Interaction of amyloidogenic proteins in pancreatic β cells from subjects with synucleinopathies

Parkinson’s disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral nervous system. Pre-existing diabetes mellitus might be a risk factor for developing Parkinson’s disease, and indeed, nearly 60% of Parkinson’s...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Acta neuropathologica Jg. 135; H. 6; S. 877 - 886
Hauptverfasser:	Martinez-Valbuena, Ivan, Amat-Villegas, Irene, Valenti-Azcarate, Rafael, Carmona-Abellan, Maria del Mar, Marcilla, Irene, Tuñon, Maria-Teresa, Luquin, Maria-Rosario
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Berlin/Heidelberg Springer Berlin Heidelberg 01.06.2018 Springer Nature B.V
Schlagworte:	Aged Aged, 80 and over alpha-Synuclein - metabolism Amylin Amyloid Amyloidogenesis Amyloidogenic Proteins - metabolism Brain - metabolism Brain - pathology Cytoplasm - metabolism Cytoplasm - pathology Dementia Dementia disorders Diabetes Diabetes mellitus Diabetes Mellitus - metabolism Diabetes Mellitus - pathology Female Fluorescent Antibody Technique Humans Insulin Insulin-Secreting Cells - metabolism Insulin-Secreting Cells - pathology Lewy bodies Lewy body disease Lewy Body Disease - metabolism Lewy Body Disease - pathology Male Medicine Medicine & Public Health Movement disorders Nervous system Neuropathology Neurosciences Original Paper Pancreas Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Pathology Phosphorylation Retrospective Studies Synuclein Cross-seeding IAPP Diabetes mellitus Alpha-synuclein Parkinson’s disease Dementia with Lewy bodies
ISSN:	0001-6322, 1432-0533, 1432-0533
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Abstract	Parkinson’s disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral nervous system. Pre-existing diabetes mellitus might be a risk factor for developing Parkinson’s disease, and indeed, nearly 60% of Parkinson’s disease patients are insulin resistant. Thus, we have investigated whether phosphorylated α-synuclein is deposited in pancreatic tissue of subjects with synucleinopathies. We studied pancreatic tissue from 39 subjects diagnosed with Parkinson’s disease, Lewy body Dementia or incidental Lewy bodies disease, as well as that from 34 subjects with diabetes mellitus and a normal neuropathological examination, and 52 subjects with a normal neuropathological examination. We examined the pancreatic accumulation of phosphorylated α-synuclein and of the islet amyloid polypeptide precursor (IAPP), an amyloidogenic protein that plays an unknown role in diabetes mellitus, but that can promote α-synuclein amyloid deposition in vitro. Moreover, we performed proximity ligation assays to assess whether these two proteins interact in the pancreas of these subjects. Cytoplasmic phosphorylated α-synuclein deposits were found in the pancreatic β cells of 14 subjects with Parkinson’s disease (93%), in 11 subjects with Lewy body Dementia (85%) and in 8 subjects with incidental Lewy body disease (73%). Furthermore, we found similar phosphorylated α-synuclein inclusions in 23 subjects with a normal neuropathological examination but with diabetes mellitus (68%) and in 9 control subjects (17%). In addition, IAPP/α-synuclein interactions appear to occur in patients with pancreatic inclusions of phosphorylated α-synuclein. The presence of phosphorylated α-synuclein inclusions in pancreatic β cells provides a new evidence of a mechanism that is potentially common to the pathogenesis of diabetes mellitus, PD and DLB. Moreover, the interaction of IAPP and α-synuclein in the pancreatic β cells of patients may represent a novel target for the development of strategies to treat these diseases.
AbstractList	Parkinson’s disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral nervous system. Pre-existing diabetes mellitus might be a risk factor for developing Parkinson’s disease, and indeed, nearly 60% of Parkinson’s disease patients are insulin resistant. Thus, we have investigated whether phosphorylated α-synuclein is deposited in pancreatic tissue of subjects with synucleinopathies. We studied pancreatic tissue from 39 subjects diagnosed with Parkinson’s disease, Lewy body Dementia or incidental Lewy bodies disease, as well as that from 34 subjects with diabetes mellitus and a normal neuropathological examination, and 52 subjects with a normal neuropathological examination. We examined the pancreatic accumulation of phosphorylated α-synuclein and of the islet amyloid polypeptide precursor (IAPP), an amyloidogenic protein that plays an unknown role in diabetes mellitus, but that can promote α-synuclein amyloid deposition in vitro. Moreover, we performed proximity ligation assays to assess whether these two proteins interact in the pancreas of these subjects. Cytoplasmic phosphorylated α-synuclein deposits were found in the pancreatic β cells of 14 subjects with Parkinson’s disease (93%), in 11 subjects with Lewy body Dementia (85%) and in 8 subjects with incidental Lewy body disease (73%). Furthermore, we found similar phosphorylated α-synuclein inclusions in 23 subjects with a normal neuropathological examination but with diabetes mellitus (68%) and in 9 control subjects (17%). In addition, IAPP/α-synuclein interactions appear to occur in patients with pancreatic inclusions of phosphorylated α-synuclein. The presence of phosphorylated α-synuclein inclusions in pancreatic β cells provides a new evidence of a mechanism that is potentially common to the pathogenesis of diabetes mellitus, PD and DLB. Moreover, the interaction of IAPP and α-synuclein in the pancreatic β cells of patients may represent a novel target for the development of strategies to treat these diseases. Parkinson's disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral nervous system. Pre-existing diabetes mellitus might be a risk factor for developing Parkinson's disease, and indeed, nearly 60% of Parkinson's disease patients are insulin resistant. Thus, we have investigated whether phosphorylated α-synuclein is deposited in pancreatic tissue of subjects with synucleinopathies. We studied pancreatic tissue from 39 subjects diagnosed with Parkinson's disease, Lewy body Dementia or incidental Lewy bodies disease, as well as that from 34 subjects with diabetes mellitus and a normal neuropathological examination, and 52 subjects with a normal neuropathological examination. We examined the pancreatic accumulation of phosphorylated α-synuclein and of the islet amyloid polypeptide precursor (IAPP), an amyloidogenic protein that plays an unknown role in diabetes mellitus, but that can promote α-synuclein amyloid deposition in vitro. Moreover, we performed proximity ligation assays to assess whether these two proteins interact in the pancreas of these subjects. Cytoplasmic phosphorylated α-synuclein deposits were found in the pancreatic β cells of 14 subjects with Parkinson's disease (93%), in 11 subjects with Lewy body Dementia (85%) and in 8 subjects with incidental Lewy body disease (73%). Furthermore, we found similar phosphorylated α-synuclein inclusions in 23 subjects with a normal neuropathological examination but with diabetes mellitus (68%) and in 9 control subjects (17%). In addition, IAPP/α-synuclein interactions appear to occur in patients with pancreatic inclusions of phosphorylated α-synuclein. The presence of phosphorylated α-synuclein inclusions in pancreatic β cells provides a new evidence of a mechanism that is potentially common to the pathogenesis of diabetes mellitus, PD and DLB. Moreover, the interaction of IAPP and α-synuclein in the pancreatic β cells of patients may represent a novel target for the development of strategies to treat these diseases.Parkinson's disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral nervous system. Pre-existing diabetes mellitus might be a risk factor for developing Parkinson's disease, and indeed, nearly 60% of Parkinson's disease patients are insulin resistant. Thus, we have investigated whether phosphorylated α-synuclein is deposited in pancreatic tissue of subjects with synucleinopathies. We studied pancreatic tissue from 39 subjects diagnosed with Parkinson's disease, Lewy body Dementia or incidental Lewy bodies disease, as well as that from 34 subjects with diabetes mellitus and a normal neuropathological examination, and 52 subjects with a normal neuropathological examination. We examined the pancreatic accumulation of phosphorylated α-synuclein and of the islet amyloid polypeptide precursor (IAPP), an amyloidogenic protein that plays an unknown role in diabetes mellitus, but that can promote α-synuclein amyloid deposition in vitro. Moreover, we performed proximity ligation assays to assess whether these two proteins interact in the pancreas of these subjects. Cytoplasmic phosphorylated α-synuclein deposits were found in the pancreatic β cells of 14 subjects with Parkinson's disease (93%), in 11 subjects with Lewy body Dementia (85%) and in 8 subjects with incidental Lewy body disease (73%). Furthermore, we found similar phosphorylated α-synuclein inclusions in 23 subjects with a normal neuropathological examination but with diabetes mellitus (68%) and in 9 control subjects (17%). In addition, IAPP/α-synuclein interactions appear to occur in patients with pancreatic inclusions of phosphorylated α-synuclein. The presence of phosphorylated α-synuclein inclusions in pancreatic β cells provides a new evidence of a mechanism that is potentially common to the pathogenesis of diabetes mellitus, PD and DLB. Moreover, the interaction of IAPP and α-synuclein in the pancreatic β cells of patients may represent a novel target for the development of strategies to treat these diseases.
