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Journal articles on the topic 'Alzheimer's disease; Amyloid precursor protein'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Nalbantoglu, Josephine. "β-Amyloid Protein in Alzheimer's Disease." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 18, S3 (August 1991): 424–27. http://dx.doi.org/10.1017/s0317167100032595.

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ABSTRACT:β-amyloid protein, a 42-43 amino acid polypeptide, accumulates abnormally in senile plaques and the cerebral vasculature in Alzheimer's disease. This polypeptide is derived from a membrane-associated precursor which has several isoforms expressed in many tissues. The precursor protein is processed constitutively within the P-amyloid domain, leading to the release of the large β-terminal portion into the extracellular medium, β-amyloid protein may be toxic to certain neuronal cell types and its early deposition may be an important event in the pathogenesis of Alzheimer's disease.

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2

Multhaup, G. "Amyloid precursor protein, copper and Alzheimer's disease." Biomedicine & Pharmacotherapy 51, no. 3 (January 1997): 105–11. http://dx.doi.org/10.1016/s0753-3322(97)86907-7.

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3

O'Brien, Richard J., and Philip C. Wong. "Amyloid Precursor Protein Processing and Alzheimer's Disease." Annual Review of Neuroscience 34, no. 1 (July 21, 2011): 185–204. http://dx.doi.org/10.1146/annurev-neuro-061010-113613.

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4

Harrison, Paul J., Wendy H. Wighton-Benn, Josephine M. Heffernan, Maurice W. Sanders, and R. Carl A. Pearson. "Amyloid Precursor Protein mRNAs in Alzheimer's Disease." Neurodegeneration 5, no. 4 (December 1996): 409–15. http://dx.doi.org/10.1006/neur.1996.0055.

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5

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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6

ROSSOR, M. N., S. NEWMAN, R. S. J. FRACKOWIAK, P. LANTOS, and A. M. KENNEDY. "Alzheimer's Disease Families with Amyloid Precursor Protein Mutationsa." Annals of the New York Academy of Sciences 695, no. 1 (September 1993): 198–202. http://dx.doi.org/10.1111/j.1749-6632.1993.tb23052.x.

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7

Ayala-Grosso, Carlos, Gordon Ng, Sophie Roy, and George S. Robertson. "Caspase-cleaved Amyloid Precursor Protein in Alzheimer's Disease." Brain Pathology 12, no. 4 (April 5, 2006): 430–41. http://dx.doi.org/10.1111/j.1750-3639.2002.tb00460.x.

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8

Ahmad, Syed S., Shahzad Khan, Mohammad A. Kamal, and Umam Wasi. "The Structure and Function of α, β and γ-Secretase as Therapeutic Target Enzymes in the Development of Alzheimer’s Disease: A Review." CNS & Neurological Disorders - Drug Targets 18, no. 9 (January 15, 2020): 657–67. http://dx.doi.org/10.2174/1871527318666191011145941.

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: Alzheimer's disease is a progressive neurodegenerative disorder that affects the central nervous system. There are several factors that cause AD, like, intracellular hyperphosphorylated Tau tangles, collection of extracellular Amyloid-β42 and generation of reactive oxygen species due to mitochondrial dysfunction. This review analyses the most active target of AD and both types of AD-like early-onset AD and late-onset AD. BACE1 is a β-secretase involved in the cleavage of amyloid precursor protein and the pathogenesis of Alzheimer's disease. The presenilin proteins play a critical role in the pathogenesis of Alzheimer malady by intervening the intramembranous cleavage of amyloid precursor protein and the generation of amyloid β. The two homologous proteins PS1 and PS2 speak to the reactant subunits of particular γ-secretase edifices that intercede an assortment of cellular processes. Natural products are common molecular platforms in drug development in AD. Many natural products are being tested in various animal model systems for their role as a potential therapeutic target in AD. Presently, there are a few theories clarifying the early mechanisms of AD pathogenesis. Recently, research advancements in the field of nanotechnology, which utilize macromolecular strategies to make drugs in nanoscale measurements, offer nanotechnology-based diagnostic tools and drug carriers which are highly sensitive for effective drug targeting in the treatment of Alzheimer’s disease.

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9

Pluta, Ryszard, Liang Ouyang, Sławomir Januszewski, Yang Li, and Stanisław J. Czuczwar. "Participation of Amyloid and Tau Protein in Post-Ischemic Neurodegeneration of the Hippocampus of a Nature Identical to Alzheimer's Disease." International Journal of Molecular Sciences 22, no. 5 (February 28, 2021): 2460. http://dx.doi.org/10.3390/ijms22052460.

