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56 records – page 1 of 6.

Aberrant iNOS signaling is under genetic control in rodent liver cancer and potentially prognostic for the human disease.

https://arctichealth.org/en/permalink/ahliterature92898
Source
Carcinogenesis. 2008 Aug;29(8):1639-47
Publication Type
Article
Date
Aug-2008
Author
Calvisi Diego F
Pinna Federico
Ladu Sara
Pellegrino Rossella
Muroni Maria R
Simile Maria M
Frau Maddalena
Tomasi Maria L
De Miglio Maria R
Seddaiu Maria A
Daino Lucia
Sanna Valeria
Feo Francesco
Pascale Rosa M
Author Affiliation
Department of Biomedical Sciences, Division of Experimental Pathology and Oncology, University of Sassari, 07100 Sassari, Italy.
Source
Carcinogenesis. 2008 Aug;29(8):1639-47
Date
Aug-2008
Language
English
Publication Type
Article
Keywords
Animals
Carcinoma, Hepatocellular - enzymology - epidemiology - genetics - pathology
Cell Line, Tumor
Genetic Predisposition to Disease
Humans
Incidence
Liver Neoplasms - enzymology - epidemiology - genetics - pathology
Male
Mice
Mice, Transgenic
Nitric Oxide Synthase Type II - genetics
Prognosis
Rats
Rats, Inbred BN
Rats, Inbred F344
Signal Transduction - physiology
Abstract
Mounting evidence underlines the role of inducible nitric oxide synthase (iNOS) in hepatocellular carcinoma (HCC) development, but its functional interactions with pathways involved in HCC progression remain uninvestigated. Here, we analyzed in preneoplastic and neoplastic livers from Fisher 344 and Brown Norway rats, possessing different genetic predisposition to HCC, in transforming growth factor-alpha (TGF-alpha) and c-Myc-TGF-alpha transgenic mice, characterized by different susceptibility to HCC, and in human HCC: (i) iNOS function and interactions with nuclear factor-kB (NF-kB) and Ha-RAS/extracellular signal-regulated kinase (ERK) during hepatocarcinogenesis; (ii) influence of genetic predisposition to liver cancer on these pathways and role of these cascades in determining a susceptible or resistant phenotype and (iii) iNOS prognostic value in human HCC. We found progressive iNos induction in rat and mouse liver lesions, always at higher levels in the most aggressive models represented by HCC of rats genetically susceptible to hepatocarcinogenesis and c-Myc-TGF-alpha transgenic mice. iNOS, inhibitor of kB kinase/NF-kB and RAS/ERK upregulation was significantly higher in HCC with poorer prognosis (as defined by patients' survival length) and positively correlated with tumor proliferation, genomic instability and microvascularization and negatively with apoptosis. Suppression of iNOS signaling by aminoguanidine led to decreased HCC growth and NF-kB and RAS/ERK expression and increased apoptosis both in vivo and in vitro. Conversely, block of NF-kB signaling by sulfasalazine or short interfering RNA (siRNA) or ERK signaling by UO126 caused iNOS downregulation in HCC cell lines. These findings indicate that iNOS cross talk with NF-kB and Ha-RAS/ERK cascades influences HCC growth and prognosis, suggesting that key component of iNOS signaling could represent important therapeutic targets for human HCC.
PubMed ID
18579559 View in PubMed
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Abeta oligomer-mediated long-term potentiation impairment involves protein phosphatase 1-dependent mechanisms.

