Immunohistochemical Demonstration of the pGlu79 α-Synuclein Fragment in Alzheimer’s Disease and Its Tg2576 Mouse Model
The deposition of β-amyloid peptides and of α-synuclein proteins is a neuropathological hallmark in the brains of Alzheimer’s disease (AD) and Parkinson’s disease (PD) subjects, respectively. However, there is accumulative evidence that both proteins are not exclusive for their clinical entity but i...
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| Published in | Biomolecules (Basel, Switzerland) Vol. 12; no. 7; p. 1006 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Basel
MDPI AG
20.07.2022
MDPI |
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| Online Access | Get full text |
| ISSN | 2218-273X 2218-273X |
| DOI | 10.3390/biom12071006 |
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| Abstract | The deposition of β-amyloid peptides and of α-synuclein proteins is a neuropathological hallmark in the brains of Alzheimer’s disease (AD) and Parkinson’s disease (PD) subjects, respectively. However, there is accumulative evidence that both proteins are not exclusive for their clinical entity but instead co-exist and interact with each other. Here, we investigated the presence of a newly identified, pyroglutamate79-modified α-synuclein variant (pGlu79-aSyn)—along with the enzyme matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) implicated in its formation—in AD and in the transgenic Tg2576 AD mouse model. In the human brain, pGlu79-aSyn was detected in cortical pyramidal neurons, with more distinct labeling in AD compared to control brain tissue. Using immunohistochemical double and triple labelings and confocal laser scanning microscopy, we demonstrate an association of pGlu79-aSyn, MMP-3 and QC with β-amyloid plaques. In addition, pGlu79-aSyn and QC were present in amyloid plaque-associated reactive astrocytes that were also immunoreactive for the chaperone heat shock protein 27 (HSP27). Our data are consistent for the transgenic mouse model and the human clinical condition. We conclude that pGlu79-aSyn can be generated extracellularly or within reactive astrocytes, accumulates in proximity to β-amyloid plaques and induces an astrocytic protein unfolding mechanism involving HSP27. |
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| AbstractList | The deposition of β-amyloid peptides and of α-synuclein proteins is a neuropathological hallmark in the brains of Alzheimer’s disease (AD) and Parkinson’s disease (PD) subjects, respectively. However, there is accumulative evidence that both proteins are not exclusive for their clinical entity but instead co-exist and interact with each other. Here, we investigated the presence of a newly identified, pyroglutamate79-modified α-synuclein variant (pGlu79-aSyn)—along with the enzyme matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) implicated in its formation—in AD and in the transgenic Tg2576 AD mouse model. In the human brain, pGlu79-aSyn was detected in cortical pyramidal neurons, with more distinct labeling in AD compared to control brain tissue. Using immunohistochemical double and triple labelings and confocal laser scanning microscopy, we demonstrate an association of pGlu79-aSyn, MMP-3 and QC with β-amyloid plaques. In addition, pGlu79-aSyn and QC were present in amyloid plaque-associated reactive astrocytes that were also immunoreactive for the chaperone heat shock protein 27 (HSP27). Our data are consistent for the transgenic mouse model and the human clinical condition. We conclude that pGlu79-aSyn can be generated extracellularly or within reactive astrocytes, accumulates in proximity to β-amyloid plaques and induces an astrocytic protein unfolding mechanism involving HSP27. The deposition of β-amyloid peptides and of α-synuclein proteins is a neuropathological hallmark in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) subjects, respectively. However, there is accumulative evidence that both proteins are not exclusive for their clinical entity but instead co-exist and interact with each other. Here, we investigated the presence of a newly identified, pyroglutamate79-modified α-synuclein variant (pGlu79-aSyn)-along with the enzyme matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) implicated in its formation-in AD and in the transgenic Tg2576 AD mouse model. In the human brain, pGlu79-aSyn was detected in cortical pyramidal neurons, with more distinct labeling in AD compared to control brain tissue. Using immunohistochemical double and triple labelings and confocal laser scanning microscopy, we demonstrate an association of