Calpain proteolysis of insulin-like growth factor binding protein (IGFBP) -2 and -3, but not of IGFBP-1.
BIOLOGICAL CHEMISTRY(2007)
Abstract
Calpains are cytoplasmic Ca(2+)-regulated cysteine proteases that may regulate insulin-like growth factor (IGF)-independent actions of insulin-like growth factor binding proteins (IGFBPs) through IGFBP proteolysis. In this study, [(125)I]-labeled IGFBP-2 and -3, but not IGFBP-1, were proteolyzed by Ca(2+)-activated m-calpain in vitro. Degradation of higher concentrations of the recombinant proteins IGFBP-2 and -3 by m-calpain was dose-dependent, but was terminated within 20 min by autolysis. By subjecting proteolytic fragments to N-terminal amino acid sequence analysis, the primary cleavage sites in IGFBP-2 and -3 were localized to the non-conserved central linker regions. Using the biosensor technique, in vitro binding of m-calpain to IGFBP-3 was demonstrated to be a Ca(2+)-dependent reaction with a rapid on/off rate.
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Key words
biosensor analysis,Ca2+ activation,cleavage site,fragmentation,kinetics,protease
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