Expression in Escherichia coli, phosphorylation with cAMP-dependent protein kinase and proteolysis by calpain of a 71-kDa domain of human endothelial actin binding protein

Biochem Biophys Res Commun. 1997 Mar 17;232(2):555-8. doi: 10.1006/bbrc.1997.6238.


A middle region of human endothelial actin-binding protein (ABP) was subcloned and expressed in the pT7-7/E. coli BL21 (DE3) system. As predicted by the amino acid sequence this 71 kD truncated protein (residues 1717-2360) contained a calpain cleavage site and two of the three presumptive cAMP-dependent protein kinase phosphorylation sites. This peptide fragment comprised all the elements needed to confer stability against calpain proteolysis to ABP after PKA phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Calpain / physiology*
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism*
  • Cloning, Molecular
  • Cyclic AMP-Dependent Protein Kinases / physiology*
  • Escherichia coli / genetics*
  • Genetic Vectors
  • Humans
  • Hydrolysis
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / genetics*
  • Microfilament Proteins / metabolism*
  • Molecular Weight
  • Peptide Fragments / metabolism
  • Phosphorylation
  • Protein Structure, Tertiary


  • Carrier Proteins
  • F-actin-binding proteins
  • Microfilament Proteins
  • Peptide Fragments
  • Cyclic AMP-Dependent Protein Kinases
  • Calpain