pGlu79-aSyn, MMP-3 and QC with β-amyloid plaques. In addition, pGlu79-aSyn and QC were present in amyloid plaque-associated reactive astrocytes that were also immunoreactive for the chaperone heat shock protein 27 (HSP27). Our data are consistent for the transgenic mouse model and the human clinical condition. We conclude that pGlu79-aSyn can be generated extracellularly or within reactive astrocytes, accumulates in proximity to β-amyloid plaques and induces an astrocytic protein unfolding mechanism involving HSP27.The deposition of β-amyloid peptides and of α-synuclein proteins is a neuropathological hallmark in the brains of Alzheimer's disease (AD) and Parkinson's disease (PD) subjects, respectively. However, there is accumulative evidence that both proteins are not exclusive for their clinical entity but instead co-exist and interact with each other. Here, we investigated the presence of a newly identified, pyroglutamate79-modified α-synuclein variant (pGlu79-aSyn)-along with the enzyme matrix metalloproteinase-3 (MMP-3) and glutaminyl cyclase (QC) implicated in its formation-in AD and in the transgenic Tg2576 AD mouse model. In the human brain, pGlu79-aSyn was detected in cortical pyramidal neurons, with more distinct labeling in AD compared to control brain tissue. Using immunohistochemical double and triple labelings and confocal laser scanning microscopy, we demonstrate an association of pGlu79-aSyn, MMP-3 and QC with β-amyloid plaques. In addition, pGlu79-aSyn and QC were present in amyloid plaque-associated reactive astrocytes that were also immunoreactive for the chaperone heat shock protein 27 (HSP27). Our data are consistent for the transgenic mouse model and the human clinical condition. We conclude that pGlu79-aSyn can be generated extracellularly or within reactive astrocytes, accumulates in proximity to β-amyloid plaques and induces an astrocytic protein unfolding mechanism involving HSP27. |
| Author | Schulze, Anja Hartlage-Rübsamen, Maike Schilling, Stephan Roßner, Steffen Schrempel, Sarah Bluhm, Alexandra von Hörsten, Stephan |
| AuthorAffiliation | 3 Faculty of Applied Biosciences and Process Engineering, Anhalt University of Applied Sciences, 06366 Köthen, Germany 2 Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, 06120 Halle (Saale), Germany; stephan.schilling@izi.fraunhofer.de (S.S.); anja.schulze@izi.fraunhofer.de (A.S.) 4 Department for Experimental Therapy, University Clinics Erlangen and Preclinical Experimental Center, University of Erlangen-Nuremberg, 91054 Erlangen, Germany; stephan.v.hoersten@fau.de 1 Paul Flechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany; alexandra.bluhm@medizin.uni-leipzig.de (A.B.); sarah.schrempel@medizin.uni-leipzig.de (Sa.S.); maikerbs@rz.uni-leipzig.de (M.H.-R.) |
| AuthorAffiliation_xml | – name: 4 Department for Experimental Therapy, University Clinics Erlangen and Preclinical Experimental Center, University of Erlangen-Nuremberg, 91054 Erlangen, Germany; stephan.v.hoersten@fau.de – name: 1 Paul Flechsig Institute for Brain Research, University of Leipzig, 04103 Leipzig, Germany; alexandra.bluhm@medizin.uni-leipzig.de (A.B.); sarah.schrempel@medizin.uni-leipzig.de (Sa.S.); maikerbs@rz.uni-leipzig.de (M.H.-R.) – name: 3 Faculty of Applied Biosciences and Process Engineering, Anhalt University of Applied Sciences, 06366 Köthen, Germany – name: 2 Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation, 06120 Halle (Saale), Germany; stephan.schilling@izi.fraunhofer.de (S.S.); anja.schulze@izi.fraunhofer.de (A.S.) |
| Author_xml | – sequence: 1 givenname: Alexandra surname: Bluhm fullname: Bluhm, Alexandra – sequence: 2 givenname: Sarah surname: Schrempel fullname: Schrempel, Sarah – sequence: 3 givenname: Stephan surname: Schilling fullname: Schilling, Stephan – sequence: 4 givenname: Stephan orcidid: 0000-0001-6409-0664 surname: von Hörsten fullname: von Hörsten, Stephan – sequence: 5 givenname: Anja orcidid: 0000-0002-3358-8299 surname: Schulze fullname: Schulze, Anja – sequence: 6 givenname: Steffen surname: Roßner fullname: Roßner, Steffen – sequence: 7 givenname: Maike surname: Hartlage-Rübsamen fullname: Hartlage-Rübsamen, Maike |
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| CitedBy_id | crossref_primary_10_3389_fmolb_2023_1153839 crossref_primary_10_1016_j_drudis_2023_103644 crossref_primary_10_1007_s00401_024_02824_9 |
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| Title | Immunohistochemical Demonstration of the pGlu79 α-Synuclein Fragment in Alzheimer’s Disease and Its Tg2576 Mouse Model |
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