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Recent evidence suggests that amyloid and tau protein are of vital importance in post-ischemic death of CA1 pyramidal neurons of the hippocampus. In this review, we summarize protein alterations associated with Alzheimer's disease and their gene expression (amyloid protein precursor and tau protein) after cerebral ischemia, as well as their roles in post-ischemic hippocampus neurodegeneration. In recent years, multiple studies aimed to elucidate the post-ischemic processes in the development of hippocampus neurodegeneration. Their findings have revealed the dysregulation of genes for amyloid protein precursor, β-secretase, presenilin 1 and 2, tau protein, autophagy, mitophagy, and apoptosis identical in nature to Alzheimer's disease. Herein, we present the latest data showing that amyloid and tau protein associated with Alzheimer's disease and their genes play a key role in post-ischemic neurodegeneration of the hippocampus with subsequent development of dementia. Therefore, understanding the underlying process for the development of post-ischemic CA1 area neurodegeneration in the hippocampus in conjunction with Alzheimer's disease-related proteins and genes will provide the most important therapeutic development goals to date.

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10

Parent, Angèle T., and Gopal Thinakaran. "Modeling Presenilin-Dependent Familial Alzheimer's Disease: Emphasis on Presenilin Substrate-Mediated Signaling and Synaptic Function." International Journal of Alzheimer's Disease 2010 (2010): 1–11. http://dx.doi.org/10.4061/2010/825918.

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Mutations inPSENgenes, which encode presenilin proteins, cause familial early-onset Alzheimer's disease (AD). Transgenic mouse models based on coexpression of familial AD-associated presenilin and amyloid precursor protein variants successfully mimic characteristic pathological features of AD, including plaque formation, synaptic dysfunction, and loss of memory. Presenilins function as the catalytic subunit ofγ-secretase, the enzyme that catalyzes intramembraneous proteolysis of amyloid precursor protein to releaseβ-amyloid peptides. Familial AD-associated mutations in presenilins alter the site ofγ-secretase cleavage in a manner that increases the generation of longer and highly fibrillogenicβ-amyloid peptides. In addition to amyloid precursor protein,γ-secretase catalyzes intramembrane proteolysis of many other substrates known to be important for synaptic function. This paper focuses on how various animal models have enabled us to elucidate the physiological importance of diverseγ-secretase substrates, including amyloid precursor protein and discusses their roles in the context of cellular signaling and synaptic function.

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11

KINBARA, KAYOKO, HIROSHI KITAGAKI, TADATOSHI KINOUCHI, MASAMICHI OKANO, HIROYUKI SORIMACHI, SHOICHI ISHIURA, and KOICHI SUZUKI. "Processing and Secretion of Alzheimer's Disease Amyloid Precursor Protein." Tohoku Journal of Experimental Medicine 174, no. 3 (1994): 209–16. http://dx.doi.org/10.1620/tjem.174.209.

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12

Preece, Paul, David J. Virley, Moheb Costandi, Robert Coombes, Stephen J. Moss, Anne W. Mudge, Elena Jazin, and Nigel J. Cairns. "Amyloid precursor protein mRNA levels in Alzheimer's disease brain." Molecular Brain Research 122, no. 1 (March 2004): 1–9. http://dx.doi.org/10.1016/j.molbrainres.2003.08.022.

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13

TCW, Julia, and Alison M. Goate. "Genetics of β-Amyloid Precursor Protein in Alzheimer's Disease." Cold Spring Harbor Perspectives in Medicine 7, no. 6 (December 21, 2016): a024539. http://dx.doi.org/10.1101/cshperspect.a024539.

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14

Hendriks, Lydia, and Christine Broeckhoven. "The betaA4 Amyloid Precursor Protein Gene and Alzheimer's Disease." European Journal of Biochemistry 237, no. 1 (April 1996): 6–15. http://dx.doi.org/10.1111/j.1432-1033.1996.0006n.x.

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15

Lopez Sanchez, M. Isabel G., Peter Wijngaarden, and Ian A. Trounce. "Amyloid precursor protein‐mediated mitochondrial regulation and Alzheimer's disease." British Journal of Pharmacology 176, no. 18 (December 18, 2018): 3464–74. http://dx.doi.org/10.1111/bph.14554.