https://arctichealth.org/en/permalink/ahliterature162439
Source
J Neurosci. 2007 Jul 18;27(29):7648-53
Publication Type
Article
Date
Jul-18-2007
Author
Marlen Knobloch
Mélissa Farinelli
Uwe Konietzko
Roger M Nitsch
Isabelle M Mansuy
Author Affiliation
Division of Psychiatry Research, University of Zurich, 8008 Zurich, Switzerland.
Source
J Neurosci. 2007 Jul 18;27(29):7648-53
Date
Jul-18-2007
Language
English
Publication Type
Article
Keywords
Age Factors
Amyloid Precursor Protein Secretases - genetics
Amyloid beta-Peptides - chemistry - metabolism - ultrastructure
Analysis of Variance
Animals
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calcium-Calmodulin-Dependent Protein Kinases - genetics
Dose-Response Relationship, Radiation
Electric Stimulation - methods
Excitatory Postsynaptic Potentials - drug effects - physiology
Gene Expression Regulation - genetics
Hippocampus - cytology
Humans
Long-Term Potentiation - genetics - physiology - radiation effects
Mice
Mice, Transgenic
Microscopy, Electron, Transmission - methods
Neurons - drug effects - physiology
Patch-Clamp Techniques
Phosphoprotein Phosphatases - physiology
Presenilin-1 - genetics
Protein Phosphatase 1
Reverse Transcriptase Polymerase Chain Reaction - methods
Abstract
Amyloid beta (Abeta) oligomers are derived from proteolytic cleavage of amyloid precursor protein (APP) and can impair memory and hippocampal long-term potentiation (LTP) in vivo and in vitro. They are recognized as the primary neurotoxic agents in Alzheimer's disease. The mechanisms underlying such toxicity on synaptic functions are complex and not fully understood. Here, we provide the first evidence that these mechanisms involve protein phosphatase 1 (PP1). Using a novel transgenic mouse model expressing human APP with the Swedish and Arctic mutations that render Abeta more prone to form oligomers (arcAbeta mice), we show that the LTP impairment induced by Abeta oligomers can be fully reversed by PP1 inhibition in vitro. We further demonstrate that the genetic inhibition of endogenous PP1 in vivo confers resistance to Abeta oligomer-mediated toxicity and preserves LTP. Overall, these results reveal that PP1 is a key player in the mechanisms of AD pathology.
PubMed ID
17634359 View in PubMed
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Abnormal adherence junctions in the heart and reduced angiogenesis in transgenic mice overexpressing mutant type XIII collagen.

https://arctichealth.org/en/permalink/ahliterature53860
Source
EMBO J. 2001 Sep 17;20(18):5153-64
Publication Type
Article
Date
Sep-17-2001
Author
M. Sund
R. Ylönen
A. Tuomisto
R. Sormunen
J. Tahkola
A P Kvist
S. Kontusaari
H. Autio-Harmainen
T. Pihlajaniemi
Author Affiliation
Collagen Research Unit, Biocenter Oulu, Department of Medical Biochemistry, University of Oulu, PL 5000, 90014 Oulu, Finland.
Source
EMBO J. 2001 Sep 17;20(18):5153-64
Date
Sep-17-2001
Language
English
Publication Type
Article
Keywords
Adherens Junctions - ultrastructure
Animals
Collagen - genetics - metabolism - physiology
Embryonic and Fetal Development
Fetus - abnormalities - blood supply
Heart - embryology
Heart Defects, Congenital - pathology
Mice
Mice, Transgenic
Mutation
Myocardium - ultrastructure
Neovascularization, Physiologic
Phenotype
Placenta - abnormalities - blood supply
RNA, Messenger - biosynthesis
Research Support, Non-U.S. Gov't
Survival Analysis
Abstract
Type XIII collagen is a type II transmembrane protein found at sites of cell adhesion. Transgenic mouse lines were generated by microinjection of a DNA construct directing the synthesis of truncated alpha1(XIII) chains. Shortened alpha 1(XIII) chains were synthesized by fibroblasts from mutant mice, and the lack of intracellular accumulation in immunofluorescent staining of tissues suggested that the mutant molecules were expressed on the cell surface. Transgene expression led to fetal lethality in offspring from heterozygous mating with two distinct phenotypes. The early phenotype fetuses were aborted by day 10.5 of development due to a lack of fusion of the chorionic and allantoic membranes. The late phenotype fetuses were aborted by day 13.5 of development and displayed a weak heartbeat, defects of the adherence junctions in the heart with detachment of myofilaments and abnormal staining for the adherence junction component cadherin. Decreased microvessel formation was observed in certain regions of the fetus and the placenta. These results indicate that type XIII collagen has an important role in certain adhesive interactions that are necessary for normal development.
PubMed ID
11566879 View in PubMed
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Abnormal ornithine decarboxylase activity in transgenic mice increases tumor formation and infertility.

