Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi


  • Yong-Hun LeeEmail author
  • William SchiemannEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_565


 BM-90;  DANCE;  EFEMP1;  EFEMP2;  EVEC;  H411;  Hemicentin;  Him4;  MBP1;  S15;  T16;  TM14;  UP50;  UPH1

Historical Background

The extracellular matrix (ECM) is very diverse in its nature and composition in vertebrates, and is essential for normal development and maintenance of the microenvironment of embryonic and adult tissues. Many ECM proteins are secreted into extracellular milieu where they aggregate with existing matrix molecules to form supramolecular structures. The functions of the ECM include supporting cells, regulating intercellular communication, controlling cell motility, growth, and development, overseeing wound healing, and directing fibrosis (Albig and Schiemann 2005; de Vega et al. 2009; Timpl et al. 2003). These ECM proteins have been classified into several families based on their domain structures and/or functions, with fibulins now being recognized as one such family of ECM molecules. Fibulins share a common structural organization with tandem repeats...

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  1. Albig AR, Schiemann WP. Fibulin-5 function during tumorigenesis. Future Oncol. 2005;1(1):23–35.PubMedPubMedCentralCrossRefGoogle Scholar
  2. Albig AR, Neil JR, Schiemann WP. Fibulins 3 and 5 antagonize tumor angiogenesis in vivo. Cancer Res. 2006;66(5):2621–9.PubMedPubMedCentralCrossRefGoogle Scholar
  3. Argraves WS, Greene LM, Cooley MA, Gallagher WM. Fibulins: physiological and disease perspectives. EMBO Rep. 2003;4(12):1127–31.PubMedPubMedCentralCrossRefGoogle Scholar
  4. de Vega S, Iwamoto T, Yamada Y. Fibulins: multiple roles in matrix structures and tissue functions. Cell Mol Life Sci. 2009;66(11–12):1890–902.PubMedPubMedCentralCrossRefGoogle Scholar
  5. Gallagher WM, Currid CA, Whelan LC. Fibulins and cancer: friend or foe? Trends Mol Med. 2005;11(7):336–40.PubMedPubMedCentralCrossRefGoogle Scholar
  6. Lee YH, Albig AR, Regner M, Schiemann BJ, Schiemann WP. Fibulin-5 initiates epithelial-mesenchymal transition (EMT) and enhances EMT induced by TGF-beta in mammary epithelial cells via a MMP-dependent mechanism. Carcinogenesis. 2008;29(12):2243–51.PubMedPubMedCentralCrossRefGoogle Scholar
  7. Tian M, Schiemann WP. The TGF-beta paradox in human cancer: an update. Future Oncol. 2009;5(2):259–71.PubMedPubMedCentralCrossRefGoogle Scholar
  8. Timpl R, Sasaki T, Kostka G, Chu ML. Fibulins: a versatile family of extracellular matrix proteins. Nat Rev Mol Cell Biol. 2003;4(6):479–89.PubMedPubMedCentralCrossRefGoogle Scholar
  9. Wendt MK, Allington TM, Schiemann WP. Mechanisms of the epithelial-mesenchymal transition by TGF-beta. Future Oncol. 2009;5(8):1145–68.PubMedPubMedCentralCrossRefGoogle Scholar
  10. Yanagisawa H, Davis EC. Unraveling the mechanism of elastic fiber assembly: the roles of short fibulins. Int J Biochem Cell Biol. 2010;42(7):1084–93.PubMedPubMedCentralCrossRefGoogle Scholar
  11. Yanagisawa H, Schluterman MK, Brekken RA. Fibulin-5, an integrin-binding matricellular protein: its function in development and disease. J Cell Commun Signal. 2009;3(3–4):337–47.PubMedPubMedCentralCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Case Comprehensive Cancer CenterCase Western Reserve UniversityClevelandUSA