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16

Thomas, Linda D. "Neuropsychological correlates of amyloid precursor protein in Alzheimer's disease." International Journal of Nursing Practice 2, no. 1 (March 1996): 29–32. http://dx.doi.org/10.1111/j.1440-172x.1996.tb00018.x.

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17

Anandatheerthavarada, Hindupur K., and Latha Devi. "Amyloid Precursor Protein and Mitochondrial Dysfunction in Alzheimer's Disease." Neuroscientist 13, no. 6 (October 2, 2007): 626–38. http://dx.doi.org/10.1177/1073858407303536.

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18

Ganjei, J. K. "Targeting amyloid precursor protein secretases: Alzheimer's disease and beyond." Drug News & Perspectives 23, no. 9 (2010): 573. http://dx.doi.org/10.1358/dnp.2010.23.9.1507297.

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19

MILEUSNIC, RADMILA, CHRISTINE L. LANCASHIRE, and STEVEN P. R. ROSE. "Amyloid Precursor Protein: From Synaptic Plasticity to Alzheimer's Disease." Annals of the New York Academy of Sciences 1048, no. 1 (June 2005): 149–65. http://dx.doi.org/10.1196/annals.1342.014.

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20

Dewji, Nazneen N., Earl R. Shelton, Mark J. Adler, Hardy W. Chan, J. E. Seegmiller, and Crystal Coronel. "Processing of Alzheimer's disease-associated β-amyloid precursor protein." Journal of Molecular Neuroscience 2, no. 1 (March 1990): 19–27. http://dx.doi.org/10.1007/bf02896922.

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21

Hooper, N. M., and A. J. Turner. "Protein processing mechanisms: from angiotensin-converting enzyme to Alzheimer's disease." Biochemical Society Transactions 28, no. 4 (August 1, 2000): 441–46. http://dx.doi.org/10.1042/bst0280441.

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Angiotensin-converting enzyme (ACE) and the Alzheimer's disease amyloid precursor protein are two examples of membrane-bound proteins that are released in a soluble form by a post-trans-lational proteolytic cleavage event involving a secretase. Site-specific antibodies and matrix-assisted laser desorption ionization-time-of-flight (‘MALDI-TOF’) MS have been used to map the secretase cleavage site in somatic ACE to Arg-1203/Ser-1204, 24 residues proximal to the membrane-anchoring domain. Trypsin, which can solubilize ACE from the membrane, cleaves the protein at the same site. The use of structurally related hydroxamic acid-based zinc metalloproteinase inhibitors indicate that tumour necrosis factor-α convertase, a member of the ADAMs (‘a disintegrin and metalloproteinase’) family of proteins, is not involved in the proteolytic release of ACE, or in the constitutive or regulated α-secretase release of the amyloid precursor protein from a human neuronal cell line.

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22

Kedia, Shekhar, Pratyush Ramakrishna, Pallavi Rao Netrakanti, Mini Jose, Jean-Baptiste Sibarita, Suhita Nadkarni, and Deepak Nair. "Real-time nanoscale organization of amyloid precursor protein." Nanoscale 12, no. 15 (2020): 8200–8215. http://dx.doi.org/10.1039/d0nr00052c.

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Regulatory nanodomains modulated by lateral diffusion control transient equilibrium between pools of APP within an excitatory synapse. Molecular fingerprints of these nanodomains are altered in variants of APP implicated in Alzheimer's Disease.

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23

Selkoe, Dennis J. "Amyloid β protein precursor and the pathogenesis of Alzheimer's disease." Cell 58, no. 4 (August 1989): 611–12. http://dx.doi.org/10.1016/0092-8674(89)90093-7.

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24

Selkoe, D. "Deciphering Alzheimer's disease: the amyloid precursor protein yields new clues." Science 248, no. 4959 (June 1, 1990): 1058–60. http://dx.doi.org/10.1126/science.2111582.

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25

Ishiura, Shoichi. "Proteolytic Cleavage of the Alzheimer's Disease Amyloid A4 Precursor Protein." Journal of Neurochemistry 56, no. 2 (February 1991): 363–69. http://dx.doi.org/10.1111/j.1471-4159.1991.tb08160.x.

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26

Bush, Ashley I., Scott Whyte, Linda D. Thomas, Timothy G. Williamson, Cees J. Van Tiggelen, Jon Currie, David H. Small, et al. "An abnormality of plasma amyloid protein precursor in Alzheimer's disease." Annals of Neurology 32, no. 1 (July 1992): 57–65. http://dx.doi.org/10.1002/ana.410320110.

