[Phospholipase D in mammalian cells: structure, properties, physiological and pathological role].
Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of glycerophospholipid phosphatidylcholine to generate phosphatidic acid (PA) and choline. Phosphatidic acid is widely considered to be the intracellular lipid mediator of many biological functions. PA is a precursor of many other bioactive lipids, including diacylglycerol (DAG) and lysophosphatidic acid (LPA). Phospholipase D activities have been described in multiple organisms, including bacteria, yeast, plants, and mammals. In mammalian cells, PLD (PLD1 and PLD2 isoenzymes) has been implicated in intracellular signal transduction, vesicle transport, endocytosis, exocytosis, cell migration, mitosis, and cytoskeletal reorganization. Mammalian phospholipase D is regulated by many factors, including phosphatidylinositol-4,5-bisphosphate (PIP2), protein kinase C (PKC), and small G-proteins of the Rho, Ral, and ARF families. In this review we discuss the relationships of PLD1 and PLD2, their structure, biological function, and implications in pathological states.
Szumiło
Maria
M
Katedra i Zakład Biochemii Akademii Medycznej w Warszawie. mszumilo@amwaw.edu.pl
Rahden-Staroń
Iwonna
I
D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D010739:Phospholipase D / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
C105606:phospholipase D2; D010739:Phospholipase D; C106801:phospholipase D1