https://arctichealth.org/en/permalink/ahliterature19846
Source
Int J Biochem Cell Biol. 2001 May;33(5):507-20
Publication Type
Article
Date
May-2001
Author
P T Kilpeläinen
J. Saarimies
S I Kontusaari
M J Järvinen
A P Soler
M J Kallioinen
O A Hietala
Author Affiliation
Department of Biochemistry, University of Oulu, FIN-90014, Oulu, Finland.
Source
Int J Biochem Cell Biol. 2001 May;33(5):507-20
Date
May-2001
Language
English
Publication Type
Article
Keywords
Animals
Female
Genitalia, Male - anatomy & histology - enzymology
Heterozygote
Infertility - etiology
Male
Mice
Mice, Transgenic
Neoplasms - enzymology - etiology
Ornithine Decarboxylase - genetics - metabolism
Promoter Regions (Genetics)
Research Support, Non-U.S. Gov't
Abstract
A transgenic mouse line carrying ornithine decarboxylase cDNA as the transgene under the control of a mouse mammary tumor virus long terminal repeat (MMTV LTR) promoter was generated in order to study whether ornithine decarboxylase transgene expression will have any physiological or pathological effect during the entire life of a transgenic mouse. The high frequency of infertile animals and the loss of pups made the breeding of homozygous mice unsuccessful. However, a colony of heterozygous transgenic mice was followed for 2 years. In adult heterozygous transgenic mice, ornithine decarboxylase activity was significantly increased in the testis, seminal vesicle and preputial gland when compared to non-transgenic controls. In contrast, ornithine decarboxylase activity was decreased in the kidney and prostate of transgenic mice. No significant changes in ornithine decarboxylase activity were found in the ovary and mammary gland and only moderate changes in ornithine decarboxylase activity were detected in the heart, brain, pancreas and lung. The most common abnormalities found in adult animals (12 males and 20 females) of the transgenic line were inflammatory processes, including pancreatitis, hepatitis, sialoadenitis and pyelonephritis. Spontaneous tumors were observed in eight animals, including two benign tumors (one dermatofibroma, one liver hemangioma) and six malignant tumors (one lymphoma, one intestinal and three mammary adenocarcinomas and one adenocarcinoma in the lung). No significant pathological changes were found in 17 nontransgenic controls.
PubMed ID
11331206 View in PubMed
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Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation.

https://arctichealth.org/en/permalink/ahliterature177782
Source
Nat Med. 2004 Nov;10(11):1190-2
Publication Type
Article
Date
Nov-2004
Author
Irene H Cheng
Jorge J Palop
Luke A Esposito
Nga Bien-Ly
Fengrong Yan
Lennart Mucke
Author Affiliation
Gladstone Institute of Neurological Disease, University of California, San Francisco, California 94158, USA.
Source
Nat Med. 2004 Nov;10(11):1190-2
Date
Nov-2004
Language
English
Publication Type
Article
Keywords
Alzheimer Disease - genetics
Amyloid beta-Protein Precursor - genetics - metabolism
Animals
Blotting, Western
Enzyme-Linked Immunosorbent Assay
Hippocampus - metabolism
Humans
Mice
Mice, Inbred C57BL
Mice, Transgenic
Mutation - genetics
Plaque, Amyloid - metabolism
Abstract
The Arctic mutation within the amyloid-beta (Abeta) peptide causes Alzheimer disease. In vitro, Arctic-mutant Abeta forms (proto)fibrils more effectively than wild-type Abeta. We generated transgenic mouse lines expressing Arctic-mutant human amyloid precursor proteins (hAPP). Amyloid plaques formed faster and were more extensive in Arctic mice than in hAPP mice expressing wild-type Abeta, even though Arctic mice had lower Abeta(1-42/1-40) ratios. Thus, the Arctic mutation is highly amyloidogenic in vivo.
PubMed ID
15502844 View in PubMed
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Altered behavior and alcohol tolerance in transgenic mice lacking MAO A: a comparison with effects of MAO A inhibitor clorgyline.