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27

Fombonne, Joanna, Shahrooz Rabizadeh, Surita Banwait, Patrick Mehlen, and Dale E. Bredesen. "Selective vulnerability in Alzheimer's disease: Amyloid precursor protein and p75NTRinteraction." Annals of Neurology 65, no. 3 (March 2009): 294–303. http://dx.doi.org/10.1002/ana.21578.

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28

Greig, Nigel H., Kumar Sambamurti, Debomoy K. Lahiri, and Robert E. Becker. "Amyloid-β precursor protein synthesis inhibitors for Alzheimer's disease treatment." Annals of Neurology 76, no. 4 (September 5, 2014): 629–30. http://dx.doi.org/10.1002/ana.24254.

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29

Younkin, Steven G. "Processing of the Alzheimer's Disease ΒZA4 Amyloid Protein Precursor (APP)." Brain Pathology 1, no. 4 (July 1991): 253–62. http://dx.doi.org/10.1111/j.1750-3639.1991.tb00668.x.

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30

Palmert, M., T. Golde, M. Cohen, D. Kovacs, R. Tanzi, J. Gusella, M. Usiak, L. Younkin, and S. Younkin. "Amyloid protein precursor messenger RNAs: differential expression in Alzheimer's disease." Science 241, no. 4869 (August 26, 1988): 1080–84. http://dx.doi.org/10.1126/science.2457949.

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31

Bush, Ashley I., Konrad Beyreuther, and Colin L. Masters. "β A4 amyloid protein and its precursor in Alzheimer's disease." Pharmacology & Therapeutics 56, no. 1 (January 1992): 97–117. http://dx.doi.org/10.1016/0163-7258(92)90039-3.

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32

Gao, Chen, Gabriela Crespi, David Ascher, Luke Miles, and Michael Parker. "P4-291: Structural studies of Alzheimer's disease amyloid precursor protein." Alzheimer's & Dementia 8, no. 4S_Part_21 (July 2012): S760. http://dx.doi.org/10.1016/j.jalz.2013.08.072.

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33

Van Duijn, CorneliaM, Lydia Hendriks, Marc Cruts, JohnA Hardy, Albert Hofman, and Christine Van Broeckhoven. "Amyloid precursor protein gene mutation in early-onset Alzheimer's disease." Lancet 337, no. 8747 (April 1991): 978. http://dx.doi.org/10.1016/0140-6736(91)91611-w.

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34

Ashall, Frank, and Alison M. Goate. "Role of the β-amyloid precursor protein in Alzheimer's disease." Trends in Biochemical Sciences 19, no. 1 (January 1994): 42–46. http://dx.doi.org/10.1016/0968-0004(94)90173-2.

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35

Whyte, Scott, Ashley I. Bush, Jon Currie, Timothy G. Williamson, Cees J. Van Tiggelen, David H. Small, Robert D. Moir, et al. "The abnormality of plasma amyloid protein precursor in Alzheimer's disease." Neurobiology of Aging 13 (January 1992): S29. http://dx.doi.org/10.1016/0197-4580(92)90241-o.

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36

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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37

Sakaki, Yoshiyuki. "Structure and expression of Alzheimer's disease amyloid protein precursor gene." Neuroscience Research Supplements 17 (January 1992): 20. http://dx.doi.org/10.1016/0921-8696(92)90672-n.

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38

Bellingham, Shayne A., Debomoy K. Lahiri, Bryan Maloney, Sharon La Fontaine, Gerd Multhaup, and James Camakaris. "Copper Depletion Down-regulates Expression of the Alzheimer's Disease Amyloid-β Precursor Protein Gene." Journal of Biological Chemistry 279, no. 19 (February 25, 2004): 20378–86. http://dx.doi.org/10.1074/jbc.m400805200.

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Alzheimer's disease is characterized by the accumulation of amyloid-β peptide, which is cleaved from the amyloid-β precursor protein (APP). Reduction in levels of the potentially toxic amyloid-β has emerged as one of the most important therapeutic goals in Alzheimer's disease. Key targets for this goal are factors that affect the regulation of theAPPgene. Recentin vivoandin vitrostudies have illustrated the importance of copper in Alzheimer's disease neuropathogenesis and suggested a role for APP and amyloid-β in copper homeostasis. We hypothesized that metals and in particular copper might alterAPPgene expression. To test the hypothesis, we utilized human fibroblasts overexpressing the Menkes protein (MNK), a major mammalian copper efflux protein.MNKdeletion fibroblasts have high intracellular copper, whereas MNK overexpressing fibroblasts have severely depleted intracellular copper. We demonstrate that copper depletion significantly reduced APP protein levels and down-regulatedAPPgene expression. Furthermore,APPpromoter deletion constructs identified the copper-regulatory region between -490 and +104 of theAPPgene promoter in both basal MNK overexpressing cells and in copper-chelatedMNKdeletion cells. Overall these data support the hypothesis that copper can regulateAPPexpression and further support a role for APP to function in copper homeostasis. Copper-regulatedAPPexpression may also provide a potential therapeutic target in Alzheimer's disease.

