Microspectroscopy (μFTIR) reveals co-localization of lipid oxidation and amyloid plaques in human Alzheimer disease brains
Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, ther...
Uloženo v:
| Vydáno v: | Analytical chemistry (Washington) Ročník 86; číslo 24; s. 12047 |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
United States
16.12.2014
|
| Témata: | |
| ISSN: | 1520-6882, 1520-6882 |
| On-line přístup: | Zjistit podrobnosti o přístupu |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role. |
|---|---|
| AbstractList | Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role. Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role.Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role. |
| Author | Klementieva, Oxana Cotte, Marine Benseny-Cases, Núria Cladera, Josep Ferrer, Isidre |
| Author_xml | – sequence: 1 givenname: Núria surname: Benseny-Cases fullname: Benseny-Cases, Núria organization: European Synchrotron Radiation Facility, 71 Avenue des Martyrs, F-38000 Grenoble, France – sequence: 2 givenname: Oxana surname: Klementieva fullname: Klementieva, Oxana – sequence: 3 givenname: Marine surname: Cotte fullname: Cotte, Marine – sequence: 4 givenname: Isidre surname: Ferrer fullname: Ferrer, Isidre – sequence: 5 givenname: Josep surname: Cladera fullname: Cladera, Josep |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25415602$$D View this record in MEDLINE/PubMed |
| BookMark | eNpNkN1KwzAcxYNM3Ide-AKSy3lRTdImTS_HcDqYCDKvy79JyiJpU5tO3Hw1n8FnsrIJXp3D4cfhcMZoUPvaIHRJyQ0ljN6C4oQJkRYnaEQ5I5GQkg3--SEah_BKCKWEijM0ZDyhXBA2Qp-PVrU-NEZ1vSjf7PD0-2uxXj5f49a8G3ABKx85r8DZPXTW19iX2NnGauw_rD5EUGsM1c75Pm0cvG1NwLbGm20FNZ65_cbYyrRY22AgGFy0YOtwjk7Lvt9cHHWCXhZ36_lDtHq6X85nqwg4JV2UcSNkATKhpgBOtCwyrqmQGWSphLhUQDRJMwKppLGkSsZKZ0miFGhKRBmzCZoeepvW_y7r8soGZZyD2vhtyKmIU86lkKxHr47otqiMzpvWVtDu8r_D2A_VlXA9 |
| CitedBy_id | crossref_primary_10_1016_j_cca_2019_01_021 crossref_primary_10_1007_s12035_024_04388_x crossref_primary_10_1038_s41598_019_50837_2 crossref_primary_10_1038_s41598_024_82999_z crossref_primary_10_1038_s41598_017_11721_z crossref_primary_10_3390_ijms21041505 crossref_primary_10_1007_s10043_018_0416_5 crossref_primary_10_3390_ijms22073430 crossref_primary_10_1016_j_joim_2025_02_001 crossref_primary_10_1016_j_vibspec_2016_09_016 crossref_primary_10_1016_j_jep_2023_117132 crossref_primary_10_1039_C6AN01580H crossref_primary_10_1038_s42003_024_07034_3 crossref_primary_10_1038_ncomms14726 crossref_primary_10_1039_C6CS00542J crossref_primary_10_1111_jnc_16306 crossref_primary_10_1155_2016_9245150 crossref_primary_10_3233_BSI_170171 crossref_primary_10_1186_s12964_018_0277_3 crossref_primary_10_1016_j_infrared_2025_106138 crossref_primary_10_1007_s11356_018_3726_z crossref_primary_10_1016_j_saa_2019_117570 crossref_primary_10_1186_s40409_017_0114_y crossref_primary_10_1016_j_vibspec_2016_07_017 crossref_primary_10_1038_s41598_021_96379_4 crossref_primary_10_3389_fnins_2018_00647 crossref_primary_10_1016_j_saa_2020_118625 crossref_primary_10_1016_j_saa_2021_120794 crossref_primary_10_1111_bpa_13202 