Detection, visualization and quantification of protein complexes in human Alzheimer's disease brains using proximity ligation assay.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
24 07 2023
Historique:
received: 06 03 2023
accepted: 30 06 2023
medline: 27 7 2023
pubmed: 25 7 2023
entrez: 24 7 2023
Statut: epublish

Résumé

Examination of healthy and diseased human brain is essential to translational neuroscience. Protein-protein interactions play a pivotal role in physiological and pathological processes, but their detection is difficult, especially in aged and fixed human brain tissue. We used the in-situ proximity ligation assay (PLA) to broaden the range of molecular interactions assessable in-situ in the human neuropathology. We adapted fluorescent in-situ PLA to detect ubiquitin-modified proteins in human brains with Alzheimer's disease (AD), including approaches for the management of autofluorescence and quantification using a high-content image analysis system. We confirmed that phosphorylated microtubule-associated protein tau (Serine202, Threonine205) aggregates were modified by ubiquitin and that phospho-tau-ubiquitin complexes were increased in hippocampal and frontal cortex regions in AD compared to non-AD brains. Overall, we refined PLA for use in human neuropathology, which has revealed a profound change in the distribution of ubiquitin in AD brain and its association with characteristic tau pathologies.

Identifiants

pubmed: 37488165
doi: 10.1038/s41598-023-38000-4
pii: 10.1038/s41598-023-38000-4
pmc: PMC10366145
doi:

Substances chimiques

tau Proteins 0
Ubiquitin 0
Ubiquitinated Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

11948

Subventions

Organisme : NIA NIH HHS
ID : R01 AG078803
Pays : United States
Organisme : NIA NIH HHS
ID : K76 AG060001
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR027396
Pays : United States

Commentaires et corrections

Type : UpdateOf

Informations de copyright

© 2023. The Author(s).

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Auteurs

Wilber Romero-Fernandez (W)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA. wilber.romero.fernandez@vumc.org.

Cristian Carvajal-Tapia (C)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.

Alex Prusky (A)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.

Ketaki A Katdare (KA)

Vanderbilt Brain Institute, Vanderbilt University, Nashville, TN, 37232, USA.

Emmeline Wang (E)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.

Alena Shostak (A)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.

Lissa Ventura-Antunes (L)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.

Hannah J Harmsen (HJ)

Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, 37240, USA.

Ethan S Lippmann (ES)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA.
Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN, 37235, USA.
Vanderbilt Memory and Alzheimer's Center, Vanderbilt University, Nashville, TN, 37235, USA.

Kjell Fuxe (K)

Department of Neuroscience, Karolinska Institute, Solna, 17177, Stockholm, Sweden.

Jason A MacGurn (JA)

Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN, 37240, USA.

Dasiel O Borroto-Escuela (DO)

Department of Neuroscience, Karolinska Institute, Solna, 17177, Stockholm, Sweden.
Receptomics and Brain Disorders Lab, Department of Human Physiology, Sport and Exercise, Faculty of Medicine, University of Malaga, Edificio Lopez-Penalver, Jimenez Fraud 10, 29071, Málaga, Spain.

Matthew S Schrag (MS)

Department of Neurology, Vanderbilt University Medical Center, MRBIII 465 21St Avenue S, Suite 6158, Nashville, TN, 37240, USA. matthew.schrag@vumc.org.
Vanderbilt Brain Institute, Vanderbilt University, Nashville, TN, 37232, USA. matthew.schrag@vumc.org.
Vanderbilt Memory and Alzheimer's Center, Vanderbilt University, Nashville, TN, 37235, USA. matthew.schrag@vumc.org.

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