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Sangram S. Sisodia - One of the best experts on this subject based on the ideXlab platform.
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Metabolism of the Swedish Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells EVIDENCE THAT CLEAVAGE AT THE “β-SECRETASE” SITE OCCURS IN THE GOLGI APPARATUS
The Journal of biological chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:The 4-kDa beta-amyloid peptide (Abeta), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Abeta production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Abeta peptides and beta-secretase-generated soluble APP derivatives (APP s beta) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of alpha-secretase-generated soluble APP derivatives (APP s alpha). Our interpretation of these findings is that beta-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by alpha-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by alpha-secretase, but not by beta-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by beta-secretase, we now unequivocally demonstrate that beta-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
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metabolism of the swedish amyloid precursor Protein Variant in neuro2a n2a cells evidence that cleavage at the β secretase site occurs in the golgi apparatus
Journal of Biological Chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:Abstract The 4-kDa β-amyloid peptide (Aβ), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Aβ production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Aβ peptides and β-secretase-generated soluble APP derivatives (APP) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of α-secretase-generated soluble APP derivatives (APP). Our interpretation of these findings is that β-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by α-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by α-secretase, but not by β-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by β-secretase, we now unequivocally demonstrate that β-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
Gopal Thinakaran - One of the best experts on this subject based on the ideXlab platform.
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Metabolism of the Swedish Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells EVIDENCE THAT CLEAVAGE AT THE “β-SECRETASE” SITE OCCURS IN THE GOLGI APPARATUS
The Journal of biological chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:The 4-kDa beta-amyloid peptide (Abeta), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Abeta production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Abeta peptides and beta-secretase-generated soluble APP derivatives (APP s beta) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of alpha-secretase-generated soluble APP derivatives (APP s alpha). Our interpretation of these findings is that beta-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by alpha-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by alpha-secretase, but not by beta-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by beta-secretase, we now unequivocally demonstrate that beta-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
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metabolism of the swedish amyloid precursor Protein Variant in neuro2a n2a cells evidence that cleavage at the β secretase site occurs in the golgi apparatus
Journal of Biological Chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:Abstract The 4-kDa β-amyloid peptide (Aβ), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Aβ production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Aβ peptides and β-secretase-generated soluble APP derivatives (APP) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of α-secretase-generated soluble APP derivatives (APP). Our interpretation of these findings is that β-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by α-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by α-secretase, but not by β-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by β-secretase, we now unequivocally demonstrate that β-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
David B. Teplow - One of the best experts on this subject based on the ideXlab platform.
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Metabolism of the Swedish Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells EVIDENCE THAT CLEAVAGE AT THE “β-SECRETASE” SITE OCCURS IN THE GOLGI APPARATUS
The Journal of biological chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:The 4-kDa beta-amyloid peptide (Abeta), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Abeta production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Abeta peptides and beta-secretase-generated soluble APP derivatives (APP s beta) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of alpha-secretase-generated soluble APP derivatives (APP s alpha). Our interpretation of these findings is that beta-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by alpha-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by alpha-secretase, but not by beta-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by beta-secretase, we now unequivocally demonstrate that beta-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
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metabolism of the swedish amyloid precursor Protein Variant in neuro2a n2a cells evidence that cleavage at the β secretase site occurs in the golgi apparatus
Journal of Biological Chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:Abstract The 4-kDa β-amyloid peptide (Aβ), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Aβ production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Aβ peptides and β-secretase-generated soluble APP derivatives (APP) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of α-secretase-generated soluble APP derivatives (APP). Our interpretation of these findings is that β-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by α-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by α-secretase, but not by β-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by β-secretase, we now unequivocally demonstrate that β-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
Robert Siman - One of the best experts on this subject based on the ideXlab platform.
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Metabolism of the Swedish Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells EVIDENCE THAT CLEAVAGE AT THE “β-SECRETASE” SITE OCCURS IN THE GOLGI APPARATUS
The Journal of biological chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:The 4-kDa beta-amyloid peptide (Abeta), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Abeta production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Abeta peptides and beta-secretase-generated soluble APP derivatives (APP s beta) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of alpha-secretase-generated soluble APP derivatives (APP s alpha). Our interpretation of these findings is that beta-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by alpha-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by alpha-secretase, but not by beta-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by beta-secretase, we now unequivocally demonstrate that beta-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
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metabolism of the swedish amyloid precursor Protein Variant in neuro2a n2a cells evidence that cleavage at the β secretase site occurs in the golgi apparatus
Journal of Biological Chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:Abstract The 4-kDa β-amyloid peptide (Aβ), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Aβ production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Aβ peptides and β-secretase-generated soluble APP derivatives (APP) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of α-secretase-generated soluble APP derivatives (APP). Our interpretation of these findings is that β-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by α-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by α-secretase, but not by β-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by β-secretase, we now unequivocally demonstrate that β-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
Barry D. Greenberg - One of the best experts on this subject based on the ideXlab platform.
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Metabolism of the Swedish Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells EVIDENCE THAT CLEAVAGE AT THE “β-SECRETASE” SITE OCCURS IN THE GOLGI APPARATUS
The Journal of biological chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:The 4-kDa beta-amyloid peptide (Abeta), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Abeta production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Abeta peptides and beta-secretase-generated soluble APP derivatives (APP s beta) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of alpha-secretase-generated soluble APP derivatives (APP s alpha). Our interpretation of these findings is that beta-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by alpha-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by alpha-secretase, but not by beta-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by beta-secretase, we now unequivocally demonstrate that beta-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
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metabolism of the swedish amyloid precursor Protein Variant in neuro2a n2a cells evidence that cleavage at the β secretase site occurs in the golgi apparatus
Journal of Biological Chemistry, 1996Co-Authors: Gopal Thinakaran, David B. Teplow, Robert Siman, Barry D. Greenberg, Sangram S. SisodiaAbstract:Abstract The 4-kDa β-amyloid peptide (Aβ), a principal component of parenchymal amyloid deposits in Alzheimer's disease, is derived from amyloid precursor Proteins (APP). To identify potential intracellular compartments involved in Aβ production, we expressed human APP-695 (APPwt) and APP-695 harboring the Swedish double mutation (APPswe) associated with familial early-onset Alzheimer's disease, in mouse N2a cells. We demonstrate that cells expressing APPswe secrete high levels of Aβ peptides and β-secretase-generated soluble APP derivatives (APP) relative to cells expressing APPwt. In addition, we observed a concomitant diminution in the levels of α-secretase-generated soluble APP derivatives (APP). Our interpretation of these findings is that β-secretase cleavage occurs in an intracellular compartment and disables those substrates which would normally be cleaved by α-secretase. As anticipated, the levels of APPswe are diminished relative to the steady-state levels of surface-bound APPwt; moreover, surface-bound APPswe and APPwt molecules are released from the plasma membrane after cleavage by α-secretase, but not by β-secretase. Finally, by examining the rate of appearance of specific APP metabolites generated by β-secretase, we now unequivocally demonstrate that β-secretase cleavage of APPswe occurs within the Golgi apparatus, as early as the medial compartment.