Author	Amat-Villegas, Irene Carmona-Abellan, Maria del Mar Marcilla, Irene Valenti-Azcarate, Rafael Luquin, Maria-Rosario Tuñon, Maria-Teresa Martinez-Valbuena, Ivan
Author_xml	– sequence: 1 givenname: Ivan surname: Martinez-Valbuena fullname: Martinez-Valbuena, Ivan organization: Neurology Department, Clinica Universidad de Navarra, Regenerative Therapy Laboratory, Neurosciences Division, Center for Applied Medical Research (CIMA), University of Navarra, Navarra’s Health Research Institute (IDISNA) – sequence: 2 givenname: Irene surname: Amat-Villegas fullname: Amat-Villegas, Irene organization: Navarra’s Health Research Institute (IDISNA), Pathology Department, Complejo Hospitalario de Navarra – sequence: 3 givenname: Rafael surname: Valenti-Azcarate fullname: Valenti-Azcarate, Rafael organization: Neurology Department, Clinica Universidad de Navarra, Regenerative Therapy Laboratory, Neurosciences Division, Center for Applied Medical Research (CIMA), University of Navarra, Navarra’s Health Research Institute (IDISNA) – sequence: 4 givenname: Maria del Mar surname: Carmona-Abellan fullname: Carmona-Abellan, Maria del Mar organization: Neurology Department, Clinica Universidad de Navarra, Regenerative Therapy Laboratory, Neurosciences Division, Center for Applied Medical Research (CIMA), University of Navarra, Navarra’s Health Research Institute (IDISNA) – sequence: 5 givenname: Irene surname: Marcilla fullname: Marcilla, Irene organization: Regenerative Therapy Laboratory, Neurosciences Division, Center for Applied Medical Research (CIMA), University of Navarra, Navarra’s Health Research Institute (IDISNA) – sequence: 6 givenname: Maria-Teresa surname: Tuñon fullname: Tuñon, Maria-Teresa organization: Navarra’s Health Research Institute (IDISNA), Pathology Department, Complejo Hospitalario de Navarra – sequence: 7 givenname: Maria-Rosario orcidid: 0000-0002-5594-1794 surname: Luquin fullname: Luquin, Maria-Rosario email: rluquin@unav.es organization: Neurology Department, Clinica Universidad de Navarra, Regenerative Therapy Laboratory, Neurosciences Division, Center for Applied Medical Research (CIMA), University of Navarra, Navarra’s Health Research Institute (IDISNA)
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/29536165$$D View this record in MEDLINE/PubMed
BookMark	eNp9kc1qFTEYhoNU7Gn1AtxIwE03o_nPmWUptRYKbnQdksx32hxmkmOSoZzb6oX0msxwqoVCXeXveZKXvCfoKKYICH2k5AslRH8thAhCO0LXHV1z1pE3aEXFMpGcH6EVIe1UccaO0Ukp27ZiWsh36Jj1kiuq5ArZ61ghW19DijhtsJ32YwpDuoUYPN7lVCHEgkPEOxt9Blvb9uMD9jCOBW9ymnCZ3RZ8Lfg-1Dtc9nH2Y5PSzta7AOU9eruxY4EPT-Mp-vXt8ufF9-7mx9X1xflN57lmtWOgudTSCccV19yve6cHZoWgIHyL7eXghl5521twijgvGSdcQS-EYoQ4forODve20L9nKNVMoSwxbYQ0F8MI5XotRC8a-vkFuk1zji3dQkmpGO91oz49UbObYDC7HCab9-bv5zWAHgCfUykZNv8QSsxSkDkUZFpBZinIkOboF44P1S6_X7MN439NdjBLeyXeQn4O_br0B5ndpHs
CitedBy_id	crossref_primary_10_1177_0271678X221135061 crossref_primary_10_3390_ijms242216132 crossref_primary_10_3390_brainsci13050797 crossref_primary_10_1021_acschembio_4c00777 crossref_primary_10_3390_life13101954 crossref_primary_10_1016_j_arr_2022_101727 crossref_primary_10_1016_j_arr_2019_100937 crossref_primary_10_1016_j_neuroscience_2019_05_029 crossref_primary_10_1016_j_parkreldis_2021_10_017 crossref_primary_10_3390_ijms25084358 crossref_primary_10_3390_ijms252212409 crossref_primary_10_1016_j_mmm_2024_02_003 crossref_primary_10_3233_JPD_191675 crossref_primary_10_1002_mds_29122 crossref_primary_10_1002_anse_202400104 crossref_primary_10_3389_fendo_2024_1408053 crossref_primary_10_3389_fmolb_2023_1080112 crossref_primary_10_1186_s40035_022_00288_z crossref_primary_10_1002_anie_202422834 crossref_primary_10_1016_j_nucmedbio_2022_01_003 crossref_primary_10_1111_jcmm_17784 crossref_primary_10_1111_ene_16041 crossref_primary_10_4103_NRR_NRR_D_23_01910 crossref_primary_10_1016_j_parkreldis_2021_06_002 crossref_primary_10_3389_fphar_2021_650597 crossref_primary_10_1007_s00018_024_05436_4 crossref_primary_10_3233_JPD_191900 crossref_primary_10_1093_brain_awac022 crossref_primary_10_1515_revneuro_2025_0034 crossref_primary_10_1038_s41366_022_01222_z crossref_primary_10_1093_brain_awad391 crossref_primary_10_3389_fnagi_2021_665348 crossref_primary_10_3390_ijms22031059 crossref_primary_10_1002_ana_25570 crossref_primary_10_1002_ange_202422834 crossref_primary_10_1016_j_parkreldis_2020_08_018 crossref_primary_10_1038_s41598_020_77409_z crossref_primary_10_1098_rsob_240239 crossref_primary_10_1111_nan_12728 crossref_primary_10_1002_acn3_51243 crossref_primary_10_1016_j_jpha_2022_11_006 crossref_primary_10_1016_j_yfrne_2021_100914 crossref_primary_10_1016_j_pneurobio_2023_102462 crossref_primary_10_1016_j_jep_2024_119095 crossref_primary_10_1016_j_bbamem_2022_184002 crossref_primary_10_1093_brain_awad265 crossref_primary_10_1186_s40478_021_01171_0 crossref_primary_10_1038_s41594_020_0442_4 crossref_primary_10_1002_mds_28493 crossref_primary_10_3390_molecules27061776 crossref_primary_10_1096_fj_202200235R crossref_primary_10_1007_s00415_022_11496_y crossref_primary_10_3389_fnins_2023_1244022 crossref_primary_10_1016_j_parkreldis_2020_10_013 crossref_primary_10_3389_fnins_2020_00063 crossref_primary_10_4103_1673_5374_332122 crossref_primary_10_3389_fnmol_2018_00465 crossref_primary_10_1002_mds_28124 crossref_primary_10_1002_mds_29298 crossref_primary_10_1002_mds_27556 crossref_primary_10_1016_j_arr_2021_101391
