Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations
The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amy...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Nuovo, Gerard [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Umfang: |
6 |
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| Übergeordnetes Werk: |
Enthalten in: Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial - Yao, Kenshi ELSEVIER, 2015, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:28 ; year:2017 ; pages:24-29 ; extent:6 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.anndiagpath.2017.02.006 |
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| 520 | |a The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. | ||
| 520 | |a The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. | ||
| 700 | 1 | |a Paniccia, Bernard |4 oth | |
| 700 | 1 | |a Mezache, Louisa |4 oth | |
| 700 | 1 | |a Quiñónez, Maria |4 oth | |
| 700 | 1 | |a Williams, James |4 oth | |
| 700 | 1 | |a Vandiver, Paige |4 oth | |
| 700 | 1 | |a Fadda, Paolo |4 oth | |
| 700 | 1 | |a Amann, Vicky |4 oth | |
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10.1016/j.anndiagpath.2017.02.006 doi GBVA2017018000009.pica (DE-627)ELV025559176 (ELSEVIER)S1092-9134(17)30042-4 DE-627 ger DE-627 rakwb eng 610 610 DE-600 610 VZ 600 670 VZ 51.00 bkl Nuovo, Gerard verfasserin aut Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations 2017transfer abstract 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. Paniccia, Bernard oth Mezache, Louisa oth Quiñónez, Maria oth Williams, James oth Vandiver, Paige oth Fadda, Paolo oth Amann, Vicky oth Enthalten in Elsevier Yao, Kenshi ELSEVIER Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial 2015 Amsterdam [u.a.] (DE-627)ELV013464221 volume:28 year:2017 pages:24-29 extent:6 https://doi.org/10.1016/j.anndiagpath.2017.02.006 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 GBV_ILN_72 GBV_ILN_2003 51.00 Werkstoffkunde: Allgemeines VZ AR 28 2017 24-29 6 045F 610 |
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10.1016/j.anndiagpath.2017.02.006 doi GBVA2017018000009.pica (DE-627)ELV025559176 (ELSEVIER)S1092-9134(17)30042-4 DE-627 ger DE-627 rakwb eng 610 610 DE-600 610 VZ 600 670 VZ 51.00 bkl Nuovo, Gerard verfasserin aut Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations 2017transfer abstract 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. Paniccia, Bernard oth Mezache, Louisa oth Quiñónez, Maria oth Williams, James oth Vandiver, Paige oth Fadda, Paolo oth Amann, Vicky oth Enthalten in Elsevier Yao, Kenshi ELSEVIER Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial 2015 Amsterdam [u.a.] (DE-627)ELV013464221 volume:28 year:2017 pages:24-29 extent:6 https://doi.org/10.1016/j.anndiagpath.2017.02.006 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 GBV_ILN_72 GBV_ILN_2003 51.00 Werkstoffkunde: Allgemeines VZ AR 28 2017 24-29 6 045F 610 |
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10.1016/j.anndiagpath.2017.02.006 doi GBVA2017018000009.pica (DE-627)ELV025559176 (ELSEVIER)S1092-9134(17)30042-4 DE-627 ger DE-627 rakwb eng 610 610 DE-600 610 VZ 600 670 VZ 51.00 bkl Nuovo, Gerard verfasserin aut Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations 2017transfer abstract 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. Paniccia, Bernard oth Mezache, Louisa oth Quiñónez, Maria oth Williams, James oth Vandiver, Paige oth Fadda, Paolo oth Amann, Vicky oth Enthalten in Elsevier Yao, Kenshi ELSEVIER Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial 2015 Amsterdam [u.a.] (DE-627)ELV013464221 volume:28 year:2017 pages:24-29 extent:6 https://doi.org/10.1016/j.anndiagpath.2017.02.006 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 GBV_ILN_72 GBV_ILN_2003 51.00 Werkstoffkunde: Allgemeines VZ AR 28 2017 24-29 6 045F 610 |
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10.1016/j.anndiagpath.2017.02.006 doi GBVA2017018000009.pica (DE-627)ELV025559176 (ELSEVIER)S1092-9134(17)30042-4 DE-627 ger DE-627 rakwb eng 610 610 DE-600 610 VZ 600 670 VZ 51.00 bkl Nuovo, Gerard verfasserin aut Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations 2017transfer abstract 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. Paniccia, Bernard oth Mezache, Louisa oth Quiñónez, Maria oth Williams, James oth Vandiver, Paige oth Fadda, Paolo oth Amann, Vicky oth Enthalten in Elsevier Yao, Kenshi ELSEVIER Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial 2015 Amsterdam [u.a.] (DE-627)ELV013464221 volume:28 year:2017 pages:24-29 extent:6 https://doi.org/10.1016/j.anndiagpath.2017.02.006 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 GBV_ILN_72 GBV_ILN_2003 51.00 Werkstoffkunde: Allgemeines VZ AR 28 2017 24-29 6 045F 610 |