https://arctichealth.org/en/permalink/ahliterature10300
Source
Pharmacol Biochem Behav. 2000 Dec;67(4):719-27
Publication Type
Article
Date
Dec-2000
Author
N K Popova
G B Vishnivetskaya
E A Ivanova
J A Skrinskaya
I. Seif
Author Affiliation
Institute of Cytology and Genetics, Siberian Branch of Russian Academy of Sciences, Lavrentieva 10, 630090 Novosibirsk 90, Russia. npopova@bionet.nsc.ru
Source
Pharmacol Biochem Behav. 2000 Dec;67(4):719-27
Date
Dec-2000
Language
English
Publication Type
Article
Keywords
Alcohol Drinking - genetics
Animals
Anxiety - genetics
Central Nervous System Depressants - pharmacology
Clorgyline - pharmacology
Drug Tolerance - genetics
Ethanol - pharmacology
Exploratory Behavior - drug effects - physiology
Hypothermia - chemically induced - genetics
Male
Mice
Mice, Inbred C3H
Mice, Transgenic
Monoamine Oxidase - deficiency - genetics
Monoamine Oxidase Inhibitors - pharmacology
Motor Activity - drug effects - genetics
Research Support, Non-U.S. Gov't
Sleep - drug effects - genetics
Startle Reaction - drug effects - genetics
Abstract
The influence of deficiency of monoamine oxidase A (MAO A) gene and the lack of enzyme MAO A on the behavior of transgenic mouse strain (Tg8) was studied. It was shown that MAO-A-lacking mice differed from mice of the wild-type strain C3H/HeJ (C3H) by an attenuated acoustic startle response, prepulse inhibition (PPI) was unchanged. In Tg 8 mice, the exploratory nose-poking in the holeboard test as well as exploratory line crossing in the "light-dark" test were decreased. No effect of MAO A deficiency on locomotor activity was found. No alcohol preference or difference between Tg8 and C3H in ethanol consumption in the free-choice test has been found, although an increase in alcohol tolerance has been demonstrated. Ethanol-induced (0.3 g/100 g ip) sleep latency was longer, duration of sleep was shorter and ethanol hypothermia was reduced in MAO-A-lacking mice. Comparison of effects of MAO A knockout with those of irreversible MAO A inhibitor clorgyline (5 and 10 mg/kg ip) on C3H mice showed a similar reducing effect on ethanol-induced sleep, but potentiated ethanol-induced hypothermia. Clorgyline administration provoked a tendency to decrease of exploratory activity in the nose-poking test and decreased the frequency of exploratory rearings in the light-dark test. Clorgyline (5 and 10 mg/kg) did not affect the acoustic startle response, but a dose of 5 mg/kg diminished PPI. Therefore, Tg8 mice exhibited a decreased startle response and exploratory activity and an increased tolerance to ethanol. A similar increase in tolerance to ethanol-induced sleep and a tendency to decrease exploratory behavior were displayed by clorgyline. Other effects on behavior were different, suggesting the influence of long-lasting action of MAO A knockout and the involvement of a compensatory mechanism in Tg8 mice.
PubMed ID
11166062 View in PubMed
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Amyloid-beta protofibril levels correlate with spatial learning in Arctic Alzheimer's disease transgenic mice.

https://arctichealth.org/en/permalink/ahliterature90033
Source
FEBS J. 2009 Feb;276(4):995-1006
Publication Type
Article
Date
Feb-2009
Author
Lord Anna
Englund Hillevi
Söderberg Linda
Tucker Stina
Clausen Fredrik
Hillered Lars
Gordon Marcia
Morgan Dave
Lannfelt Lars
Pettersson Frida E
Nilsson Lars N G
Author Affiliation
Department of Public Health and Caring Sciences/Molecular Geriatrics, Uppsala University, Sweden.
Source
FEBS J. 2009 Feb;276(4):995-1006
Date
Feb-2009
Language
English
Publication Type
Article
Keywords
Aging - pathology
Alzheimer Disease - genetics - metabolism - pathology
Amyloid beta-Protein - cerebrospinal fluid - genetics - metabolism
Animals
Mice
Mice, Transgenic
Mutation
Senile Plaques - pathology
Abstract
Oligomeric assemblies of amyloid-beta (Abeta) are suggested to be central in the pathogenesis of Alzheimer's disease because levels of soluble Abeta correlate much better with the extent of cognitive dysfunctions than do senile plaque counts. Moreover, such Abeta species have been shown to be neurotoxic, to interfere with learned behavior and to inhibit the maintenance of hippocampal long-term potentiation. The tg-ArcSwe model (i.e. transgenic mice with the Arctic and Swedish Alzheimer mutations) expresses elevated levels of Abeta protofibrils in the brain, making tg-ArcSwe a highly suitable model for investigating the pathogenic role of these Abeta assemblies. In the present study, we estimated Abeta protofibril levels in the brain and cerebrospinal fluid of tg-ArcSwe mice, and also assessed their role with respect to cognitive functions. Protofibril levels, specifically measured with a sandwich ELISA, were found to be elevated in young tg-ArcSwe mice compared to several transgenic models lacking the Arctic mutation. In aged tg-ArcSwe mice with considerable plaque deposition, Abeta protofibrils were approximately 50% higher than in younger mice, whereas levels of total Abeta were exponentially increased. Young tg-ArcSwe mice showed deficits in spatial learning, and individual performances in the Morris water maze were correlated inversely with levels of Abeta protofibrils, but not with total Abeta levels. We conclude that Abeta protofibrils accumulate in an age-dependent manner in tg-ArcSwe mice, although to a far lesser extent than total Abeta. Our findings suggest that increased levels of Abeta protofibrils could result in spatial learning impairment.
PubMed ID
19215301 View in PubMed
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Amyloid neuropathology in the single Arctic APP transgenic model affects interconnected brain regions.

