The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology

Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD)...
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Autor*in:	Nadia Canu [verfasserIn] Giuseppina Amadoro [verfasserIn] Viviana Triaca [verfasserIn] Valentina Latina [verfasserIn] Valentina Sposato [verfasserIn] Veronica Corsetti [verfasserIn] Cinzia Severini [verfasserIn] Maria Teresa Ciotti [verfasserIn] Pietro Calissano [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD)

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 18(2017), 6, p 1319
Übergeordnetes Werk:	volume:18 ; year:2017 ; number:6, p 1319

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/ijms18061319

Katalog-ID:	DOAJ059762764

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allfields	10.3390/ijms18061319 doi (DE-627)DOAJ059762764 (DE-599)DOAJ6592cf13925245a5bfcbf4426db9d05d DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Nadia Canu verfasserin aut The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system. nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry Giuseppina Amadoro verfasserin aut Viviana Triaca verfasserin aut Valentina Latina verfasserin aut Valentina Sposato verfasserin aut Veronica Corsetti verfasserin aut Cinzia Severini verfasserin aut Maria Teresa Ciotti verfasserin aut Pietro Calissano verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 18(2017), 6, p 1319 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:18 year:2017 number:6, p 1319 https://doi.org/10.3390/ijms18061319 kostenfrei https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d kostenfrei http://www.mdpi.com/1422-0067/18/6/1319 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2017 6, p 1319
spelling	10.3390/ijms18061319 doi (DE-627)DOAJ059762764 (DE-599)DOAJ6592cf13925245a5bfcbf4426db9d05d DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Nadia Canu verfasserin aut The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system. nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry Giuseppina Amadoro verfasserin aut Viviana Triaca verfasserin aut Valentina Latina verfasserin aut Valentina Sposato verfasserin aut Veronica Corsetti verfasserin aut Cinzia Severini verfasserin aut Maria Teresa Ciotti verfasserin aut Pietro Calissano verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 18(2017), 6, p 1319 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:18 year:2017 number:6, p 1319 https://doi.org/10.3390/ijms18061319 kostenfrei https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d kostenfrei http://www.mdpi.com/1422-0067/18/6/1319 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2017 6, p 1319
allfields_unstemmed	10.3390/ijms18061319 doi (DE-627)DOAJ059762764 (DE-599)DOAJ6592cf13925245a5bfcbf4426db9d05d DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Nadia Canu verfasserin aut The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system. nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry Giuseppina Amadoro verfasserin aut Viviana Triaca verfasserin aut Valentina Latina verfasserin aut Valentina Sposato verfasserin aut Veronica Corsetti verfasserin aut Cinzia Severini verfasserin aut Maria Teresa Ciotti verfasserin aut Pietro Calissano verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 18(2017), 6, p 1319 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:18 year:2017 number:6, p 1319 https://doi.org/10.3390/ijms18061319 kostenfrei https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d kostenfrei http://www.mdpi.com/1422-0067/18/6/1319 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2017 6, p 1319
allfieldsGer	10.3390/ijms18061319 doi (DE-627)DOAJ059762764 (DE-599)DOAJ6592cf13925245a5bfcbf4426db9d05d DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Nadia Canu verfasserin aut The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system. nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry Giuseppina Amadoro verfasserin aut Viviana Triaca verfasserin aut Valentina Latina verfasserin aut Valentina Sposato verfasserin aut Veronica Corsetti verfasserin aut Cinzia Severini verfasserin aut Maria Teresa Ciotti verfasserin aut Pietro Calissano verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 18(2017), 6, p 1319 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:18 year:2017 number:6, p 1319 https://doi.org/10.3390/ijms18061319 kostenfrei https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d kostenfrei http://www.mdpi.com/1422-0067/18/6/1319 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2017 6, p 1319
allfieldsSound	10.3390/ijms18061319 doi (DE-627)DOAJ059762764 (DE-599)DOAJ6592cf13925245a5bfcbf4426db9d05d DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Nadia Canu verfasserin aut The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system. nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry Giuseppina Amadoro verfasserin aut Viviana Triaca verfasserin aut Valentina Latina verfasserin aut Valentina Sposato verfasserin aut Veronica Corsetti verfasserin aut Cinzia Severini verfasserin aut Maria Teresa Ciotti verfasserin aut Pietro Calissano verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 18(2017), 6, p 1319 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:18 year:2017 number:6, p 1319 https://doi.org/10.3390/ijms18061319 kostenfrei https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d kostenfrei http://www.mdpi.com/1422-0067/18/6/1319 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2017 6, p 1319