Cites_doi	10.1159/000112832 10.1016/j.pneurobio.2014.02.005 10.1016/j.tins.2016.10.008 10.1002/ana.23956 10.1038/mp.2016.230 10.1016/j.molmed.2013.01.002 10.1212/WNL.0b013e3182553cc9 10.1152/ajpendo.00262.2010 10.1101/cshperspect.a024315 10.1073/pnas.1703420114 10.1111/ene.12753 10.1016/S1353-8020(09)70769-2 10.1084/jem.20161134 10.1016/j.pneurobio.2016.10.001 10.1007/s00018-011-0905-1 10.1111/j.1365-2990.2006.00727.x 10.1007/s00401-009-0523-2 10.1002/ana.23746 10.1016/j.neuron.2016.05.040 10.1093/jnen/nlw103 10.1038/ncb748 10.1038/42166 10.1038/nrdp.2017.13 10.1016/S1474-4422(16)00080-6 10.1016/S0140-6736(17)31585-4 10.1016/S0197-4580(02)00065-9 10.1093/brain/awu369 10.3233/JAD-170192 10.1021/ar200189b 10.2337/db12-1045 10.1371/journal.pone.0085781 10.1002/mds.26605 10.1016/j.ymeth.2008.06.014 10.1016/j.jns.2011.12.008 10.1002/mds.25776 10.1212/01.wnl.0000187889.17253.b1 10.3233/JAD-160047 10.1016/0024-3205(95)02197-Q 10.1007/s00401-010-0664-3 10.1093/brain/awv040 10.1016/j.nbd.2011.07.003 10.1186/s40478-016-0408-2 10.1073/pnas.1610371113
ContentType	Journal Article
Copyright	Springer-Verlag GmbH Germany, part of Springer Nature 2018 Acta Neuropathologica is a copyright of Springer, (2018). All Rights Reserved.
Copyright_xml	– notice: Springer-Verlag GmbH Germany, part of Springer Nature 2018 – notice: Acta Neuropathologica is a copyright of Springer, (2018). All Rights Reserved.
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7TK 7U9 7X7 7XB 88E 88G 8AO 8FI 8FJ 8FK ABUWG AFKRA AZQEC BENPR CCPQU DWQXO FYUFA GHDGH GNUQQ H94 K9. M0S M1P M2M PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQQKQ PQUKI PRINS PSYQQ Q9U 7X8
DOI	10.1007/s00401-018-1832-0
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Neurosciences Abstracts Virology and AIDS Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Psychology Database (Alumni) ProQuest Pharma Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central ProQuest Central UK/Ireland ProQuest Central Essentials - QC ProQuest Central ProQuest One ProQuest Central Korea Proquest Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) ProQuest Health & Medical Collection Medical Database Psychology Database Proquest Central Premium ProQuest One Academic (New) ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China ProQuest One Psychology New ProQuest Central Basic MEDLINE - Academic
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest One Psychology ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Pharma Collection ProQuest Central China ProQuest Central ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Health & Medical Research Collection AIDS and Cancer Research Abstracts ProQuest Central (New) ProQuest Medical Library (Alumni) Virology and AIDS Abstracts ProQuest Central Basic ProQuest One Academic Eastern Edition ProQuest Hospital Collection Health Research Premium Collection (Alumni) ProQuest Psychology Journals (Alumni) Neurosciences Abstracts ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest Psychology Journals ProQuest One Academic UKI Edition ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	MEDLINE MEDLINE - Academic ProQuest One Psychology
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: BENPR name: ProQuest Central url: https://www.proquest.com/central sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Medicine
EISSN	1432-0533
EndPage	886
ExternalDocumentID	29536165 10_1007_s00401_018_1832_0
Genre	Research Support, Non-U.S. Gov't Journal Article
GrantInformation_xml	– fundername: Instituto de Salud Carlos III grantid: PI15/01816 funderid: http://dx.doi.org/10.13039/501100004587 – fundername: Instituto de Salud Carlos III grantid: PI15/01816
GroupedDBID	--- -53 -5E -5G -BR -EM -Y2 -~C .55 .86 .GJ .VR 06C 06D 0R~ 0VY 199 1N0 1SB 2.D 203 23M 28- 29~ 2J2 2JN 2JY 2KG 2KM 2LR 2P1 2VQ 2~H 30V 36B 3O- 3V. 4.4 406 408 409 40D 40E 53G 5GY 5QI 5RE 5VS 67Z 6NX 78A 7X7 88E 8AO 8FI 8FJ 8TC 8UJ 95- 95. 95~ 96X AAAVM AABHQ AACDK AAHNG AAIAL AAJBT AAJKR AANXM AANZL AARHV AARTL AASML AATNV AATVU AAUYE AAWCG AAYIU AAYQN AAYTO AAYZH ABAKF ABBBX ABBXA ABDZT ABECU ABFTV ABHLI ABHQN ABIPD ABIVO ABJNI ABJOX ABKCH ABKTR ABLJU ABMNI ABMQK ABNWP ABPLI ABQBU ABQSL ABSXP ABTEG ABTKH ABTMW ABULA ABUWG ABUWZ ABWNU ABXPI ACAOD ACBXY ACDTI ACGFS ACHSB ACHVE ACHXU ACKNC ACMDZ ACMLO ACOKC ACOMO ACPIV ACPRK ACUDM ACZOJ ADBBV ADHHG ADHIR ADIMF ADINQ ADJJI ADKNI ADKPE ADRFC ADTPH ADURQ ADYFF ADZKW AEBTG AEFIE AEFQL AEGAL AEGNC AEJHL AEJRE AEKMD AEMSY AENEX AEOHA AEPYU AESKC AETLH AEVLU AEXYK AFBBN AFDYV AFEXP AFFNX AFKRA AFLOW AFQWF AFWTZ AFZKB AGAYW AGDGC AGGDS AGJBK AGMZJ AGQEE AGQMX AGRTI AGWIL AGWZB AGYKE AHAVH AHBYD AHIZS AHKAY AHMBA AHSBF AHYZX AIAKS AIGIU AIIXL AILAN AITGF AJBLW AJRNO AJZVZ AKMHD ALIPV ALMA_UNASSIGNED_HOLDINGS ALWAN AMKLP AMXSW AMYLF AMYQR AOCGG ARMRJ ASPBG AVWKF AXYYD AZFZN AZQEC B-. BA0 BBWZM BDATZ BENPR BGNMA BPHCQ BSONS BVXVI CAG CCPQU COF CS3 CSCUP DDRTE DL5 DNIVK DPUIP DWQXO EBLON EBS EIOEI EJD EMOBN EN4 ESBYG F5P FEDTE FERAY FFXSO FIGPU FINBP FNLPD FRRFC FSGXE FWDCC FYUFA G-Y G-Z GGCAI GGRSB GJIRD GNUQQ GNWQR GQ6 GQ7 GQ8 GRRUI GXS H13 HF~ HG5 HG6 HMCUK HMJXF HQYDN HRMNR HVGLF HZ~ I09 IAO IHE IHR IJ- IKXTQ IMOTQ INH INR IPY ITC ITM IWAJR IXC IZIGR IZQ I~X I~Z J-C J0Z JBSCW JCJTX JZLTJ KDC KOV KOW KPH L7B LAS LLZTM M1P M2M M4Y MA- N2Q NB0 NDZJH NPVJJ NQJWS NU0 O9- O93 O9G O9I O9J OAM OVD P19 P2P P9S PF0 PQQKQ PROAC PSQYO PSYQQ PT4 PT5 Q2X QOK QOR QOS R4E R89 R9I RHV RIG RNI ROL RPX RRX RSV RZK S16 S1Z S26 S27 S28 S37 S3B SAP SCLPG SDE SDH SDM SHX SISQX SJYHP SMD SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW SSXJD STPWE SZ9 SZN T13 T16 TEORI TSG TSK TSV TT1 TUC U2A U9L UG4 UKHRP UOJIU UTJUX UZXMN VC2 VFIZW W23 W48 WH7 WJK WK8 X7M YLTOR Z45 Z7U Z7V Z81 Z82 Z83 Z87 Z8O Z8P Z8U Z8V Z8W Z91 ZGI ZOVNA ~EX AAPKM AAYXX ABBRH ABDBE ABFSG ABRTQ ACSTC ADHKG AEZWR AFDZB AFFHD AFHIU AFOHR AGQPQ AHPBZ AHWEU AIXLP ATHPR AYFIA CITATION PHGZM PHGZT PJZUB PPXIY CGR CUY CVF ECM EIF NPM 7TK 7U9 7XB 8FK H94 K9. PKEHL PQEST PQUKI PRINS Q9U 7X8 PUEGO