https://arctichealth.org/en/permalink/ahliterature131757
Source
Neurobiol Aging. 2012 Apr;33(4):831.e11-9
Publication Type
Article
Date
Apr-2012
Author
Annica Rönnbäck
Hanna Sagelius
Karin Dillner Bergstedt
Jan Näslund
Gunilla T Westermark
Bengt Winblad
Caroline Graff
Author Affiliation
Department of Neurobiology, Care Sciences and Society, Karolinska Institutet Alzheimer Disease Research Center, Karolinska Institutet, Huddinge, Sweden. annica.ronnback@ki.se
Source
Neurobiol Aging. 2012 Apr;33(4):831.e11-9
Date
Apr-2012
Language
English
Publication Type
Article
Keywords
Age Factors
Alzheimer Disease - genetics - metabolism - pathology
Amyloid beta-Peptides - metabolism
Amyloid beta-Protein Precursor - genetics - metabolism
Analysis of Variance
Animals
Disease Models, Animal
Enzyme-Linked Immunosorbent Assay - methods
Female
Hippocampus - metabolism - pathology - ultrastructure
Humans
Male
Mice
Mice, Transgenic
Microscopy, Immunoelectron
Mutation - genetics
Peptide Fragments - metabolism
Abstract
The Arctic APP mutation (E693G) within the amyloid ß (Aß) domain of amyloid precursor protein (APP) leads to dementia with clinical features similar to Alzheimer's disease (AD), which is believed to be mediated via increased formation of protofibrils. We have generated a transgenic mouse model, TgAPParc, with neuron-specific expression of human amyloid precursor protein with the Arctic mutation (hAPParc), showing mild amyloid pathology with a relatively late onset. Here we performed a detailed analysis of the spatiotemporal progression of neuropathology in homozygous TgAPParc, focusing on intracellular Aß and diffuse Aß aggregates rather than amyloid plaques. We show that the neuropathology in homozygous TgAPParc mice starts with intracellular Aß aggregates, which is followed by diffuse extracellular Aß deposits in subiculum that later expands to brain regions receiving neuronal projections from regions already affected. Together this suggests that the pathology in TgAPParc mice affects interconnected brain regions and may represent a valuable tool to study the spread and progression of neuropathology in Alzheimer's disease.
PubMed ID
21880397 View in PubMed
Less detail

An amyloid-beta protofibril-selective antibody prevents amyloid formation in a mouse model of Alzheimer's disease.