crossref_primary_10_3389_fcell_2021_704298 crossref_primary_10_1016_j_crci_2016_05_011 crossref_primary_10_3390_diagnostics11112133 crossref_primary_10_1038_s41377_021_00590_x crossref_primary_10_3390_ijms242216353 crossref_primary_10_3389_fnagi_2023_1266859 crossref_primary_10_3389_fphar_2025_1588375 crossref_primary_10_1371_journal_pbio_3001358 crossref_primary_10_1016_j_nano_2022_102563 crossref_primary_10_1016_j_nbd_2016_03_006 crossref_primary_10_1080_17435390_2017_1342011 crossref_primary_10_1016_j_biopha_2023_115656 crossref_primary_10_1016_j_cclet_2025_111628 crossref_primary_10_1039_C7AN01904A crossref_primary_10_1016_j_arr_2024_102599 crossref_primary_10_3390_antiox9080649 crossref_primary_10_1002_jbio_202000303 crossref_primary_10_1016_j_carbpol_2024_121815 crossref_primary_10_1016_j_cca_2019_07_037 crossref_primary_10_1038_s41377_023_01191_6 crossref_primary_10_3390_ijms22031206 crossref_primary_10_1007_s11011_025_01587_w crossref_primary_10_1038_s41598_024_59165_6 crossref_primary_10_1039_C6AN01797E crossref_primary_10_3390_cells10082127 crossref_primary_10_1016_j_desal_2025_119243 crossref_primary_10_3389_fnins_2022_823741 crossref_primary_10_3390_ijms25105317 crossref_primary_10_1021_jacs_3c08854 crossref_primary_10_3390_photonics4020032 crossref_primary_10_1016_j_saa_2018_12_054 crossref_primary_10_1016_j_heliyon_2025_e42111 crossref_primary_10_1186_s40478_020_01091_5 crossref_primary_10_1038_s41467_019_09111_2 crossref_primary_10_3389_fncel_2023_1223912 crossref_primary_10_1016_j_bbrc_2025_152583 crossref_primary_10_3390_biom10081099 crossref_primary_10_1016_j_pneurobio_2024_102572 crossref_primary_10_1016_j_bbagen_2024_130688 crossref_primary_10_1038_s41598_020_62708_2 crossref_primary_10_3390_ijms232012631 crossref_primary_10_1177_13872877251319553 crossref_primary_10_1111_febs_16344 crossref_primary_10_1186_s40478_021_01259_7 |
| ContentType | Journal Article |
| DBID | CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1021/ac502667b |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic |
| 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: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | no_fulltext_linktorsrc |
| Discipline | Engineering Chemistry |
| EISSN | 1520-6882 |
| ExternalDocumentID | 25415602 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GroupedDBID | --- -DZ -~X .DC .K2 23M 4.4 53G 55A 5GY 5RE 5VS 6J9 7~N 85S AABXI AAHBH ABBLG ABHFT ABHMW ABJNI ABLBI ABMVS ABOCM ABPPZ ABQRX ABUCX ACBEA ACGFO ACGFS ACGOD ACIWK ACJ ACKOT ACNCT ACPRK ACS ADHLV AEESW AENEX AFEFF AFRAH AGXLV AHGAQ ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH BKOMP CGR CS3 CUPRZ CUY CVF D0L EBS ECM ED~ EIF EJD F5P GGK GNL IH9 IHE JG~ KZ1 LG6 LMP NPM P2P PQQKQ ROL RXW TAE TN5 UHB UI2 UKR VF5 VG9 W1F WH7 X6Y XSW YZZ ZCA ~02 7X8 |
| ID | FETCH-LOGICAL-a510t-95e68ba841eba50d8b95d1689a978a3fca0d0790a781381c83cd944ccad106f32 |
| IEDL.DBID | 7X8 |
| ISICitedReferencesCount | 95 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000346683900021&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 1520-6882 |
