Abstract
In this study we demonstrate that: (1) although the major phospholipase A2 present in sheep platelets is activated by calcium ions, it can effectively catalyze hydrolysis of the sn-2 ester linkage in phospholipids in the absence of calcium: (2) expression of calcium-independent phospholipase A2 activity can be induced by NACl utilizing purified (but not crude) cytosolic enzyme; and (3) calcium-independent phospholipase A2 activity is regulated by a reconstitutable cytosolic protein. Collectively, these results underscore the fundamental catalytic differences between extracellular and intracellular calcium-dependent phospholipases A2 and demonstrate that calcium is sufficient, but not necessary, for the activation of this class of intracellular phospholipases A2.
Original language | English |
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Pages (from-to) | 27-30 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 284 |
Issue number | 1 |
DOIs | |
State | Published - Jun 17 1991 |
Keywords
- Arachidonic acid
- Calcium
- Phospholipase A
- Plasmalogen
- Platelet