https://arctichealth.org/en/permalink/ahliterature98930
Source
Neurobiol Dis. 2009 Dec;36(3):425-34
Publication Type
Article
Date
Dec-2009
Author
Anna Lord
Astrid Gumucio
Hillevi Englund
Dag Sehlin
Valentina Screpanti Sundquist
Linda Söderberg
Christer Möller
Pär Gellerfors
Lars Lannfelt
Frida Ekholm Pettersson
Lars N G Nilsson
Author Affiliation
Department of Public Health and Caring Sciences/Molecular Geriatrics, Uppsala University, Rudbeck Laboratory, Dag Hammarskjölds väg 20, SE-751 85 Uppsala, Sweden.
Source
Neurobiol Dis. 2009 Dec;36(3):425-34
Date
Dec-2009
Language
English
Publication Type
Article
Keywords
Aging
Alzheimer Disease - metabolism - pathology - therapy
Amyloid - immunology - metabolism
Amyloid beta-Protein - immunology - metabolism - toxicity
Animals
Antibodies, Monoclonal - administration & dosage - immunology - therapeutic use
Brain - immunology - metabolism - pathology
Disease Models, Animal
Humans
Immunization, Passive
Kinetics
Learning
Mice
Mice, Transgenic
Peptide Fragments - immunology - metabolism - toxicity
Protein Multimerization
Senile Plaques - immunology - metabolism - pathology
Space Perception
Abstract
Human genetics link Alzheimer's disease pathogenesis to excessive accumulation of amyloid-beta (Abeta) in brain, but the symptoms do not correlate with senile plaque burden. Since soluble Abeta aggregates can cause synaptic dysfunctions and memory deficits, these species could contribute to neuronal dysfunction and dementia. Here we explored selective targeting of large soluble aggregates, Abeta protofibrils, as a new immunotherapeutic strategy. The highly protofibril-selective monoclonal antibody mAb158 inhibited in vitro fibril formation and protected cells from Abeta protofibril-induced toxicity. When the mAb158 antibody was administered for 4 months to plaque-bearing transgenic mice with both the Arctic and Swedish mutations (tg-ArcSwe), Abeta protofibril levels were lowered while measures of insoluble Abeta were unaffected. In contrast, when treatment began before the appearance of senile plaques, amyloid deposition was prevented and Abeta protofibril levels diminished. Therapeutic intervention with mAb158 was however not proven functionally beneficial, since place learning depended neither on treatment nor transgenicity. Our findings suggest that Abeta protofibrils can be selectively cleared with immunotherapy in an animal model that display highly insoluble Abeta deposits, similar to those of Alzheimer's disease brain.
PubMed ID
19703562 View in PubMed
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APP heterozygosity averts memory deficit in knockin mice expressing the Danish dementia BRI2 mutant.

https://arctichealth.org/en/permalink/ahliterature134422
Source
EMBO J. 2011 Jun 15;30(12):2501-9
Publication Type
Article
Date
Jun-15-2011
Author
Robert Tamayev
Shuji Matsuda
Luca Giliberto
Ottavio Arancio
Luciano D'Adamio
Author Affiliation
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.
Source
EMBO J. 2011 Jun 15;30(12):2501-9
Date
Jun-15-2011
Language
English
Publication Type
Article
Keywords
Alzheimer Disease - genetics
Amyloid beta-Peptides - genetics
Animals
Dementia - genetics
Denmark
Disease Models, Animal
Gene Knock-In Techniques
Heterozygote Detection
Humans
Male
Membrane Proteins - genetics - metabolism
Memory Disorders - genetics - prevention & control
Mice
Mice, Inbred C57BL
Mice, Transgenic
Mutant Chimeric Proteins - genetics
Mutation
Peptide Fragments - genetics
Abstract
An autosomal dominant mutation in the BRI2/ITM2B gene causes familial Danish dementia (FDD). Analysis of FDD(KI) mice, a mouse model of FDD genetically congruous to the human disease since they carry one mutant and one wild-type Bri2/Itm2b allele, has shown that the Danish mutation causes loss of Bri2 protein, synaptic plasticity and memory impairments. BRI2 is a physiological interactor of Aß-precursor protein (APP), a gene associated with Alzheimer disease, which inhibits processing of APP. Here, we show that APP/Bri2 complexes are reduced in synaptic membranes of FDD(KI) mice. Consequently, APP metabolites derived from processing of APP by ß-, a- and ?-secretases are increased in Danish dementia mice. APP haplodeficiency prevents memory and synaptic dysfunctions, consistent with a role for APP metabolites in the pathogenesis of memory and synaptic deficits. This genetic suppression provides compelling evidence that APP and BRI2 functionally interact, and that the neurological effects of the Danish form of BRI2 only occur when sufficient levels of APP are supplied by two alleles. This evidence establishes a pathogenic sameness between familial Danish and Alzheimer's dementias.
Notes
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PubMed ID
21587206 View in PubMed
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56 records – page 1 of 6.