ID	FETCH-LOGICAL-c372t-2e73575b4b36373c89b7d2a441e4c274c5dbd96ca9aeb60bc523036e9446200b3
IEDL.DBID	RSV
ISICitedReferencesCount	65
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000432296500005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	0001-6322 1432-0533
IngestDate	Fri Sep 05 08:10:26 EDT 2025 Thu Nov 13 04:43:01 EST 2025 Mon Jul 21 05:59:08 EDT 2025 Sat Nov 29 05:44:48 EST 2025 Tue Nov 18 21:39:41 EST 2025 Fri Feb 21 02:35:54 EST 2025
IsPeerReviewed	true
IsScholarly	true
Issue	6
Keywords	Cross-seeding IAPP Diabetes mellitus Alpha-synuclein Parkinson’s disease Dementia with Lewy bodies
Language	English
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c372t-2e73575b4b36373c89b7d2a441e4c274c5dbd96ca9aeb60bc523036e9446200b3
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ORCID	0000-0002-5594-1794
PMID	29536165
PQID	2015562397
PQPubID	49178
PageCount	10
ParticipantIDs	proquest_miscellaneous_2013784494 proquest_journals_2015562397 pubmed_primary_29536165 crossref_primary_10_1007_s00401_018_1832_0 crossref_citationtrail_10_1007_s00401_018_1832_0 springer_journals_10_1007_s00401_018_1832_0
PublicationCentury	2000
PublicationDate	20180600 2018-6-00 2018-06-00 20180601
PublicationDateYYYYMMDD	2018-06-01
PublicationDate_xml	– month: 6 year: 2018 text: 20180600
PublicationDecade	2010
PublicationPlace	Berlin/Heidelberg
PublicationPlace_xml	– name: Berlin/Heidelberg – name: Germany – name: Heidelberg
PublicationSubtitle	Pathology and Mechanisms of Neurological Disease
PublicationTitle	Acta neuropathologica
PublicationTitleAbbrev	Acta Neuropathol
PublicationTitleAlternate	Acta Neuropathol
PublicationYear	2018
Publisher	Springer Berlin Heidelberg Springer Nature B.V
Publisher_xml	– name: Springer Berlin Heidelberg – name: Springer Nature B.V
References	Lutz (CR28) 2012; 69 Bassil, Fernagut, Bezard, Meissner (CR8) 2014; 118 Dickson, Fujishiro, Orr, DelleDonne, Josephs, Frigerio (CR15) 2009; 15 Vilas, Iranzo, Tolosa, Aldecoa, Berenguer, Vilaseca (CR43) 2016 Fujiwara, Hasegawa, Dohmae, Kawashima, Masliah, Goldberg (CR17) 2002; 4 Singleton, Hardy (CR38) 2016; 90 Leino, Popova, Alafuzoff (CR26) 2017 Íñigo-Marco, Valencia, Larrea, Bugallo, Martínez-Goikoetxea, Zuriguel (CR22) 2017 Barbour, Kling, Anderson, Banducci, Cole, Diep (CR6) 2008; 5 Gjerløff, Fedorova, Knudsen, Munk, Nahimi, Jacobsen (CR20) 2015; 138 Lu, Fu, Li, Liu, Li, Zheng (CR27) 2014; 9 Bosco, Plastino, Cristiano, Colica, Ermio, De Bartolo (CR11) 2012; 315 Poewe, Seppi, Tanner, Halliday, Brundin, Volkmann (CR33) 2017; 3 Söderberg, Leuchowius, Gullberg, Jarvius, Weibrecht, Larsson (CR39) 2008; 45 Lee, Derkinderen, Kordower, Freeman, Munoz, Kremer (CR25) 2017; 76 Kalia, Kalia, McLean, Lozano, Lang (CR24) 2013; 73 Santiago, Potashkin (CR36) 2013; 19 Bloch, Probst, Bissig, Adams, Tolnay (CR10) 2006; 32 Banks, Kastin, Maness, Huang, Jaspan (CR5) 1995; 57 Verma, Ly, Liu, Chen, Zhu, Chow (CR42) 2016; 53 Schneider, Boettner, Alexoudi, Zorenkov, Deuschl, Wedel (CR37) 2016; 23 Mukherjee, Soto (CR32) 2017 Engelender, Isacson (CR16) 2017; 40 Barrenschee, Zorenkov, Böttner, Lange, Cossais, Scharf (CR7) 2017; 5 Beach, Adler, Sue, Vedders, Lue, White (CR9) 2010; 119 Moreno-Gonzalez, Edwards, Salvadores, Shahnawaz, Diaz-Espinoza, Soto (CR30) 2017; 22 Steneberg, Bernardo, Edfalk, Lundberg, Backlund, Östenson (CR41) 2013; 62 Mukherjee, Morales-Scheihing, Salvadores, Moreno-Gonzalez, Gonzalez, Taylor-Presse (CR31) 2017 Horvath, Wittung-Stafshede (CR21) 2016; 113 Roberts, Wade-Martins, Alegre-Abarrategui (CR34) 2015; 138 Adler, Beach (CR1) 2016; 31 Alafuzoff, Ince, Arzberger, Al-Sarraj, Bell, Bodi (CR2) 2009; 117 Sang Ryong, Vicent, Hsiao-Chun, Tatyana, Tinmarla, Karen (CR35) 2011; 44 Brender, Salamekh, Ramamoorthy (CR13) 2012; 45 Gelpi, Navarro-Otano, Tolosa, Gaig, Compta, Rey (CR18) 2014; 29 Jackson, Barisone, Diaz, Jin, DeCarli, Despa (CR23) 2013; 74 Athauda, Foltynie (CR3) 2016; 145–146 Geng, Lou, Wang, Li, Swanson, Sun (CR19) 2011; 300 Cereda, Barichella, Cassani, Caccialanza, Pezzoli (CR14) 2012; 78 McKeith, Dickson, Lowe, Emre, O’Brien, Feldman (CR29) 2005; 65 Athauda, Maclagan, Skene, Bajwa-Joseph, Letchford, Chowdhury (CR4) 2017; 6736 Braak, Del Tredici, Rüb, De Vos, Jansen Steur, Braak (CR12) 2003; 24 Spillantini, Schmidt, Lee, Trojanowski, Jakes, Goedert (CR40) 1997; 388 H Fujiwara (1832_CR17) 2002; 4 T Gjerløff (1832_CR20) 2015; 138 IG McKeith (1832_CR29) 2005; 65 P Steneberg (1832_CR41) 2013; 62 DW Dickson (1832_CR15) 2009; 15 SA Schneider (1832_CR37) 2016; 23 N Verma (1832_CR42) 2016; 53 WA Banks (1832_CR5) 1995; 57 E Cereda (1832_CR14) 2012; 78 A Mukherjee (1832_CR31) 2017 M Barrenschee (1832_CR7) 2017; 5 CH Adler (1832_CR1) 2016; 31 E Gelpi (1832_CR18) 2014; 29 A Singleton (1832_CR38) 2016; 90 JA Santiago (1832_CR36) 2013; 19 I Alafuzoff (1832_CR2) 2009; 117 R Barbour (1832_CR6) 2008; 5 W Poewe (1832_CR33) 2017; 3 K Sang Ryong (1832_CR35) 2011; 44 D Athauda (1832_CR3) 2016; 145–146 JR Brender (1832_CR13) 2012; 45 L Lu (1832_CR27) 2014; 9 MG Spillantini (1832_CR40) 1997; 388 D Vilas (1832_CR43) 2016 JM Lee (1832_CR25) 2017; 76 M Leino (1832_CR26) 2017 A Bloch (1832_CR10) 2006; 32 S Engelender (1832_CR16) 2017; 40 D Athauda (1832_CR4) 2017; 6736 I Íñigo-Marco (1832_CR22) 2017 LV Kalia (1832_CR24) 2013; 73 O Söderberg (1832_CR39) 2008; 45 K Jackson (1832_CR23) 2013; 74 RF Roberts (1832_CR34) 2015; 138 TA Lutz (1832_CR28) 2012; 69 F Bassil (1832_CR8) 2014; 118 H Braak (1832_CR12) 2003; 24 X Geng (1832_CR19) 2011; 300 I Moreno-Gonzalez (1832_CR30) 2017; 22 D Bosco (1832_CR11) 2012; 315 A Mukherjee (1832_CR32) 2017 I Horvath (1832_CR21) 2016; 113 TG Beach (1832_CR9) 2010; 119
References_xml	– volume: 5 start-page: 55 year: 2008 end-page: 59 ident: CR6 article-title: Red blood cells are the major source of alpha-synuclein in blood publication-title: Neurodegener Dis doi: 10.1159/000112832 – volume: 118 start-page: 1 year: 2014 end-page: 18 ident: CR8 article-title: Insulin, IGF-1 and GLP-1 signaling in neurodegenerative disorders: targets for disease modification? publication-title: Prog Neurobiol doi: 10.1016/j.pneurobio.2014.02.005 – volume: 40 start-page: 4 year: 2017 end-page: 14 ident: CR16 article-title: the threshold theory for Parkinson’s disease publication-title: Trends Neurosci doi: 10.1016/j.tins.2016.10.008 – volume: 74 start-page: 517 year: 2013 end-page: 526 ident: CR23 article-title: Amylin deposition in the brain: a second amyloid in Alzheimer disease? publication-title: Ann Neurol doi: 10.1002/ana.23956 – volume: 22 start-page: 1327 year: 2017 end-page: 1334 ident: CR30 article-title: Molecular interaction between type 2 diabetes and Alzheimer’s disease through cross-seeding of protein misfolding publication-title: Mol Psychiatry doi: 10.1038/mp.2016.230 – volume: 19 start-page: 176 year: 2013 end-page: 186 ident: CR36 article-title: Shared dysregulated pathways lead to Parkinson’s disease and diabetes publication-title: Trends Mol Med doi: 10.1016/j.molmed.2013.01.002 – volume: 78 start-page: 1507 year: 2012 end-page: 1511 ident: CR14 article-title: Clinical features of Parkinson disease when onset of diabetes came first: a case-control study publication-title: Neurology doi: 10.1212/WNL.0b013e3182553cc9 – volume: 300 start-page: E276 year: 2011 end-page: E286 ident: CR19 article-title: α-Synuclein binds the K(ATP) channel at insulin-secretory granules and inhibits insulin secretion publication-title: Am J Physiol Endocrinol Metab doi: 10.1152/ajpendo.00262.2010 – year: 2017 ident: CR32 article-title: Prion-like protein aggregates and type 2 diabetes publication-title: Cold Spring Harb Perspect Med doi: 10.1101/cshperspect.a024315 – year: 2017 ident: CR22 article-title: E46K α-synuclein pathological mutation causes cell-autonomous toxicity without altering protein turnover or aggregation publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.1703420114 – volume: 23 start-page: 247 year: 2016 end-page: 261 ident: CR37 article-title: Can we use peripheral tissue biopsies to diagnose Parkinson’s disease? A review of the literature publication-title: Eur J Neurol doi: 10.1111/ene.12753 – volume: 15 start-page: S1 issue: Suppl 3 year: 2009 end-page: S5 ident: CR15 article-title: Neuropathology of non-motor features of Parkinson disease publication-title: Parkinsonism Relat Disord doi: 10.1016/S1353-8020(09)70769-2 – year: 2017 ident: CR31 article-title: Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism publication-title: J Exp Med doi: 10.1084/jem.20161134 – volume: 145–146 start-page: 98 year: 2016 end-page: 120 ident: CR3 article-title: Insulin resistance and Parkinson’s disease: a new target for disease modification? publication-title: Prog Neurobiol doi: 10.1016/j.pneurobio.2016.10.001 – volume: 69 start-page: 1947 year: 2012 end-page: 1965 ident: CR28 article-title: Control of energy homeostasis by amylin publication-title: Cell Mol Life Sci doi: 10.1007/s00018-011-0905-1 – volume: 32 start-page: 284 year: 2006 end-page: 295 ident: CR10 article-title: α-Synuclein pathology of the spinal and peripheral autonomic nervous system in neurologically unimpaired elderly subjects publication-title: Neuropathol Appl Neurobiol doi: 10.1111/j.1365-2990.2006.00727.x – volume: 117 start-page: 635 year: 2009 end-page: 652 ident: CR2 article-title: Staging/typing of Lewy body related α-synuclein pathology: a study of the BrainNet Europe Consortium publication-title: Acta Neuropathol doi: 10.1007/s00401-009-0523-2 – volume: 73 start-page: 155 year: 2013 end-page: 169 ident: CR24 article-title: α-Synuclein oligomers and clinical implications for parkinson disease publication-title: Ann Neurol doi: 10.1002/ana.23746 – volume: 90 start-page: 1154 year: 2016 end-page: 1163 ident: CR38 article-title: The evolution of genetics: alzheimer’s and Parkinson’s diseases publication-title: Neuron doi: 10.1016/j.neuron.2016.05.040 – volume: 76 start-page: 2 year: 2017 end-page: 15 ident: CR25 article-title: The search for a peripheral