| IngestDate | Thu Oct 02 09:43:02 EDT 2025 Mon Jul 21 05:49:56 EDT 2025 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 24 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-a510t-95e68ba841eba50d8b95d1689a978a3fca0d0790a781381c83cd944ccad106f32 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | https://zenodo.org/record/3424006 |
| PMID | 25415602 |
| PQID | 1637558682 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_1637558682 pubmed_primary_25415602 |
| PublicationCentury | 2000 |
| PublicationDate | 2014-12-16 |
| PublicationDateYYYYMMDD | 2014-12-16 |
| PublicationDate_xml | – month: 12 year: 2014 text: 2014-12-16 day: 16 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Analytical chemistry (Washington) |
| PublicationTitleAlternate | Anal Chem |
| PublicationYear | 2014 |
| SSID | ssj0011016 |
| Score | 2.4845216 |
| Snippet | Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the... |
| SourceID | proquest pubmed |
| SourceType | Aggregation Database Index Database |
| StartPage | 12047 |
| SubjectTerms | Alzheimer Disease - pathology Brain Chemistry Humans Immunohistochemistry - instrumentation Immunohistochemistry - methods Lipids - chemistry Oxidation-Reduction Plaque, Amyloid - chemistry Spectroscopy, Fourier Transform Infrared |
| Title | Microspectroscopy (μFTIR) reveals co-localization of lipid oxidation and amyloid plaques in human Alzheimer disease brains |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/25415602 https://www.proquest.com/docview/1637558682 |
| Volume | 86 |
| WOSCitedRecordID | wos000346683900021&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3LSsNAFB3UCurC96O-GMGFLkLzzmQlpVgUbClSobswr2CgTWJTxcev-Q1-k3cmCXUjCG6yCCQMNzdzz5k7cw5C54xDEXABuVHXNw3XlpbBiOsYjBMo5iRmDtMirndBv09Go3BQLbgV1bbKek7UE7XIuFojbwFuCDyP-MS-yp8M5RqluquVhcYiajgAZVRWB6N5F0ExU62XqigSQMlaWci2WpR7wD78gP2OLHWF6W78d2ybaL3ClrhdJsMWWpDpNlrp1JZu22jth_rgDvroqc14-qilkrTM8jd88fXZHd7eX2Il7ASJiXlm6GpXndbEWYzHSZ4InL0mpRsTpqnAdAK8H-7mY6rGjZMUa_M_3B6_P8pkIqe46gRhpjwpil300L0edm6MyovBoPDXzozQkz5hlLiWZNQzBWGhJyyfhBRoKHViTk1hBqFJA2IBCODE4SJ0XcgPAaQzduw9tJRmqTxAGKJFGTVdpqT2gQFRLiwBLJNwbsILrCY6q6McQXxUA4OmMnsuonmcm2i__FRRXopyREB01aFw-_APTx-hVcA9Wq_R8o9RI4aAyhO0zF9mSTE91UkE1_6g9w33btPr |
| linkProvider | ProQuest |
| 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=Microspectroscopy+%28%CE%BCFTIR%29+reveals+co-localization+of+lipid+oxidation+and+amyloid+plaques+in+human+Alzheimer+disease+brains&rft.jtitle=Analytical+chemistry+%28Washington%29&rft.au=Benseny-Cases%2C+N%C3%BAria&rft.au=Klementieva%2C+Oxana&rft.au=Cotte%2C+Marine&rft.au=Ferrer%2C+Isidre&rft.date=2014-12-16&rft.eissn=1520-6882&rft.volume=86&rft.issue=24&rft.spage=12047&rft_id=info:doi/10.1021%2Fac502667b&rft_id=info%3Apmid%2F25415602&rft_id=info%3Apmid%2F25415602&rft.externalDocID=25415602 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1520-6882&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1520-6882&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1520-6882&client=summon |