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10.1016/j.anndiagpath.2017.02.006 doi GBVA2017018000009.pica (DE-627)ELV025559176 (ELSEVIER)S1092-9134(17)30042-4 DE-627 ger DE-627 rakwb eng 610 610 DE-600 610 VZ 600 670 VZ 51.00 bkl Nuovo, Gerard verfasserin aut Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations 2017transfer abstract 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. Paniccia, Bernard oth Mezache, Louisa oth Quiñónez, Maria oth Williams, James oth Vandiver, Paige oth Fadda, Paolo oth Amann, Vicky oth Enthalten in Elsevier Yao, Kenshi ELSEVIER Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial 2015 Amsterdam [u.a.] (DE-627)ELV013464221 volume:28 year:2017 pages:24-29 extent:6 https://doi.org/10.1016/j.anndiagpath.2017.02.006 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 GBV_ILN_72 GBV_ILN_2003 51.00 Werkstoffkunde: Allgemeines VZ AR 28 2017 24-29 6 045F 610 |
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Enthalten in Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial Amsterdam [u.a.] volume:28 year:2017 pages:24-29 extent:6 |
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Nuovo, Gerard @@aut@@ Paniccia, Bernard @@oth@@ Mezache, Louisa @@oth@@ Quiñónez, Maria @@oth@@ Williams, James @@oth@@ Vandiver, Paige @@oth@@ Fadda, Paolo @@oth@@ Amann, Vicky @@oth@@ |
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Su1557 Development of an E-Learning System for the Endoscopic Diagnosis of Early Gastric Cancer: an International Multicenter Randomized Controlled Trial |
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diagnostic pathology of alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations |
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Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations |
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The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. |
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The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. |
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The absence of any histologic correlate for Alzheimer's disease despite its commonness and severe clinical sequelae may offers clues to its etiology. Recent evidence strongly suggests that the central event of this disease is the hyperphosphorylation of neuronal tau protein and not the beta amyloid precipitates. In each case, essential and soluble neuronal proteins derivatives form insoluble aggregates that can readily be detected by immunohistochemistry using antibodies specific for the misfolded proteins. Immunohistochemistry also demonstrates that neurons with hyperphosphorylated tau protein are viable. Experimental evidence using neuronal cell cultures suggests that the affected neurons in Alzheimer's disease may have undergone molecular changes that include accumulation of anti-apopotic proteins MCL1 and cFLIP that do not allow the cell to undergo programmed cell death but, rather, to “immortalize” and thus accumulate hyperphosphorylated tau protein in the neuronal cell body and beta amyloid in downstream dendrites. We describe a simplified protocol to demonstrate such changes based on tagged LNA modified microRNA/antimicroRNA oligomers and cell cultures. Co-expression showed that the tagged antimiR-512 strongly localized with the markedly up-regulated proteins MCL1 and cFLIP with concomitant accumulation of hyperphosphorylated tau protein. The data underscore to the anatomic pathologist that the diagnosis of Alzheimer's disease is best accomplished by simple immunohistochemistry tests correlated to the clinical history and the key role pathologists can play in understanding the cause of the disease. |
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Diagnostic pathology of Alzheimer's disease from routine microscopy to immunohistochemistry and experimental correlations |
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