biopsy indicator of α-synuclein pathology for Parkinson disease publication-title: J Neuropathol Exp Neurol doi: 10.1093/jnen/nlw103 – volume: 4 start-page: 160 year: 2002 end-page: 164 ident: CR17 article-title: α-Synuclein is phosphorylated in synucleinopathy lesions publication-title: Nat Cell Biol doi: 10.1038/ncb748 – volume: 388 start-page: 839 year: 1997 end-page: 840 ident: CR40 article-title: Alpha-synuclein in Lewy bodies publication-title: Nature doi: 10.1038/42166 – volume: 3 start-page: 17013 year: 2017 ident: CR33 article-title: Parkinson disease publication-title: Nat Rev Dis Prim doi: 10.1038/nrdp.2017.13 – year: 2016 ident: CR43 article-title: Assessment of α-synuclein in submandibular glands of patients with idiopathic rapid-eye-movement sleep behaviour disorder: a case-control study publication-title: Lancet Neurol doi: 10.1016/S1474-4422(16)00080-6 – volume: 6736 start-page: 1 year: 2017 end-page: 12 ident: CR4 article-title: Exenatide once weekly versus placebo in Parkinson’s disease: a randomised, double-blind, placebo-controlled trial publication-title: Lancet doi: 10.1016/S0140-6736(17)31585-4 – volume: 24 start-page: 197 year: 2003 end-page: 211 ident: CR12 article-title: Staging of brain pathology related to sporadic Parkinson’s disease publication-title: Neurobiol Aging doi: 10.1016/S0197-4580(02)00065-9 – volume: 138 start-page: 653 year: 2015 end-page: 663 ident: CR20 article-title: Imaging acetylcholinesterase density in peripheral organs in Parkinson’s disease with 11 C-donepezil PET publication-title: Brain doi: 10.1093/brain/awu369 – year: 2017 ident: CR26 article-title: Transactive DNA binding protein 43 rather than other misfolded proteins in the brain is associated with islet amyloid polypeptide in pancreas in aged subjects with diabetes mellitus publication-title: J Alzheimer’s Dis doi: 10.3233/JAD-170192 – volume: 45 start-page: 454 year: 2012 end-page: 462 ident: CR13 article-title: Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective publication-title: Acc Chem Res doi: 10.1021/ar200189b – volume: 62 start-page: 2004 year: 2013 end-page: 2014 ident: CR41 article-title: The type 2 diabetes-associated gene Ide is required for insulin secretion and suppression of α-synuclein levels in β-cells publication-title: Diabetes doi: 10.2337/db12-1045 – volume: 9 start-page: e85781 year: 2014 ident: CR27 article-title: Diabetes and risk of Parkinson’s disease: an updated meta-analysis of case-control studies publication-title: PLoS ONE doi: 10.1371/journal.pone.0085781 – volume: 31 start-page: 1114 year: 2016 end-page: 1119 ident: CR1 article-title: Neuropathological basis of nonmotor manifestations of Parkinson’s disease publication-title: Mov Disord doi: 10.1002/mds.26605 – volume: 45 start-page: 227 year: 2008 end-page: 232 ident: CR39 article-title: Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay publication-title: Methods doi: 10.1016/j.ymeth.2008.06.014 – volume: 315 start-page: 39 year: 2012 end-page: 43 ident: CR11 article-title: Dementia is associated with insulin resistance in patients with Parkinson’s disease publication-title: J Neurol Sci doi: 10.1016/j.jns.2011.12.008 – volume: 29 start-page: 1010 year: 2014 end-page: 1018 ident: CR18 article-title: Multiple organ involvement by alpha-synuclein pathology in Lewy body disorders publication-title: Mov Disord doi: 10.1002/mds.25776 – volume: 65 start-page: 1863 year: 2005 end-page: 1872 ident: CR29 article-title: Diagnosis and management of dementia with Lewy bodies: third report of the DLB Consortium publication-title: Neurology doi: 10.1212/01.wnl.0000187889.17253.b1 – volume: 53 start-page: 259 year: 2016 end-page: 272 ident: CR42 article-title: Intraneuronal amylin deposition, peroxidative membrane injury and increased IL-1β synthesis in brains of Alzheimer’s disease patients with type-2 diabetes and in diabetic HIP rats publication-title: J Alzheimer’s Dis doi: 10.3233/JAD-160047 – volume: 57 start-page: 1993 year: 1995 end-page: 2001 ident: CR5 article-title: Permeability of the blood-brain barrier to amylin publication-title: Life Sci doi: 10.1016/0024-3205(95)02197-Q – volume: 119 start-page: 689 year: 2010 end-page: 702 ident: CR9 article-title: Multi-organ distribution of phosphorylated α-synuclein histopathology in subjects with Lewy body disorders publication-title: Acta Neuropathol doi: 10.1007/s00401-010-0664-3 – volume: 138 start-page: 1642 year: 2015 end-page: 1657 ident: CR34 article-title: Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson’s disease brain publication-title: Brain doi: 10.1093/brain/awv040 – volume: 44 start-page: 215 year: 2011 end-page: 222 ident: CR35 article-title: Age and alpha-synuclein expression interact to reveal a dependence of dopaminergic axons on edogenous Akt/PKB signaling publication-title: Neurobiol Dis doi: 10.1016/j.nbd.2011.07.003 – volume: 5 start-page: 1 year: 2017 ident: CR7 article-title: Distinct pattern of enteric phospho-alpha-synuclein aggregates and gene expression profiles in patients with Parkinson’s disease publication-title: Acta Neuropathol Commun doi: 10.1186/s40478-016-0408-2 – volume: 113 start-page: 12473 year: 2016 end-page: 12477 ident: CR21 article-title: Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson’s disease publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1610371113 – volume: 57 start-page: 1993 year: 1995 ident: 1832_CR5 publication-title: Life Sci doi: 10.1016/0024-3205(95)02197-Q – volume: 15 start-page: S1 issue: Suppl 3 year: 2009 ident: 1832_CR15 publication-title: Parkinsonism Relat Disord doi: 10.1016/S1353-8020(09)70769-2 – volume: 69 start-page: 1947 year: 2012 ident: 1832_CR28 publication-title: Cell Mol Life Sci doi: 10.1007/s00018-011-0905-1 – volume: 5 start-page: 1 year: 2017 ident: 1832_CR7 publication-title: Acta Neuropathol Commun doi: 10.1186/s40478-016-0408-2 – volume: 5 start-page: 55 year: 2008 ident: 1832_CR6 publication-title: Neurodegener Dis doi: 10.1159/000112832 – volume: 315 start-page: 39 year: 2012 ident: 1832_CR11 publication-title: J Neurol Sci doi: 10.1016/j.jns.2011.12.008 – volume: 45 start-page: 454 year: 2012 ident: 1832_CR13 publication-title: Acc Chem Res doi: 10.1021/ar200189b – volume: 300 start-page: E276 year: 2011 ident: 1832_CR19 publication-title: Am J Physiol Endocrinol Metab doi: 10.1152/ajpendo.00262.2010 – volume: 45 start-page: 227 year: 2008 ident: 1832_CR39 publication-title: Methods doi: 10.1016/j.ymeth.2008.06.014 – volume: 6736 start-page: 1 year: 2017 ident: 1832_CR4 publication-title: Lancet doi: 10.1016/S0140-6736(17)31585-4 – volume: 32 start-page: 284 year: 2006 ident: 1832_CR10 publication-title: Neuropathol Appl Neurobiol doi: 10.1111/j.1365-2990.2006.00727.x – volume: 31 start-page: 1114 year: 2016 ident: 1832_CR1 publication-title: Mov Disord doi: 10.1002/mds.26605 – volume: 3 start-page: 17013 year: 2017 ident: 1832_CR33 publication-title: Nat Rev Dis Prim doi: 10.1038/nrdp.2017.13 – volume: 40 start-page: 4 year: 2017 ident: 1832_CR16 publication-title: Trends Neurosci doi: 10.1016/j.tins.2016.10.008 – volume: 113 start-page: 12473 year: 2016 ident: 1832_CR21 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1610371113 – volume: 74 start-page: 517 year: 2013 ident: 1832_CR23 publication-title: Ann Neurol doi: 10.1002/ana.23956 – volume: 73 start-page: 155 year: 2013 ident: 1832_CR24 publication-title: Ann Neurol doi: 10.1002/ana.23746 – volume: 65 start-page: 1863 year: 2005 ident: 1832_CR29 publication-title: Neurology doi: 10.1212/01.wnl.0000187889.17253.b1 – volume: 138 start-page: 1642 year: 2015 ident: 1832_CR34 publication-title: Brain doi: 10.1093/brain/awv040 – year: 2017 ident: 1832_CR32 publication-title: Cold Spring Harb Perspect Med doi: 10.1101/cshperspect.a024315 – year: 2017 ident: 1832_CR26 publication-title: J Alzheimer’s Dis doi: 10.3233/JAD-170192 – volume: 23 start-page: 247 year: 2016 ident: 1832_CR37 publication-title: Eur J Neurol doi: 10.1111/ene.12753 – year: 2017 ident: 1832_CR31 publication-title: J Exp Med doi: 10.1084/jem.20161134 – volume: 388 start-page: 839 year: 1997 ident: 1832_CR40 publication-title: Nature doi: 10.1038/42166 – volume: 19 start-page: 176 year: 2013 ident: 1832_CR36 publication-title: Trends Mol Med doi: 10.1016/j.molmed.2013.01.002 – year: 2016 ident: 1832_CR43 publication-title: Lancet Neurol doi: 10.1016/S1474-4422(16)00080-6 – volume: 145–146 start-page: 98 year: 2016 ident: 1832_CR3 publication-title: Prog Neurobiol doi: 10.1016/j.pneurobio.2016.10.001 – volume: 22 start-page: 1327 year: 2017 ident: 1832_CR30 publication-title: Mol Psychiatry doi: 10.1038/mp.2016.230 – volume: 138 start-page: 653 year: 2015 ident: 1832_CR20 publication-title: Brain doi: 10.1093/brain/awu369 – year: 2017 ident: 1832_CR22 publication-title: Proc Natl Acad Sci doi: 10.1073/pnas.1703420114 – volume: 119 start-page: 689 year: 2010 ident: 1832_CR9 publication-title: Acta Neuropathol doi: 10.1007/s00401-010-0664-3 – volume: 29 start-page: 1010 year: 2014 ident: 1832_CR18 publication-title: Mov Disord doi: 10.1002/mds.25776 – volume: 24 start-page: 197 year: 2003 ident: 1832_CR12 publication-title: Neurobiol Aging doi: 10.1016/S0197-4580(02)00065-9 – volume: 9 start-page: e85781 year: 2014 ident: 1832_CR27 publication-title: PLoS ONE doi: 10.1371/journal.pone.0085781 – volume: 90 start-page: 1154 year: 2016 ident: 1832_CR38 publication-title: Neuron doi: 10.1016/j.neuron.2016.05.040 – volume: 118 start-page: 1 year: 2014 ident: 1832_CR8 publication-title: Prog Neurobiol doi: 10.1016/j.pneurobio.2014.02.005 – volume: 44 start-page: 215 year: 2011 ident: 1832_CR35 publication-title: Neurobiol Dis doi: 10.1016/j.nbd.2011.07.003 – volume: 78 start-page: 1507 year: 2012 ident: 1832_CR14 publication-title: Neurology doi: 10.1212/WNL.0b013e3182553cc9 – volume: 4 start-page: 160 year: 2002 ident: 1832_CR17 publication-title: Nat Cell Biol doi: 10.1038/ncb748 – volume: 76 start-page: 2 year: 2017 ident: 1832_CR25 publication-title: J Neuropathol Exp Neurol doi: 10.1093/jnen/nlw103 – volume: 117 start-page: 635 year: 2009 ident: 1832_CR2 publication-title: Acta Neuropathol doi: 10.1007/s00401-009-0523-2 – volume: 53 start-page: 259 year: 2016 ident: 1832_CR42 publication-title: J Alzheimer’s Dis doi: 10.3233/JAD-160047 – volume: 62 start-page: 2004 year: 2013 ident: 1832_CR41 publication-title: Diabetes doi: 10.2337/db12-1045
SSID	ssj0012745
Score	2.488598
Snippet	Parkinson’s disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral... Parkinson's disease patients experience a wide range of non-motor symptoms that may be provoked by deposits of phosphorylated α-synuclein in the peripheral...
