Abstract
The Ca 2+-activated neutral protease can proteolyze both Ca 2+-dependent cyclic nucleotide phosphodiesterase and smooth muscle myosin light chain kinase. Ca 2+-dependent cyclic nucleotide phosphodiesterase from rat brain was converted to the Ca 2+-independent active form by Ca 2+-activated protease. The proteolytic effects on myosin light chain kinase of Ca 2+-activated protease differed in the presence and absence of the Ca 2+-calmodulin (CaM) complex. In the presence of bound CaM, myosin light chain kinase (130k dalton) was degradated to a major fragment of 62 kDa, which had Ca 2+ CaM -dependent enzyme and CaM-binding activity. When digestion occurred in the absence of bound CaM, myosin light chain kinase cleaved to a fragment of 60 kDa. This peptide had no enzymatic activity in the presence or absence of the Ca 2+-CaM complex. Available evidence suggests that the Ca 2+-activated proteases may recognize the conformational change of smooth muscle myosin light chain kinase induced by Ca 2+-CaM complex.
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