The first draft of the endostatin interaction network

J Biol Chem. 2009 Aug 14;284(33):22041-7. doi: 10.1074/jbc.M109.002964. Epub 2009 Jun 19.

Abstract

Endostatin is a C-terminal proteolytic fragment of collagen XVIII that is localized in vascular basement membrane zones in various organs. It binds to heparin/heparan sulfate and to a number of proteins, but its molecular mechanisms of action are not fully elucidated. We have used surface plasmon resonance (SPR) arrays to identify new partners of endostatin, and to give further insights on its molecular mechanism of action. New partners of endostatin include glycosaminoglycans (chondroitin and dermatan sulfate), matricellular proteins (thrombospondin-1 and SPARC), collagens (I, IV, and VI), the amyloid peptide Abeta-(1-42), and transglutaminase-2. The biological functions of the endostatin network involve a number of extracellular proteins containing epidermal growth factor and epidermal growth factor-like domains, and able to bind calcium. Depending on the trigger event, and on the availability of its members in a given tissue at a given time, the endostatin network might be involved either in the control of angiogenesis, and tumor growth, or in neurogenesis and neurodegenerative diseases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Databases, Protein
  • Endostatins / chemistry*
  • Epidermal Growth Factor / chemistry
  • Humans
  • Laminin / chemistry
  • Models, Biological
  • Neovascularization, Pathologic
  • Neurodegenerative Diseases / metabolism
  • Protein Binding
  • Protein Interaction Mapping*
  • Protein Structure, Tertiary
  • Surface Plasmon Resonance
  • Time Factors

Substances

  • Endostatins
  • Laminin
  • laminin 1
  • Epidermal Growth Factor