umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
1915-Pos 195 Pt Nmr: Interactions Of The Cancer Drug Cis-platin With Membranes And Mgst1, A Integral Membrane Detoxification Protein
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Show others and affiliations
2008 (English)In: Biophysical Journal, 2008, 1915- p.Conference paper, Published paper (Other academic)
Abstract [en]

The microsomal Glutathione-transferase (MGST1) is an integral membrane protein, which catalyses the conjugation of glutathione (tripeptide GSH) with xenobiotics; a process essential for cells to remove and detoxify e. g. carcinogens. While this glutathione system plays an essential role in healthy cell survival, glutathione has been shown to have a pivotal role in the development of acquired drug resistance. It prevents successful chemotherapies against a range of cancer types, therapies often based on cisplatin based drugs. These Pt compounds are initially quite effective, they become non-effective e.g. during the treatment of prostate cancer (very common 10000 new cases/a in Sweden) which progresses into a non-curable form during therapy. To understand the molecular mechanism behind the activity of Pt drugs and their inhibition by the human defense system, we use an solid state NMR approach (complemented by liquid NMR) to elucidate for cis-platin (diamino-dichloroplatinat II):

conversion of cis-platin complex into an diamino-diaqua-complex, essential for its membrane passage into the cell interior.

lipid membrane - drug interactions: binding to cell membrane surface, solubility and membrane transport.

Pt drug binding to MGST1 enzyme, followed by glutathione conjugation into more water soluble compounds.

Place, publisher, year, edition, pages
2008. 1915- p.
Identifiers
URN: urn:nbn:se:umu:diva-11186OAI: oai:DiVA.org:umu-11186DiVA: diva2:150857
Note
Biophysical Journal 94:1915 (2008)Available from: 2009-01-22 Created: 2009-01-22 Last updated: 2011-03-30Bibliographically approved

Open Access in DiVA

No full text

Other links

http://www.biophysj.org/cgi/content/meeting_abstract/94/1_MeetingAbstracts/1915?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&author1=gr%F6bner%2C+g&searchid=1&FIRSTINDEX=0&fdate=1/1/2008&resourcetype=HWCIT

Search in DiVA

By author/editor
Wallgren, MarcusSchleucher, JürgenGröbner, Gerhard
By organisation
Department of ChemistryDepartment of Medical Biochemistry and Biophysics

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 105 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf