Insulin has multiple antiamyloidogenic effects on human neuronal cells (646 views)
Endocrinology (ISSN: 0013-7227, 1945-7170), 2013 Jan; 154(1): 375-387.
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Paper type: Journal Article,
Impact factor: 4.644, 5-year impact factor: 4.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84871691509&partnerID=40&md5=7b15f53cd9131de65d6c7f40c7b4da94
Keywords: Alpha Secretase, Amyloid Beta Protein[1-40], Amyloid Precursor Protein, Beta Secretase, Glycogen Synthase Kinase 3beta, Insulin, Animal Cell, Article, Cell Fractionation, Controlled Study, Drug Effect, Embryo, Human, Human Cell, Immunofluorescence, In Vitro Study, Kidney Cell, Nerve Cell, Nonhuman, Nucleotide Sequence, Priority Journal, Protein Dephosphorylation, Protein Phosphorylation, Amyloid Beta-Protein Precursor, Amyloid Precursor Protein Secretases, Cell Line, Tumor, Cultured, Insulysin, Neurons, Signal Transduction, Amyloid Precursor Protein Secretases Metabolism, Amyloid Beta-Protein Precursor Metabolism, Glycogen Synthase Kinases Metabolism, Insulin Pharmacology, Insulysin Metabolism, Neurons Drug Effects Metabolism, Phosphorylation Drug Effects, Signal Transduction Drug Effects, Amyloid Beta Protein [1-40],
Affiliations:
*** IBB - CNR ***
Department of Clinical and Molecular Biomedicine, University of Catania, Garibaldi-Nesima Hospital, Via Palermo 636, Catania 95122, Italy
Department of Drug Sciences, University of Catania, National Council of Research (Institute of Biostructures and Bioimages), Catania, 95125, Italy
References:
Not available.
Endocrinology (ISSN: 0013-7227, 1945-7170), 2013 Jan; 154(1): 375-387.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.644, 5-year impact factor: 4.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84871691509&partnerID=40&md5=7b15f53cd9131de65d6c7f40c7b4da94
Keywords: Alpha Secretase, Amyloid Beta Protein[1-40], Amyloid Precursor Protein, Beta Secretase, Glycogen Synthase Kinase 3beta, Insulin, Animal Cell, Article, Cell Fractionation, Controlled Study, Drug Effect, Embryo, Human, Human Cell, Immunofluorescence, In Vitro Study, Kidney Cell, Nerve Cell, Nonhuman, Nucleotide Sequence, Priority Journal, Protein Dephosphorylation, Protein Phosphorylation, Amyloid Beta-Protein Precursor, Amyloid Precursor Protein Secretases, Cell Line, Tumor, Cultured, Insulysin, Neurons, Signal Transduction, Amyloid Precursor Protein Secretases Metabolism, Amyloid Beta-Protein Precursor Metabolism, Glycogen Synthase Kinases Metabolism, Insulin Pharmacology, Insulysin Metabolism, Neurons Drug Effects Metabolism, Phosphorylation Drug Effects, Signal Transduction Drug Effects, Amyloid Beta Protein [1-40],
Affiliations:
*** IBB - CNR ***
Department of Clinical and Molecular Biomedicine, University of Catania, Garibaldi-Nesima Hospital, Via Palermo 636, Catania 95122, Italy
Department of Drug Sciences, University of Catania, National Council of Research (Institute of Biostructures and Bioimages), Catania, 95125, Italy
References:
Not available.
