Intracellular β-Thymosins

  • Ewald Hannappel
  • Thomas Huff
  • Daniel Safer
Chapter
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

The β-thymosins are a family of highly conserved polar peptides consisting of 40 to 44 amino acid residues. All β-thymosins bind monomeric G-actin in a 1:1 complex. The dissociation constant of the complex is in the micromolar range and allows for fast binding and release of G-actin. Because of the high intracellular concentration of β-thymosins (up to 500 µM) in most vertebrate cells, β-thymosins are considered the main intracellular G-actin sequestering peptides. Thymosin β4 binds to G-actin in an extended conformation, and folds into a stable conformation upon binding. The N- and C-termini of thymosin β4 contact the barbed and pointed ends of the monomeric actin. Thymosin β4 is present in the nucleus as well as the cytoplasm and might be responsible for sequestering nuclear actin. Even minor cell damage might be responsible for the release of β-thymosins detectable in the extracellular fluids. Extracellular β-thymosins affect matrix metallo-proteinases, chemotaxis, angiogenesis and wound healing. However, only very little is known about the molecular mechanisms mediating the effects attributed to extracellular β-thymosins.

Keywords

Actin Polymerization Sodium Lauryl Sulfate Actin Monomer Post Column Derivatization Nuclear Actin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Landes Bioscience and Springer Science+Business Media 2007

Authors and Affiliations

  • Ewald Hannappel
    • 1
  • Thomas Huff
    • 1
  • Daniel Safer
    • 2
  1. 1.Institute of Biochemistry, Faculty of MedicineUniversity of Erlangen-NurembergErlangenGermany
  2. 2.Pennsylvania Muscle Institute Department of PhysiologyUniversity of Pennsylvania School of MedicinePhiladelphiaUSA

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