Diadenosine polyphosphate-mediated activation of phospholipase D in isolated rat liver cells.
Diadenosine polyphosphates (ApnAs) can, through interaction with appropriate purinoceptors, affect a range of cellular activities. Ap4A, the most prominent naturally occurring diadenosine polyphosphate, stimulates alterations in intracellular calcium homeostasis and subsequent activation of glycogen breakdown in isolated liver cells. Here we show that Ap4A, and other naturally occurring diadenosine polyphosphates, also stimulates phospholipase D (PLD) activity in isolated rat liver cells. The characteristics of Ap4A-mediated activation of PLD are similar to those for the activation of PLD by extracellular ATP. These results are discussed in the context of the relation between diadenosine polyphosphate- and adenine mononucleotide-mediated cellular signalling processes.
Edgecombe
M
M
Department of Biochemistry, University of Liverpool, UK.
Eckersley
S P
SP
McLennan
A G
AG
Fisher
M J
MJ
D000818:Animals; D002478:Cells, Cultured; D015226:Dinucleoside Phosphates / Q000378:metabolism* / Q000494:pharmacology; D004789:Enzyme Activation; D020404:Glycerophospholipids / Q000378:metabolism; D008099:Liver / Q000166:cytology; D008297:Male; D010739:Phospholipase D / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
D015226:Dinucleoside Phosphates; D020404:Glycerophospholipids; C051521:phosphatidylethanol; C020733:diadenosine tetraphosphate; D010739:Phospholipase D