oru.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
Role of phosphoinositide 3OH-kinase in autocrine transformation by PDGF-BB
Department of Genetics and Pathology, The Rudbeck Laboratory, Uppsala University, Sweden.
Department of Genetics and Pathology, The Rudbeck Laboratory, Uppsala University, Sweden.
Department of Genetics and Pathology, The Rudbeck Laboratory, Uppsala University, Sweden.ORCID iD: 0000-0001-8889-5803
2001 (English)In: Journal of Cellular Physiology, ISSN 0021-9541, E-ISSN 1097-4652, Vol. 188, no 3, p. 369-382Article in journal (Refereed) Published
Abstract [en]

Phosphoinositide 3OH-kinases (PI3K) are a family of lipid kinases that activates signalling pathways important for migration, cytoskeletal rearrangements, and cell survival. These processes are important hallmarks in transformation. We have evaluated the functional role of PI3K for development of a transformed morphology and migratory responses of murine fibroblasts (NIH/sis and COL1A1/NIH3T3 cell lines) stimulated in an autocrine fashion by constitutive expression of platelet-derived growth factor-BB (PDGF-BB). We show that prolonged treatment with the specific PI3K inhibitor LY294002, induced a reversion of the transformed morphology, and prevented density-independent growth and focus formation. Functional PI3K was also required for development of the transformed morphology of NIH/sis and COL1A1/NIH3T3. Furthermore, treatment with LY294002 completely perturbed random migration of the cells. In addition our data show that, in the signalling pathways downstream of PI3K, activation of the small GTPase Rac was a prerequisite for the transformation signal. Our data also indicate the presence of a suramin-insensitive PI3K activity. Most likely this was due to the presence of a suramin-insensitive intracellular PDGFR pool that allowed activation of PI3K located in intracellular compartments. In conclusion these data show that intact PI3K activity was required for the morphological alterations and the enhanced migratory response that are hallmarks for PDGF induced autocrine transformation.

Place, publisher, year, edition, pages
Wiley-Blackwell Publishing Inc., 2001. Vol. 188, no 3, p. 369-382
National Category
Medical and Health Sciences Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-79056DOI: 10.1002/jcp.1126ISI: 000170325400011PubMedID: 11473364Scopus ID: 2-s2.0-0034888532OAI: oai:DiVA.org:oru-79056DiVA, id: diva2:1386263
Funder
Swedish Cancer Society, 3219-B99-06xABSwedish Cancer Society, 4255-B99-01PAA
Note

Contract grant sponsor: Swedish Cancer Society; Contract grant numbers: 3219-B99-06xAB, 4255-B99-01PAA.

Available from: 2013-10-17 Created: 2020-01-17 Last updated: 2020-01-28Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records BETA

Nånberg, Eewa

Search in DiVA

By author/editor
Nånberg, Eewa
In the same journal
Journal of Cellular Physiology
Medical and Health SciencesCell and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 27 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