Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines
Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species req...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1999 |
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| Umfang: |
8 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Cell & tissue research - 1924, 298(1999) vom: Feb., Seite 225-232 |
| Übergeordnetes Werk: |
volume:298 ; year:1999 ; month:02 ; pages:225-232 ; extent:8 |
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| 520 | |a Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. | ||
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(DE-627)NLEJ205804330 DE-627 ger DE-627 rakwb eng Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. Springer Online Journal Archives 1860-2002 Morelli, Laura oth Prat, Maria I. oth Castaño, Eduardo M. oth in Cell & tissue research 1924 298(1999) vom: Feb., Seite 225-232 (DE-627)NLEJ188990097 (DE-600)1458496-7 1432-0878 nnns volume:298 year:1999 month:02 pages:225-232 extent:8 http://dx.doi.org/10.1007/s004419900109 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 298 1999 2 225-232 8 |
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(DE-627)NLEJ205804330 DE-627 ger DE-627 rakwb eng Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. Springer Online Journal Archives 1860-2002 Morelli, Laura oth Prat, Maria I. oth Castaño, Eduardo M. oth in Cell & tissue research 1924 298(1999) vom: Feb., Seite 225-232 (DE-627)NLEJ188990097 (DE-600)1458496-7 1432-0878 nnns volume:298 year:1999 month:02 pages:225-232 extent:8 http://dx.doi.org/10.1007/s004419900109 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 298 1999 2 225-232 8 |
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(DE-627)NLEJ205804330 DE-627 ger DE-627 rakwb eng Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. Springer Online Journal Archives 1860-2002 Morelli, Laura oth Prat, Maria I. oth Castaño, Eduardo M. oth in Cell & tissue research 1924 298(1999) vom: Feb., Seite 225-232 (DE-627)NLEJ188990097 (DE-600)1458496-7 1432-0878 nnns volume:298 year:1999 month:02 pages:225-232 extent:8 http://dx.doi.org/10.1007/s004419900109 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 298 1999 2 225-232 8 |
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(DE-627)NLEJ205804330 DE-627 ger DE-627 rakwb eng Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. Springer Online Journal Archives 1860-2002 Morelli, Laura oth Prat, Maria I. oth Castaño, Eduardo M. oth in Cell & tissue research 1924 298(1999) vom: Feb., Seite 225-232 (DE-627)NLEJ188990097 (DE-600)1458496-7 1432-0878 nnns volume:298 year:1999 month:02 pages:225-232 extent:8 http://dx.doi.org/10.1007/s004419900109 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 298 1999 2 225-232 8 |
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(DE-627)NLEJ205804330 DE-627 ger DE-627 rakwb eng Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines 1999 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. Springer Online Journal Archives 1860-2002 Morelli, Laura oth Prat, Maria I. oth Castaño, Eduardo M. oth in Cell & tissue research 1924 298(1999) vom: Feb., Seite 225-232 (DE-627)NLEJ188990097 (DE-600)1458496-7 1432-0878 nnns volume:298 year:1999 month:02 pages:225-232 extent:8 http://dx.doi.org/10.1007/s004419900109 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 298 1999 2 225-232 8 |
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Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. 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differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines |
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Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines |
| abstract |
Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. |
| abstractGer |
Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. |
| abstract_unstemmed |
Abstract. Alzheimer's disease (AD) is characterized by the massive deposition in the brain of the 40–42-residue amyloid β protein (Aβ). While Aβ1–40 predominates in the vascular system, Aβ1–42 is the major component of the senile plaques in the neuropil. The concentration of both Aβ species required to form amyloid fibrils in vitro is micromolar, yet soluble Aβs found in normal and AD brains are in the low nanomolar range. It has been recently proposed that the levels of Aβ sufficient to trigger amyloidogenesis may be reached intracellularly. To study the internalization and intracellular accumulation of the major isoforms of Aβ, we used THP-1 and IMR-32 neuroblastoma cells as models of human monocytic and/or macrophagic and neuronal lineages, respectively. We tested whether these cells were able to internalize and accumulate 125I-Aβ1–40 and 125I-Aβ1–42 differentially when offered at nanomolar concentrations and free of large aggregates, conditions that mimic a prefibrillar stage of Aβ in AD brain. Our results showed that THP-1 monocytic cells internalized at least 10 times more 125I-Aβs than IMR-32 neuroblastoma cells, either isolated or in a coculture system. Moreover, 125I-Aβ1–42 presented a higher adsorption, internalization, and accumulation of undigested peptide inside cells, as opposed to 125I-Aβ1–40. These results support that Aβ1–42, the major pathogenic form in AD, may reach supersaturation and generate competent nuclei for amyloid fibril formation intracellularly. In light of the recently reported strong neurotoxicity of soluble, nonfibrillar Aβ1–42, we propose that intracellular amyloidogenesis in microglia is a protective mechanism that may delay neurodegeneration at early stages of the disease. |
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Differential accumulation of soluble amyloid β peptides 1–40 and 1–42 in human monocytic and neuroblastoma cell lines |
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http://dx.doi.org/10.1007/s004419900109 |
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Morelli, Laura Prat, Maria I. Castaño, Eduardo M. |
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