Abstract
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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Calpain / physiology*
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism*
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Cloning, Molecular
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Cyclic AMP-Dependent Protein Kinases / physiology*
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Escherichia coli / genetics*
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Genetic Vectors
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Humans
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Hydrolysis
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics*
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Microfilament Proteins / metabolism*
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Molecular Weight
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Peptide Fragments / metabolism
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Phosphorylation
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Protein Structure, Tertiary
Substances
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Carrier Proteins
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F-actin-binding proteins
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Microfilament Proteins
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Peptide Fragments
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Cyclic AMP-Dependent Protein Kinases
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Calpain