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39

Wang, Xiaonan, Xihai Li, Jie Yang, Ming Yu, and Jinmei Wu. "Amyloid precursor protein in peripheral granulocytes as a potential biomarker for Alzheimers disease." Bangladesh Journal of Pharmacology 11 (March 5, 2016): S92—S97. http://dx.doi.org/10.3329/bjp.v11is1.26412.

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The aim of this study was to assess the potential of amyloid precursor protein in peripheral granulocytes as a diagnostic biomarker for early detection of Alzheimers disease. Immunohistochemistry and flow cytometry were used to evaluate amyloid precursor protein expression levels and subcellular localization in Alzheimers disease. Much higher amyloid precursor protein expression was observed in some leukocytes from Alzheimers disease patients, compared with samples from non-Alzheimers disease controls. In addition, flow cytometry data indicated significantly higher amyloid precursor protein expression in granulocytes from Alzheimers disease patients compared with control values. No statistically significant differences in amyloid precursor protein expression were obtained in lymphocytes or monocytes between the patient groups. In conclusion, amyloid precursor protein expression level in peripheral blood granulocyte is a potential biomarker for early diagnosis of Alzheimers disease.

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40

Parsons, R. B., and B. M. Austen. "Protein–protein interactions in the assembly and subcellular trafficking of the BACE (β-site amyloid precursor protein-cleaving enzyme) complex of Alzheimer's disease." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 974–79. http://dx.doi.org/10.1042/bst0350974.

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The correct assembly of the BACE (β-site amyloid precursor protein-cleaving enzyme or β-secretase) complex and its subsequent trafficking to cellular compartments where it associates with the APP (amyloid precursor protein) is essential for the production of Aβ (amyloid β-peptide), the protein whose aggregation into senile plaques is thought to be responsible for the pathogenesis of AD (Alzheimer's disease). These processes rely upon both transient and permanent BACE–protein interactions. This review will discuss what is currently known about these BACE–protein interactions and how they may reveal novel therapeutic targets for the treatment of AD.

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41

Evin, Genevieve, Konrad Beyreuther, and Colin L. Masters. "Alzheimer's disease amyloid precursor protein (ApPP): proteolytic processing, secretases and βA4 amyloid production." Amyloid 1, no. 4 (January 1994): 263–80. http://dx.doi.org/10.3109/13506129409146118.

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42

Lahiri, D. K., M. R. Farlow, N. Hintz, T. Utsuki, and N. H. Greig. "Cholinesterase inhibitors, β-amyloid precursor protein and amyloid β-peptides in Alzheimer's disease." Acta Neurologica Scandinavica 102 (December 2000): 60–67. http://dx.doi.org/10.1034/j.1600-0404.2000.00309.x.

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43

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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44

Allsop, David, and Jennifer Mayes. "Amyloid β-peptide and Alzheimer's disease." Essays in Biochemistry 56 (August 18, 2014): 99–110. http://dx.doi.org/10.1042/bse0560099.

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One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.

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45

Salloway, Stephen. "Introduction: The Prevalence of Alzheimer's Disease — A Growing Crisis." CNS Spectrums 13, S3 (March 2008): 3. http://dx.doi.org/10.1017/s109285290001717x.

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In 1906, the German physician Alois Alzheimer provided the first description of the “serious and peculiar disease” of mental deterioration that would later on take his name. Alzheimer described the classic pathology of neuritic plaques and neurofibrillary tangles in an affected patient. Since that time, understanding of Alzheimer's disease (AD) has progressed substantially, although the ability to influence disease progression has not progressed as rapidly. It is likely that over the next decade these advances will lead to earlier diagnosis and development of disease-modifying treatments for AD.It is known that two variants of AD exist: a rare hereditary form and a more prevalent sporadic form. As with many neurodegenerative diseases, early clues to the pathology of AD came from the inherited form of the disease. Hereditary links include mutations of the amyloid precursor protein (APP) and the presenilins, both of which are integrally involved in the cascade of events that leads to the deposition of the 42-amino-acid amyloid β protein and the eventual cell death responsible for AD.

