Engineering Systems (INES). IEEE, 2016. http://dx.doi.org/10.1109/ines.2016.7555143.

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von Arnim, Christine, Michael Wagner, Petra Weber i Herbert Schneckenburger. "TIRET microscopy: monitoring protein (amyloid precursor protein and beta-secretase) interaction on the surface of living cells". W Biomedical Optics (BiOS) 2007, redaktorzy Daniel L. Farkas, Robert C. Leif i Dan V. Nicolau. SPIE, 2007. http://dx.doi.org/10.1117/12.699856.

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Shakila, G., C. Meganathan, N. Sundaraganesan i H. Saleem. "Pharmacophore based virtual screening, molecular docking and density functional theory approaches to discover the potent beta-amyloid precursor protein (B-APP) inhibitor". W 7TH NATIONAL CONFERENCE ON HIERARCHICALLY STRUCTURED MATERIALS (NCHSM-2019). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5114592.

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Raporty organizacyjne na temat "Amyloid beta-protein precursor"

Elmann, Anat, Orly Lazarov, Joel Kashman i Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, marzec 2015. http://dx.doi.org/10.32747/2015.7597913.bard.

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We chose to focus our investigations on the effect of the active forms, TTF and AcA, rather than the whole (crude) extract. 1. To establish cultivation program designed to develop lead cultivar/s (which will be selected from the different Af accessions) with the highest yield of the active compounds TTF and/or achillolide A (AcA). These cultivar/s will be the source for the purification of large amounts of the active compounds when needed in the future for functional foods/drug development. This task was completed. 2. To determine the effect of the Af extract, TTF and AcA on neuronal vulnerability to oxidative stress in cultured neurons expressing FAD-linked mutants.Compounds were tested in N2a neuroblastoma cell line. In addition, we have tested the effects of TTF and AcA on signaling events promoted by H₂O₂ in astrocytes and by β-amyloid in neuronal N2a cells. 3. To determine the effect of the Af extract, TTF and AcA on neuropathology (amyloidosis and tau phosphorylation) in cultured neurons expressing FAD-linked mutants. 4. To determine the effect of A¦ extract, AcA and TTF on FAD-linked neuropathology (amyloidosis, tau phosphorylation and inflammation) in transgenic mice. 5. To examine whether A¦ extract, TTF and AcA can reverse behavioral deficits in APPswe/PS1DE9 mice, and affect learning and memory and cognitive performance in these FAD-linked transgenic mice. Background to the topic.Neuroinflammation, oxidative stress, glutamate toxicity and amyloid beta (Ab) toxicity are involved in the pathogenesis of Alzheimer's diseases. We have previously purified from Achilleafragrantissimatwo active compounds: a protective flavonoid named 3,5,4’-trihydroxy-6,7,3’-trimethoxyflavone (TTF, Fl-72/2) and an anti-inflammatory sesquiterpenelactone named achillolide A (AcA). Major conclusions, solutions, achievements. In this study we could show that TTF and AcA protected cultured astrocytes from H₂O₂ –induced cell death via interference with cell signaling events. TTF inhibited SAPK/JNK, ERK1/2, MEK1 and CREBphosphorylation, while AcA inhibited only ERK1/2 and MEK1 phosphorylation. In addition to its protective activities, TTF had also anti-inflammatory activities, and inhibited the LPS-elicited secretion of the proinflammatorycytokinesInterleukin 6 (IL-6) and IL-1b from cultured microglial cells. Moreover, TTF and AcA protected neuronal cells from glutamate and Abcytotoxicity by reducing the glutamate and amyloid beta induced levels of intracellular reactive oxygen species (ROS) and via interference with cell signaling events induced by Ab. These compounds also reduced amyloid precursor protein net processing in vitro and in vivo in a mouse model for Alzheimer’s disease and improvedperformance in the novel object recognition learning and memory task. Conclusion: TTF and AcA are potential candidates to be developed as drugs or food additives to prevent, postpone or ameliorate Alzheimer’s disease. Implications, both scientific and agricultural.The synthesis ofAcA and TTF is very complicated. Thus, the plant itself will be the source for the isolation of these compounds or their precursors for synthesis. Therefore, Achilleafragrantissima could be developed into a new crop with industrial potential for the Arava-Negev area in Israel, and will generate more working places in this region.

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