language	English
source	In International Journal of Molecular Sciences 18(2017), 6, p 1319 volume:18 year:2017 number:6, p 1319
sourceStr	In International Journal of Molecular Sciences 18(2017), 6, p 1319 volume:18 year:2017 number:6, p 1319
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD) Biology (General) Chemistry
isfreeaccess_bool	true
container_title	International Journal of Molecular Sciences
authorswithroles_txt_mv	Nadia Canu @@aut@@ Giuseppina Amadoro @@aut@@ Viviana Triaca @@aut@@ Valentina Latina @@aut@@ Valentina Sposato @@aut@@ Veronica Corsetti @@aut@@ Cinzia Severini @@aut@@ Maria Teresa Ciotti @@aut@@ Pietro Calissano @@aut@@
publishDateDaySort_date	2017-01-01T00:00:00Z
hierarchy_top_id	316340715
id	DOAJ059762764
language_de	englisch
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callnumber-first	Q - Science
author	Nadia Canu
spellingShingle	Nadia Canu misc QH301-705.5 misc QD1-999 misc nerve growth factor (NGF) misc Tropomyosin receptor kinase A (TrkA) receptor misc basal forebrain cholinergic neurons (BFCN) misc Amyloid Precursor Protein (APP) misc synapses misc tau protein misc Alzheimer’s disease (AD) misc Biology (General) misc Chemistry The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology
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topic_title	QH301-705.5 QD1-999 The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology nerve growth factor (NGF) Tropomyosin receptor kinase A (TrkA) receptor basal forebrain cholinergic neurons (BFCN) Amyloid Precursor Protein (APP) synapses tau protein Alzheimer’s disease (AD)
topic	misc QH301-705.5 misc QD1-999 misc nerve growth factor (NGF) misc Tropomyosin receptor kinase A (TrkA) receptor misc basal forebrain cholinergic neurons (BFCN) misc Amyloid Precursor Protein (APP) misc synapses misc tau protein misc Alzheimer’s disease (AD) misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc nerve growth factor (NGF) misc Tropomyosin receptor kinase A (TrkA) receptor misc basal forebrain cholinergic neurons (BFCN) misc Amyloid Precursor Protein (APP) misc synapses misc tau protein misc Alzheimer’s disease (AD) misc Biology (General) misc Chemistry
topic_browse	misc QH301-705.5 misc QD1-999 misc nerve growth factor (NGF) misc Tropomyosin receptor kinase A (TrkA) receptor misc basal forebrain cholinergic neurons (BFCN) misc Amyloid Precursor Protein (APP) misc synapses misc tau protein misc Alzheimer’s disease (AD) misc Biology (General) misc Chemistry
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title	The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology
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title_full	The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology
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author_browse	Nadia Canu Giuseppina Amadoro Viviana Triaca Valentina Latina Valentina Sposato Veronica Corsetti Cinzia Severini Maria Teresa Ciotti Pietro Calissano
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title_sort	intersection of ngf/trka signaling and amyloid precursor protein processing in alzheimer’s disease neuropathology
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title_auth	The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology
abstract	Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system.
abstractGer	Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system.
abstract_unstemmed	Dysfunction of nerve growth factor (NGF) and its high-affinity Tropomyosin receptor kinase A (TrkA) receptor has been suggested to contribute to the selective degeneration of basal forebrain cholinergic neurons (BFCN) associated with the progressive cognitive decline in Alzheimer's disease (AD). The aim of this review is to describe our progress in elucidating the molecular mechanisms underlying the dynamic interplay between NGF/TrkA signaling and amyloid precursor protein (APP) metabolism within the context of AD neuropathology. This is mainly based on the finding that TrkA receptor binding to APP depends on a minimal stretch of ~20 amino acids located in the juxtamembrane/extracellular domain of APP that carries the α- and β-secretase cleavage sites. Here, we provide evidence that: (i) NGF could be one of the “routing” proteins responsible for modulating the metabolism of APP from amyloidogenic towards non-amyloidogenic processing via binding to the TrkA receptor; (ii) the loss of NGF/TrkA signaling could be linked to sporadic AD contributing to the classical hallmarks of the neuropathology, such as synaptic loss, β-amyloid peptide (Aβ) deposition and tau abnormalities. These findings will hopefully help to design therapeutic strategies for AD treatment aimed at preserving cholinergic function and anti-amyloidogenic activity of the physiological NGF/TrkA pathway in the septo-hippocampal system.
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title_short	The Intersection of NGF/TrkA Signaling and Amyloid Precursor Protein Processing in Alzheimer’s Disease Neuropathology
url	https://doi.org/10.3390/ijms18061319 https://doaj.org/article/6592cf13925245a5bfcbf4426db9d05d http://www.mdpi.com/1422-0067/18/6/1319 https://doaj.org/toc/1422-0067
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