12S-lipoxygenase protein associates with α-actin fibers in human umbilical artery vascular smooth muscle cells

Gary Weisinger, Rona Limor, Yonit Marcus-Perlman, Esther Knoll, Fortune Kohen, Vera Schinder, Michael Firer, Naftali Stern

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4 Scopus citations


The current study sets out to characterize the intracellular localization of the platelet-type 12S-lipoxygenase (12-LO), an enzyme involved in angiotensin-II induced signaling in vascular smooth muscle cells (VSMC). Immunohistochemical analysis of VSMC in vitro or human umbilical arteries in vivo showed a clear cytoplasmic localization. On immunogold electron microscopy, 12-LO was found primarily associated with cytoplasmic VSMC muscle fibrils. Upon angiotensin-II treatment of cultured VSMC, immunoprecipitated 12-LO was found bound to α-actin, a component of the cytoplasmic myofilaments. 12-LO/α-actin binding was blocked by VSMC pretreatment with the 12-LO inhibitors, baicalien or esculetine and the protein synthesis inhibitor, cycloheximide. Moreover, the binding of 12-LO to α-actin was not associated with 12-LO serine or tyrosine phosphorylation. These observations suggest a previously unrecognized angiotensin-II dependent protein interaction in VSMC through which 12-LO protein may be trafficked, for yet undiscovered purposes towards the much more abundantly expressed cytoskeletal protein α-actin.

Original languageEnglish
Pages (from-to)554-560
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 11 May 2007


  • Actin
  • Angiotensin II
  • Arteries
  • Lipoxygenase
  • Protein-interaction
  • Vascular smooth muscle


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