The BMP type II receptor is located in lipid rafts, including caveolae, of pulmonary endothelium in vivo and in vitro.

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  • Author(s): Ramos M;Ramos M; Lamé MW; Segall HJ; Wilson DW
  • Source:
    Vascular pharmacology [Vascul Pharmacol] 2006 Jan; Vol. 44 (1), pp. 50-9. Date of Electronic Publication: 2005 Nov 03.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Science Country of Publication: United States NLM ID: 101130615 Publication Model: Print-Electronic Cited Medium: Print ISSN: 1537-1891 (Print) Linking ISSN: 15371891 NLM ISO Abbreviation: Vascul Pharmacol Subsets: MEDLINE
    • Publication Information:
      Original Publication: New York, NY : Elsevier Science, c2002-
    • Subject Terms:
      Bone Morphogenetic Protein Receptors, Type II/*analysis ; Caveolae/*metabolism ; Endothelium, Vascular/*metabolism ; Lung/*blood supply; Adult ; Animals ; Caveolin 1/analysis ; Cell Line ; Child, Preschool ; Endothelium, Vascular/ultrastructure ; Female ; Golgi Apparatus/metabolism ; Humans ; Lung/ultrastructure ; Male ; Membrane Microdomains/metabolism ; Rats ; Rats, Sprague-Dawley
    • Abstract:
      Polymorphic mutations in the Bone Morphogenetic Protein type II receptor (BMPrII) gene have been implicated in the development of familial primary pulmonary hypertension (PPH) however, the role BMPrII mutations play in the development of PH has not yet been elucidated. Endothelial caveolae are an important domain of hemodynamics containing eNOS, the serotonin transporter, and endothelin receptors. In this study we show by standard immunohistochemistry (IHC) that BMPrII is widely distributed in the vasculature of the rat lung, and more specifically distributed to both apical and basal membranes of the arteriolar endothelium by fluorescent IHC. We also examined compartmentalization of BMPrII in lipid fractions of plasma membranes isolated by silica based extraction from human pulmonary artery endothelial cells and rat lung endothelium. Density gradient centrifugation demonstrated BMPrII in separate caveolin-1 (cav-1) and non-cav-1 lipid rich fractions. Electron microscopy co-localized cav-1 and BMPrII in flask shaped membrane fragments. Three-dimensional fluorescence microscopy demonstrated BMPrII in discrete membrane foci, a portion of which were co-localized with cav-1, as well as in Golgi. Our findings indicate that BMPrII is located within lipid-dense fractions of pulmonary endothelial cell membranes with a portion present in caveolae suggesting potential dynamic regulatory structural relationships.
    • Grant Information:
      ESO7055 United States ES NIEHS NIH HHS; HL48411 United States HL NHLBI NIH HHS
    • Accession Number:
      0 (Caveolin 1)
      EC 2.7.11.30 (Bmpr2 protein, rat)
      EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type II)
    • Publication Date:
      Date Created: 20051108 Date Completed: 20060425 Latest Revision: 20120625
    • Publication Date:
      20231215
    • Accession Number:
      10.1016/j.vph.2005.09.007
    • Accession Number:
      16271518