uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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
Heparan sulfate in trans potentiates VEGFR-mediated angiogenesis
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Show others and affiliations
2006 (English)In: Developmental Cell, ISSN 1534-5807, E-ISSN 1878-1551, Vol. 10, no 5, 625-634 p.Article in journal (Refereed) Published
Abstract [en]

Several receptor tyrosine kinases require heparan sulfate proteoglycans (HSPGs) as coreceptors for efficient signal transduction. We have studied the role of HSPGs in the development of blood capillary structures from embryonic stem cells, a process strictly dependent on signaling via vascular endothelial growth factor receptor-2 (VEGFR-2). We show, by using chimeric cultures of embryonic stem cells defective in either HS production or VEGFR-2 synthesis, that VEGF signaling in endothelial cells is fully supported by HS expressed in trans by adjacent perivascular smooth muscle cells. Transactivation of VEGFR-2 leads to prolonged and enhanced signal transduction due to HS-dependent trapping of the active VEGFR-2 signaling complex. Our data imply that direct signaling via HSPG core proteins is dispensable for a functional VEGF response in endothelial cells. We propose that transactivation of tyrosine kinase receptors by HSPGs constitutes a mechanism for crosstalk between adjacent cells.

Place, publisher, year, edition, pages
2006. Vol. 10, no 5, 625-634 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-22534ISI: 000237648800012PubMedID: 16678777OAI: oai:DiVA.org:uu-22534DiVA: diva2:50307
Available from: 2007-04-16 Created: 2007-04-16 Last updated: 2017-12-07

Open Access in DiVA

No full text

Other links

PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=16678777&dopt=Citation

Authority records BETA

Jakobsson, LarsKreuger, JohanHolmborn, KatarinaEriksson, IngerKjellén, LenaClaesson-Welsh, Lena

Search in DiVA

By author/editor
Jakobsson, LarsKreuger, JohanHolmborn, KatarinaEriksson, IngerKjellén, LenaClaesson-Welsh, Lena
By organisation
Department of Genetics and PathologyDepartment of Medical Biochemistry and Microbiology
In the same journal
Developmental Cell
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric score

pubmed
urn-nbn
Total: 1211 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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