Abstract
This chapter presents an analysis of regulation of mammalian cytosolic Ca 2+ -requiring neutral proteinases. The presence of proteinases in the cytosol imposes a number of restrictions on their properties, including a requirement for significant activity at neutral pH, a high degree of specificity consistent with the known degradation rates for cytosolic proteins, and some form of metabolic control or regulation. These properties are found among the neutral Ca 2+ -requiring proteinases, which appear to be the most highly active of the cytosolic proteinases. In addition to the functions proposed for the brain and muscle enzymes, physiological roles have also been suggested for the Ca2+-dependent neutral proteinases from other tissues. The cytosolic fraction from rabbit liver contains three distinct proteinases that can be separated by gel filtration through a column of Ultrogel AcA34. The presence of endogenous inhibitors of Ca 2+ -activated proteinases has been demonstrated in muscle in human erythrocytes and also in rat liver. The cell surface receptors and binding proteins may be among the physiological substrates for these cytosolic enzymes.
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