Insulin has multiple antiamyloidogenic effects on human neuronal cells
Alzheimer's disease is increased in diabetic patients. A defective insulin activity on the brain has been hypothesized to contribute to the neuronal cell dysregulation leading to AD, but the mechanism is not clear.Weanalyzed the effect of insulin on several molecular steps of amyloid precursor protein (APP) processing and β-amyloid (Aβ) intracellular accumulation in a panel of human neuronal cells and inhumanembryonic kidney 293 cells overexpressing APP-695. The data indicate that insulin, via its own receptor and the phosphatidylinositol-3-kinase/AKT pathway, influences APP phosphorylation at different sites. This rapid-onset, dose-dependent effect lasts many hours and mainly concerns dephosphorylation at the APP-T668 site. This effect of insulin was confirmed also in a human cortical neuronal cell line and in rat primary neurons. Cell fractionation and immunofluorescence studies indicated that insulin-induced APP-T668 dephosphorylation prevents the translocation of the APP intracellular domain fragment into the nucleus. As a consequence, insulin increases the transcription of antiamyloidogenic proteins such as the insulin-degrading enzyme, involved in Aβ degradation, and α-secretase. In contrast, the transcripts of pro-amyloidogenic proteins such as APP, β-secretase, and glycogen synthase kinase (Gsk)-3β are decreased. Moreover, cell exposure to insulin favors the nonamyloidogenic, α-secretase-dependent APP-processing pathway and reduces Aβ40 and Aβ42 intracellular accumulation, promoting their release in the extracellular compartment. The latter effects of insulin are independent of both Gsk-3β phosphorylation and APP-T668 dephosphorylation, as indicated by experiments with Gsk-3β inhibitors and with cells transfected with the nonphosphorylatable mutated APP-T668A analog. In human neuronal cells, therefore, insulin may prevent Aβ formation and accumulation by multiple mechanisms, both Gsk-3β dependent and independent. Copyright © 2013 by The Endocrine Society.
Alzheimer's disease is increased in diabetic patients. A defective insulin activity on the brain has been hypothesized to contribute to the neuronal cell dysregulation leading to AD, but the mechanism is not clear.Weanalyzed the effect of insulin on several molecular steps of amyloid precursor protein (APP) processing and β-amyloid (Aβ) intracellular accumulation in a panel of human neuronal cells and inhumanembryonic kidney 293 cells overexpressing APP-695. The data indicate that insulin, via its own receptor and the phosphatidylinositol-3-kinase/AKT pathway, influences APP phosphorylation at different sites. This rapid-onset, dose-dependent effect lasts many hours and mainly concerns dephosphorylation at the APP-T668 site. This effect of insulin was confirmed also in a human cortical neuronal cell line and in rat primary neurons. Cell fractionation and immunofluorescence studies indicated that insulin-induced APP-T668 dephosphorylation prevents the translocation of the APP intracellular domain fragment into the nucleus. As a consequence, insulin increases the transcription of antiamyloidogenic proteins such as the insulin-degrading enzyme, involved in Aβ degradation, and α-secretase. In contrast, the transcripts of pro-amyloidogenic proteins such as APP, β-secretase, and glycogen synthase kinase (Gsk)-3β are decreased. Moreover, cell exposure to insulin favors the nonamyloidogenic, α-secretase-dependent APP-processing pathway and reduces Aβ40 and Aβ42 intracellular accumulation, promoting their release in the extracellular compartment. The latter effects of insulin are independent of both Gsk-3β phosphorylation and APP-T668 dephosphorylation, as indicated by experiments with Gsk-3β inhibitors and with cells transfected with the nonphosphorylatable mutated APP-T668A analog. In human neuronal cells, therefore, insulin may prevent Aβ formation and accumulation by multiple mechanisms, both Gsk-3β dependent and independent. Copyright © 2013 by The Endocrine Society.
Insulin has multiple antiamyloidogenic effects on human neuronal cells
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Insulin has multiple antiamyloidogenic effects on human neuronal cells
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Chem Commun (ISSN: 1364-548xelectronic, 1359-7345linking), 2018 Apr 5; 54(29): 3629-3631.
Impact Factor: 6.169
View Export to BibTeX Export to EndNote
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8 Records (8 excluding Abstracts).
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Total 5 year impact factor: 36.38 (36.38 excluding Abstracts).
Total impact factor: 36.316 (36.316 excluding Abstracts).
Total 5 year impact factor: 36.38 (36.38 excluding Abstracts).
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