Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD
PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a ge...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Perluigi, Marzia [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells - Wu, Zhi-Sheng ELSEVIER, 2020, the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:108 ; year:2017 ; pages:62 |
| Links: |
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| DOI / URN: |
10.1016/j.freeradbiomed.2017.04.216 |
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| 520 | |a PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression | ||
| 520 | |a PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression | ||
| 650 | 7 | |a Alzheimer disease |2 Elsevier | |
| 650 | 7 | |a O-GlcNacylation |2 Elsevier | |
| 650 | 7 | |a glucose metabolism |2 Elsevier | |
| 700 | 1 | |a Tramutola, Antonella |4 oth | |
| 700 | 1 | |a Sharma, Nidhi |4 oth | |
| 700 | 1 | |a di Domenico, Fabio |4 oth | |
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10.1016/j.freeradbiomed.2017.04.216 doi GBVA2017014000025.pica (DE-627)ELV015230414 (ELSEVIER)S0891-5849(17)30419-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Perluigi, Marzia verfasserin aut Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD 2017transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression Alzheimer disease Elsevier O-GlcNacylation Elsevier glucose metabolism Elsevier Tramutola, Antonella oth Sharma, Nidhi oth di Domenico, Fabio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:108 year:2017 pages:62 https://doi.org/10.1016/j.freeradbiomed.2017.04.216 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 108 2017 62 108.2017, S62- 045F 570 |
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10.1016/j.freeradbiomed.2017.04.216 doi GBVA2017014000025.pica (DE-627)ELV015230414 (ELSEVIER)S0891-5849(17)30419-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Perluigi, Marzia verfasserin aut Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD 2017transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression Alzheimer disease Elsevier O-GlcNacylation Elsevier glucose metabolism Elsevier Tramutola, Antonella oth Sharma, Nidhi oth di Domenico, Fabio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:108 year:2017 pages:62 https://doi.org/10.1016/j.freeradbiomed.2017.04.216 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 108 2017 62 108.2017, S62- 045F 570 |
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10.1016/j.freeradbiomed.2017.04.216 doi GBVA2017014000025.pica (DE-627)ELV015230414 (ELSEVIER)S0891-5849(17)30419-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Perluigi, Marzia verfasserin aut Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD 2017transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression Alzheimer disease Elsevier O-GlcNacylation Elsevier glucose metabolism Elsevier Tramutola, Antonella oth Sharma, Nidhi oth di Domenico, Fabio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:108 year:2017 pages:62 https://doi.org/10.1016/j.freeradbiomed.2017.04.216 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 108 2017 62 108.2017, S62- 045F 570 |
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10.1016/j.freeradbiomed.2017.04.216 doi GBVA2017014000025.pica (DE-627)ELV015230414 (ELSEVIER)S0891-5849(17)30419-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Perluigi, Marzia verfasserin aut Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD 2017transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression Alzheimer disease Elsevier O-GlcNacylation Elsevier glucose metabolism Elsevier Tramutola, Antonella oth Sharma, Nidhi oth di Domenico, Fabio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:108 year:2017 pages:62 https://doi.org/10.1016/j.freeradbiomed.2017.04.216 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 108 2017 62 108.2017, S62- 045F 570 |
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10.1016/j.freeradbiomed.2017.04.216 doi GBVA2017014000025.pica (DE-627)ELV015230414 (ELSEVIER)S0891-5849(17)30419-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Perluigi, Marzia verfasserin aut Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD 2017transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression Alzheimer disease Elsevier O-GlcNacylation Elsevier glucose metabolism Elsevier Tramutola, Antonella oth Sharma, Nidhi oth di Domenico, Fabio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:108 year:2017 pages:62 https://doi.org/10.1016/j.freeradbiomed.2017.04.216 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 108 2017 62 108.2017, S62- 045F 570 |
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Enthalten in New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells New York, NY [u.a.] volume:108 year:2017 pages:62 |
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Enthalten in New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells New York, NY [u.a.] volume:108 year:2017 pages:62 |
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Altered protein O-GlcNAcylation profile revealed by proteomics: Novel insights on protein signalling mechanisms in AD |
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PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression |
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PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression |
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PET studies have demonstrated the early deficiency of cerebral glucose metabolism in AD patients. Reduced glucose utilization lead to altered protein O-GlcNAcylation, which might represent a link between glucose hypometabolism and the progression of AD. Increasing evidence support, in AD brain, a general decrease of protein O-GlcNAcylation coupled with a mutual inverse increased phosphorylation on Ser/Thr residues. Several redox signalling proteins are aberrantly regulated by O-GlcNacylation, during AD contributing to decreased cell survival and increased stress conditions. In this study, we investigated, by 1D and 2D SDS-PAGE, the levels of total and protein specific O-GlcNAcylation levels in the cortex of 12 months-old 3xTg-AD compared with age-matched non-Tg mice. Our data demonstrate a general decrease of total levels of O-GlcNAcylation in 3xTg-AD together with the impairment of O-GlcNacylation cycling enzymes. Data from proteomics analysis led to the identification of several proteins with differential O-GlcNAc levels between transgenic and WT animals which belongs to key pathways involved in the progression of AD, such as, neuronal structure, degradation processes and energy metabolism. Our findings may contribute to understand the effects of altered protein O-GlcNAcylation profile during AD, identifying novel mechanisms of disease progression |
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