liu.seSearch for publications in DiVA
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Efficient imaging of amyloid deposits in Drosophila models of human amyloidoses
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi. Linköpings universitet, Tekniska fakulteten.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Organisk Kemi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0002-5582-140X
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Utvecklingsbiologi. Linköpings universitet, Hälsouniversitetet.ORCID-id: 0000-0001-5095-541X
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0001-5827-3587
2010 (engelsk)Inngår i: Nature Protocols, ISSN 1754-2189, E-ISSN 1750-2799, Vol. 5, nr 5, s. 935-944Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Drosophila melanogaster is emerging as an important model system for neurodegenerative disease research. In this protocol, we describe an efficient method for imaging amyloid deposits in the Drosophila brain, by the use of a luminescent-conjugated oligothiophene (lco), p-Ftaa polymer probe. We also demonstrate the feasibility of co-staining with antibodies and compare the lco staining with standard amyloid-specific probes. the lco protocol enables high-resolution imaging of several different protein aggregates, such as aβ1-42, aβ1-42e22G, transthyretin V30M and human tau, in the Drosophila brain. aβ and tau aggregates could also be distinguished from each other because of distinct lco emission spectra. Furthermore, this protocol enables threedimensional brain mapping of amyloid distribution in whole-mount Drosophila brains. the use of p-Ftaa combined with other probes, antibodies and/or dyes will aid the rapid characterization of various amyloid deposits in the rapidly growing number of Drosophila models of neurodegenerative diseases.

sted, utgiver, år, opplag, sider
Macmillan Publishers Ltd., 2010. Vol. 5, nr 5, s. 935-944
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-55024DOI: 10.1038/nprot.2010.41ISI: 000277174100012OAI: oai:DiVA.org:liu-55024DiVA, id: diva2:314356
Tilgjengelig fra: 2010-04-27 Laget: 2010-04-27 Sist oppdatert: 2018-04-25bibliografisk kontrollert
Inngår i avhandling
1. Modeling Amyloid Disease in Drosophila melanogaster
Åpne denne publikasjonen i ny fane eller vindu >>Modeling Amyloid Disease in Drosophila melanogaster
2010 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Amyloid diseases are caused by protein misfolding and aggregation. To date there are 27 known proteins causing amyloid disorders involving brain and peripheral protein deposition. The proteins involved in this mechanism do not share sequence homology, but the amyloid fibrils share biophysical properties and possibly a common pathogenic mechanism. Amyloid deposits are known to be involved in a broad range of neurodegenerative diseases, such as Alzheimer’s disease and Creutzfeldt-Jakob disease, as well as in non-neuropathic diseases, such as senile systemic amyloidosis and type II diabetes.

During the last decade the fruit fly, Drosophila melanogaster (Drosophila), have increasingly been used as a model for neurodegenerative disease, such as Alzheimer’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and familial amyloidotic polyneuropathy. The advantages of using the Drosophila model are the well-defined genetic characteristics, the quantity, short life span, simplicity in genetic manipulation and the powerful binary UAS-Gal4 transgenic system. The UAS-Gal4 system allows for rapid generation of individual strains in which expression of a specific gene of interest can be directed to different tissues or cell types. The system allows the target gene to be activated in different cell- and tissue-types by altering the activator-expressing lines.

This thesis has been focused on modeling amyloid diseases in Drosophila. This has been performed by:

  • Creating new model systems of senile systemic amyloidosis and familial amyloidotic polyneuropathy in Drosophila
  • Developing a new staining protocol for detection of amyloid in Drosophila
  • Initiate a compound screen of Alzheimer’s disease modeled in Drosophila
sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2010. s. 88
Serie
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1320
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-55025 (URN)978-91-7393-379-7 (ISBN)
Disputas
2010-05-21, Planck, Fysikhuset, Campus Valla, Linköpings universitet, Linköping, 09:15 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2010-04-27 Laget: 2010-04-27 Sist oppdatert: 2018-04-25bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekst

Personposter BETA

Berg, InaNilsson, PeterThor, StefanHammarström, Per

Søk i DiVA

Av forfatter/redaktør
Berg, InaNilsson, PeterThor, StefanHammarström, Per
Av organisasjonen
I samme tidsskrift
Nature Protocols

Søk utenfor DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric

doi
urn-nbn
Totalt: 479 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf