Interaction of rat brain cytidylate cyclase with phospholipids.
The interaction of rat brain cytidylate cyclase with some phospholipids such as L-alpha-phosphatidylcholine (PC), L-alpha-phosphatidylserine (PS), L-alpha-phosphatidylethanolamine (PE) and L-alpha-phosphatidic acid (PA) was studied. Cytidylate cyclase activity of Triton X-100 - solubilized fraction was inhibited by PS, PE and PA, but not with PC. The addition of PC to the incubation mixture containing PS, PE or PA dose - dependently reversed the inhibition of enzyme activity by these phospholipids. Phospholipids showed similar effect on the intact membrane - bound enzyme. PC could reactivate the enzyme which was inactivated by deoxycholate treatment, suggesting that PC may be an important factor to reconstitute an active conformation of the enzyme. These findings indicate that cytidylate cyclase could be regulated by phospholipids constituting its microenvironment of the membrane.
Mori
S
S
Department of Immunochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Muto
N
N
Yamamoto
I
I
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D003563:Cyclic CMP / Q000378:metabolism*; D003597:Cytosine Nucleotides / Q000378:metabolism*; D066298:In Vitro Techniques; D008190:Lyases / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000494:pharmacology; D010743:Phospholipids / Q000378:metabolism*; D019761:Phosphorus-Oxygen Lyases; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D003597:Cytosine Nucleotides; D010713:Phosphatidylcholines; D010743:Phospholipids; D003563:Cyclic CMP; D008190:Lyases; D019761:Phosphorus-Oxygen Lyases; C019978:cytidylate cyclase