Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins.

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  • Additional Information
    • Source:
      Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print Cited Medium: Print ISSN: 0014-5793 (Print) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
    • Publication Information:
      Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
      Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
    • Subject Terms:
      Heparan Sulfate Proteoglycans*; Calcium-Binding Proteins/*metabolism ; Carrier Proteins/*metabolism ; Extracellular Matrix Proteins/*metabolism ; Membrane Glycoproteins/*metabolism ; Tropoelastin/*metabolism; Animals ; Aorta/metabolism ; Cell Adhesion Molecules ; Dose-Response Relationship, Drug ; Heparitin Sulfate/metabolism ; Humans ; Immunohistochemistry ; Mice ; Protein Binding ; Proteoglycans/metabolism ; Recombinant Proteins/metabolism ; Serum Albumin/metabolism ; Surface Plasmon Resonance ; Time Factors
    • Abstract:
      Elastic fibers in vessel walls and other tissues consist of cross-linked tropoelastin in association with several microfibrillar proteins. In order to understand the molecular basis of these structures, we examined the binding of recombinant human tropoelastin to other extracellular matrix ligands in solid phase binding and surface plasmon resonance assays. These studies demonstrated a particularly high affinity (K(d) about 1 nM) of tropoelastin for microfibrillar fibulin-2 and the recently described nidogen-2 isoform. More moderate affinities were observed for fibulin-1, laminin-1 and perlecan, while several other ligands such as collagens, nidogen-1, fibronectin and BM-40 showed little or no binding. In immunogold staining of mouse aortic media, elastic fibers were heavily decorated with tropoelastin, fibulin-2 and nidogen-2, while the reaction with fibulin-1 was lower. The colocalization of these proteins emphasizes the potential for in vivo interactions.
    • Grant Information:
      HL 56401 United States HL NHLBI NIH HHS
    • Accession Number:
      0 (Calcium-Binding Proteins)
      0 (Carrier Proteins)
      0 (Cell Adhesion Molecules)
      0 (Extracellular Matrix Proteins)
      0 (Heparan Sulfate Proteoglycans)
      0 (Membrane Glycoproteins)
      0 (NID2 protein, human)
      0 (Proteoglycans)
      0 (Recombinant Proteins)
      0 (Serum Albumin)
      0 (Tropoelastin)
      0 (fibulin)
      143972-95-6 (perlecan)
      9050-30-0 (Heparitin Sulfate)
    • Publication Date:
      Date Created: 19991102 Date Completed: 19991210 Latest Revision: 20190621
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/s0014-5793(99)01362-9
    • Accession Number:
      10544250