Regulation of distinct pools of amyloid β-protein by multiple cellular proteases

Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms...
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Gespeichert in:

Autor*in:	Leissring, Malcolm A [verfasserIn] Turner, Anthony J

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2013

Schlagwörter:	Down Syndrome Amyloid Precursor Protein Cerebral Amyloid Angiopathy Intracellular Pool Amyloid Cascade Hypothesis

Anmerkung:	© BioMed Central Ltd. 2013

Übergeordnetes Werk:	Enthalten in: Alzheimer's research & therapy - London : BioMed Central, 2009, 5(2013), 4 vom: 13. Aug.
Übergeordnetes Werk:	volume:5 ; year:2013 ; number:4 ; day:13 ; month:08

Links:	Volltext

DOI / URN:	10.1186/alzrt194

Katalog-ID:	SPR030812542

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spelling	10.1186/alzrt194 doi (DE-627)SPR030812542 (SPR)alzrt194-e DE-627 ger DE-627 rakwb eng Leissring, Malcolm A verfasserin aut Regulation of distinct pools of amyloid β-protein by multiple cellular proteases 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd. 2013 Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. Down Syndrome (dpeaa)DE-He213 Amyloid Precursor Protein (dpeaa)DE-He213 Cerebral Amyloid Angiopathy (dpeaa)DE-He213 Intracellular Pool (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Turner, Anthony J aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 5(2013), 4 vom: 13. Aug. (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:5 year:2013 number:4 day:13 month:08 https://dx.doi.org/10.1186/alzrt194 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 5 2013 4 13 08
allfields_unstemmed	10.1186/alzrt194 doi (DE-627)SPR030812542 (SPR)alzrt194-e DE-627 ger DE-627 rakwb eng Leissring, Malcolm A verfasserin aut Regulation of distinct pools of amyloid β-protein by multiple cellular proteases 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd. 2013 Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. Down Syndrome (dpeaa)DE-He213 Amyloid Precursor Protein (dpeaa)DE-He213 Cerebral Amyloid Angiopathy (dpeaa)DE-He213 Intracellular Pool (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Turner, Anthony J aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 5(2013), 4 vom: 13. Aug. (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:5 year:2013 number:4 day:13 month:08 https://dx.doi.org/10.1186/alzrt194 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 5 2013 4 13 08
allfieldsGer	10.1186/alzrt194 doi (DE-627)SPR030812542 (SPR)alzrt194-e DE-627 ger DE-627 rakwb eng Leissring, Malcolm A verfasserin aut Regulation of distinct pools of amyloid β-protein by multiple cellular proteases 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd. 2013 Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. Down Syndrome (dpeaa)DE-He213 Amyloid Precursor Protein (dpeaa)DE-He213 Cerebral Amyloid Angiopathy (dpeaa)DE-He213 Intracellular Pool (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Turner, Anthony J aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 5(2013), 4 vom: 13. Aug. (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:5 year:2013 number:4 day:13 month:08 https://dx.doi.org/10.1186/alzrt194 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 5 2013 4 13 08
allfieldsSound	10.1186/alzrt194 doi (DE-627)SPR030812542 (SPR)alzrt194-e DE-627 ger DE-627 rakwb eng Leissring, Malcolm A verfasserin aut Regulation of distinct pools of amyloid β-protein by multiple cellular proteases 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © BioMed Central Ltd. 2013 Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. Down Syndrome (dpeaa)DE-He213 Amyloid Precursor Protein (dpeaa)DE-He213 Cerebral Amyloid Angiopathy (dpeaa)DE-He213 Intracellular Pool (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213 Turner, Anthony J aut Enthalten in Alzheimer's research & therapy London : BioMed Central, 2009 5(2013), 4 vom: 13. Aug. (DE-627)605683557 (DE-600)2506521-X 1758-9193 nnns volume:5 year:2013 number:4 day:13 month:08 https://dx.doi.org/10.1186/alzrt194 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 5 2013 4 13 08
language	English
source	Enthalten in Alzheimer's research & therapy 5(2013), 4 vom: 13. Aug. volume:5 year:2013 number:4 day:13 month:08
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institution	findex.gbv.de
topic_facet	Down Syndrome Amyloid Precursor Protein Cerebral Amyloid Angiopathy Intracellular Pool Amyloid Cascade Hypothesis
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container_title	Alzheimer's research & therapy
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author	Leissring, Malcolm A
spellingShingle	Leissring, Malcolm A misc Down Syndrome misc Amyloid Precursor Protein misc Cerebral Amyloid Angiopathy misc Intracellular Pool misc Amyloid Cascade Hypothesis Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
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topic_title	Regulation of distinct pools of amyloid β-protein by multiple cellular proteases Down Syndrome (dpeaa)DE-He213 Amyloid Precursor Protein (dpeaa)DE-He213 Cerebral Amyloid Angiopathy (dpeaa)DE-He213 Intracellular Pool (dpeaa)DE-He213 Amyloid Cascade Hypothesis (dpeaa)DE-He213
topic	misc Down Syndrome misc Amyloid Precursor Protein misc Cerebral Amyloid Angiopathy misc Intracellular Pool misc Amyloid Cascade Hypothesis
topic_unstemmed	misc Down Syndrome misc Amyloid Precursor Protein misc Cerebral Amyloid Angiopathy misc Intracellular Pool misc Amyloid Cascade Hypothesis
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title	Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
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title_full	Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
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title_sort	regulation of distinct pools of amyloid β-protein by multiple cellular proteases
title_auth	Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
abstract	Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. © BioMed Central Ltd. 2013
abstractGer	Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. © BioMed Central Ltd. 2013
abstract_unstemmed	Abstract Alzheimer’s disease (AD) is a progressive, age-related neurodegenerative disorder characterized by extracellular and intracellular deposition of the amyloid β-protein (Aβ). The study of rare, familial forms of AD has shown that sustained elevations in the production of Aβ (either all forms or specific pathogenic variants thereof) are sufficient to trigger the full spectrum of cognitive and histopathological features of the disease. Although the exact cause or causes remain unknown, emerging evidence suggests that impairments in the clearance of Aβ, after it is produced, may underlie the vast majority of sporadic AD cases. This review focuses on Aβ-degrading proteases (AβDPs), which have emerged as particularly important mediators of Aβ clearance. A wide variety of proteases that – by virtue of their particular regional and subcellular localization profiles – define distinct pools of Aβ have been identified. Different pools of Aβ, in turn, may contribute differentially to the pathogenesis of the disease. The study of individual AβDPs, therefore, promises to offer new insights into the mechanistic basis of AD pathogenesis and, ultimately, may facilitate the development of effective methods for its prevention or treatment or both. © BioMed Central Ltd. 2013
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title_short	Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
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Regulation of distinct pools of amyloid β-protein by multiple cellular proteases

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