Inhibition of phospholipase A2 and phospholipase C by polyamines
AM Sechi, L Cabrini, L Landi, P Pasquali… - Archives of Biochemistry …, 1978 - Elsevier
AM Sechi, L Cabrini, L Landi, P Pasquali, G Lenaz
Archives of Biochemistry and Biophysics, 1978•ElsevierThe polyamines spermine, spermidine, and putrescine inhibit the activity of phospholipase A
2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and
mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is
highest for spermine and lowest for putrescine. With both enzymes, inhibition is stronger
when phospholipid vesicles rather than mitochondrial membranes are used as the
substrate. No clear competition of polyamines with Ca 2+, which is required for the activity of …
2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and
mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is
highest for spermine and lowest for putrescine. With both enzymes, inhibition is stronger
when phospholipid vesicles rather than mitochondrial membranes are used as the
substrate. No clear competition of polyamines with Ca 2+, which is required for the activity of …
Abstract
The polyamines spermine, spermidine, and putrescine inhibit the activity of phospholipase A2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is highest for spermine and lowest for putrescine. With both enzymes, inhibition is stronger when phospholipid vesicles rather than mitochondrial membranes are used as the substrate. No clear competition of polyamines with Ca2+, which is required for the activity of both enzymes, has been observed. The inhibition appears to be due to steric hindrance of enzyme-substrate interaction due to the binding of the organic polycations to the phospholipid bilayer.
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