SourceID	proquest pubmed crossref springer
SourceType	Aggregation Database Index Database Enrichment Source Publisher
StartPage	877
SubjectTerms	Aged Aged, 80 and over alpha-Synuclein - metabolism Amylin Amyloid Amyloidogenesis Amyloidogenic Proteins - metabolism Brain - metabolism Brain - pathology Cytoplasm - metabolism Cytoplasm - pathology Dementia Dementia disorders Diabetes Diabetes mellitus Diabetes Mellitus - metabolism Diabetes Mellitus - pathology Female Fluorescent Antibody Technique Humans Insulin Insulin-Secreting Cells - metabolism Insulin-Secreting Cells - pathology Lewy bodies Lewy body disease Lewy Body Disease - metabolism Lewy Body Disease - pathology Male Medicine Medicine & Public Health Movement disorders Nervous system Neuropathology Neurosciences Original Paper Pancreas Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Pathology Phosphorylation Retrospective Studies Synuclein
SummonAdditionalLinks	– databaseName: Health & Medical Collection dbid: 7X7 link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1NT9wwEB3Rpaq4AG1pSYHKSJxaRUrirJ2cqgqx4sKKQyvtLXJsrxQJHLrerdS_xQ_pb-qM84EqBBfOSRzL8-yZN5O8ATibFtIIo8gChsfoIWSsLGJZp4bkxdJUpiY0m5DzebFYlNd9ws33n1UOZ2I4qE2rKUeOJB09H_rqUn67-xVT1yiqrvYtNF7BNrXNJpzLxUi4UmRcXQcDpMwCkTtUNZNORDQQaeRQCOo4-d8vPQo2HxVKg_-Z7b105vuw20ee7HsHlbewZd07eHPV19bfgwrJwe4_B9YumbpFLt-YFhHWaBb0HBrnWeMYHiBdrKnZ33tGqX_P6DcV5jc1pXU8o-wu838ciSU3rg1tj60_gJ-zix_nl3HfgCHWXGbrOLOSYzhX5zUXXHJdlLU0mcIIyuYaF1dPTW1KoUnhuxZJrSnFzIUtkWPi7qv5B5i41tlDYFLnebYsRIEjkV5OWSRKSCWnZkmCViqCZFj-Svfq5NQk46YadZWDxSq0WEUWq5IIvoyP3HXSHM_dfDwYp-p3qa8eLBPB6XgZ9xetnHK23YR7uCzyvMwj-NhhYXxbRrXvVEwj-DqA42HwJ6fy6fmpHMFORrAMmZ5jmKxXG3sCr_XvdeNXnwPA_wGca_6z priority: 102 providerName: ProQuest
Title	Interaction of amyloidogenic proteins in pancreatic β cells from subjects with synucleinopathies
URI	https://link.springer.com/article/10.1007/s00401-018-1832-0 https://www.ncbi.nlm.nih.gov/pubmed/29536165 https://www.proquest.com/docview/2015562397 https://www.proquest.com/docview/2013784494
Volume	135
WOSCitedRecordID	wos000432296500005&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAVX databaseName: SpringerLINK Contemporary 1997-Present customDbUrl: eissn: 1432-0533 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0012745 issn: 0001-6322 databaseCode: RSV dateStart: 19970101 isFulltext: true titleUrlDefault: https://link.springer.com/search?facet-content-type=%22Journal%22 providerName: Springer Nature
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3NatwwEB7SpJRe0qZtWqfpokBPLYa1ZUv2MSkbctllSdKwNyNLWjAkdoh2A3mtPkieKTPyTyhpC83FYDyWxeiTND_WNwBf00waYRSNgOEh7hAyVBaxrCND9GJRJCPji03I2SxbLPJ5d47b9X-79ylJv1IPh90Ib-T6oteDMAzRT99KiWyGXPSziyF1gG5WW7YAhQXCtU9l_qmJ3zejJxbmk-yo33SO3zyru29hu7Mx2WELih3YsPU7eDXtsujvQfkwYHuigTVLpq7Qa69Mg1iqNPPMDVXtWFUzXCpaq1Kz-1-MgvyO0YEU5tYlBXAcozguc3c10SJXdeMLHFv3AX4eT85_nIRdqYVQcxmvwthKjoZbmZRccMl1lpfSxAptJZto1KhOTWlyoYnLuxTjUlMwmQubozeJ86zku7BZN7X9BEzqJImXmciwJWLGybOxElLJ1CyJukoFMO51XuiOh5zKYVwWA4OyV12BqitIdcU4gG_DK9ctCce_hPf7gSy6-eiKmExDtPRyGcDB8BhnEmlO1bZZexkusyTJkwA-tgAYvhZTljsSaQDf-9F-bPyvXdn7L-nP8DomuPgQzz5srm7W9gu81Leryt2M4IVcSH_NRrB1NJnNT_FuGk9HHv4P-Cn4XA
linkProvider	Springer Nature
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3LbtQwFL0qBQEb3oWUAkaCDShSYmfsZIEQAqpW7YxYFKm74NgeKVKblHoGND_Fgg_hm3qv86hQRXddsE7iJPa5b_tcgFeTXFlpNa2AFTFaCBVrh1g2qSV6sTRVqQ3NJtRslh8eFl_W4NdwFoa2VQ46MShq2xrKkWOQjpYPbXWh3p98j6lrFFVXhxYaHSz23Oonhmz-3e4nXN_XnG9_Pvi4E_ddBWIjFF_E3CmBPkqVVUIKJUxeVMpyjW6BywzGaGZiK1tIQ7TVlUwqQ3lTIV2BgRNCqhI47jW4nqElpI4JUz4dqxb4dNcxAUN0iZIyVFGTjrQ0BO4Ys6EQxcnfdvCCc3uhMBvs3fbd_22m7sGd3rNmHzpRuA9rrnkAN6f93oGHoEPyszvHwdo508ero7a2LUpQbVjgq6gbz-qGoYLsfGnD_vxmVNrwjI7hML-sKG3lGWWvmV81RAZdN21o6-z8I_h6JT-4AetN27gnwJTJMj7PZY4jER9QkSdaKq0mdk6EXTqCZFju0vTs69QE5KgceaMDQkpESEkIKZMI3oyPnHTUI5fdvDWAoey1kC_PkRDBy_Ey6g-aOd24dhnuESrPsiKL4HGHvfFtnGr7qZxE8HYA4_ng__yUzcs_5QXc2jmY7pf7u7O9p3Cbk0iErNYWrC9Ol-4Z3DA_FrU_fR6Ei8G3q8boGas5WiI
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3LbtQwFL0qU1SxobwJLWAk2IAikjhjJwuEgHZEVRiNEEjdpY7tkSKVpNQzoPktlv2IfhP3Oo8KVXTXBeskTmKf-7bPBXg-zqQRRtEKGB6ihZChsohlHRuiF4tjGRvfbEJOp9nBQT5bg9P-LAxtq-x1olfUptGUI8cgHS0f2upcvp532yJmO5O3xz9C6iBFlda-nUYLkX27-oXhm3uzt4Nr_SJJJrtfP3wMuw4DoeYyWYSJlRz9lTItueCS6ywvpUkUugg21Riv6bEpTS40UViXIio15VC5sDkGUQivkuO412Bdcgx6RrD-fnc6-zLUMPD5tn8CBuwC5aavqUYthakP4zGCQ5EKo7-t4gVX90KZ1lu_yeb_PG-34Gbnc7N3rZDchjVb34GNz92ugrugfFq0PeHBmjlT31dHTWUalK1KM89kUdWOVTVD1dl62Zqd_WZU9HCMDugwtywpoeUY5bWZW9VEE13VjW_4bN09-HYlP3gfRnVT24fApE7TZJ6JDEcipqA8i5SQSo7NnKi8VABRv_SF7njZqT3IUTEwSnu0FIiWgtBSRAG8HB45bklJLrt5uwdG0eknV5yjIoBnw2XULDRzqrbN0t_DZZameRrAgxaHw9sSqvrHYhzAqx6Y54P_81MeXf4pT2EDoVl82pvub8GNhKTDp7u2YbQ4WdrHcF3_XFTu5EknaQwOrxqkfwAfDGRF
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Interaction+of+amyloidogenic+proteins+in+pancreatic+%CE%B2+cells+from+subjects+with+synucleinopathies&rft.jtitle=Acta+neuropathologica&rft.au=Martinez-Valbuena%2C+Ivan&rft.au=Amat-Villegas%2C+Irene&rft.au=Valenti-Azcarate%2C+Rafael&rft.au=Carmona-Abellan%2C+Maria+del+Mar&rft.date=2018-06-01&rft.pub=Springer+Berlin+Heidelberg&rft.issn=0001-6322&rft.eissn=1432-0533&rft.volume=135&rft.issue=6&rft.spage=877&rft.epage=886&rft_id=info:doi/10.1007%2Fs00401-018-1832-0&rft.externalDocID=10_1007_s00401_018_1832_0
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0001-6322&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0001-6322&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0001-6322&client=summon