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46

Badhwar, AmanPreet, Rebecca Brown, Danica B. Stanimirovic, Arsalan S. Haqqani, and Edith Hamel. "Proteomic differences in brain vessels of Alzheimer’s disease mice: Normalization by PPARγ agonist pioglitazone." Journal of Cerebral Blood Flow & Metabolism 37, no. 3 (July 20, 2016): 1120–36. http://dx.doi.org/10.1177/0271678x16655172.

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Cerebrovascular insufficiency appears years prior to clinical symptoms in Alzheimer’s disease. The soluble, highly toxic amyloid-β species, generated from the amyloidogenic processing of amyloid precursor protein, are known instigators of the chronic cerebrovascular insufficiency observed in both Alzheimer’s disease patients and transgenic mouse models. We have previously demonstrated that pioglitazone potently reverses cerebrovascular impairments in a mouse model of Alzheimer’s disease overexpressing amyloid-β. In this study, we sought to characterize the effects of amyloid-β overproduction on the cerebrovascular proteome; determine how pioglitazone treatment affected the altered proteome; and analyze the relationship between normalized protein levels and recovery of cerebrovascular function. Three-month-old wildtype and amyloid precursor protein mice were treated with pioglitazone- (20 mg/kg/day, 14 weeks) or control-diet. Cerebral arteries were surgically isolated, and extracted proteins analyzed by gel-free and gel-based mass spectrometry. 193 cerebrovascular proteins were abnormally expressed in amyloid precursor protein mice. Pioglitazone treatment rescued a third of these proteins, mainly those associated with oxidative stress, promotion of cerebrovascular vasocontractile tone, and vascular compliance. Our results demonstrate that amyloid-β overproduction perturbs the cerebrovascular proteome. Recovery of cerebrovascular function with pioglitazone is associated with normalized levels of key proteins in brain vessel function, suggesting that pioglitazone-responsive cerebrovascular proteins could be early biomarkers of Alzheimer’s disease.

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47

Chen, Qi, Hideo Kimura, and David Schubert. "A novel mechanism for the regulation of amyloid precursor protein metabolism." Journal of Cell Biology 158, no. 1 (July 1, 2002): 79–89. http://dx.doi.org/10.1083/jcb.200110151.

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Modifier of cell adhesion protein (MOCA; previously called presenilin [PS] binding protein) is a DOCK180-related molecule, which interacts with PS1 and PS2, is localized to brain areas involved in Alzheimer's disease (AD) pathology, and is lost from the soluble fraction of sporadic Alzheimer's disease (AD) brains. Because PS1 has been associated with γ-secretase activity, MOCA may be involved in the regulation of β-amyloid precursor protein (APP) processing. Here we show that the expression of MOCA decreases both APP and amyloid β-peptide secretion and lowers the rate of cell-substratum adhesion. In contrast, MOCA does not lower the secretion of amyloid precursor-like protein (APLP) or several additional type 1 membrane proteins. The phenotypic changes caused by MOCA are due to an acceleration in the rate of intracellular APP degradation. The effect of MOCA expression on the secretion of APP and cellular adhesion is reversed by proteasome inhibitors, suggesting that MOCA directs nascent APP to proteasomes for destruction. It is concluded that MOCA plays a major role in APP metabolism and that the effect of MOCA on APP secretion and cell adhesion is a downstream consequence of MOCA-directed APP catabolism. This is a new mechanism by which the expression of APP is regulated.

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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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Abstract:

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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Jin, Jae-Kwang, Bong-Hyun Ahn, Yeo-Jung Na, Jae-Il Kim, Yong-Sun Kim, Eun-Kyoung Choi, Young-Gyu Ko, Kwang Chul Chung, Piotr B. Kozlowski, and Do Sik Min. "Phospholipase D1 is associated with amyloid precursor protein in Alzheimer's disease." Neurobiology of Aging 28, no. 7 (July 2007): 1015–27. http://dx.doi.org/10.1016/j.neurobiolaging.2006.05.022.

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Tang, Kun, Linda S. Hynan, Fred Baskin, and Roger N. Rosenberg. "Platelet amyloid precursor protein processing: A bio-marker for Alzheimer's disease." Journal of the Neurological Sciences 240, no. 1-2 (January 2006): 53–58. http://dx.doi.org/10.1016/j.jns.2005.09.002.

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