@article{oai:teapot.lib.ocha.ac.jp:00034661,
 author = {Kobayashi, Tetsuyuki and Murakami-Murofushi, Kimiko},
 issue = {1},
 journal = {お茶の水女子大學自然科學報告},
 month = {Jun},
 note = {application/pdf, 紀要論文, Cyclic phosphatidic acid (cPA) possessing phosphate at sn-2 and -3 positions of glycerol is a unique analog of lysophosphatidic acid (LPA). The biosynthesis and functions of cPA as a novel lipid mediator have been studied. The biosynthetic enzyme activity of cPA was detected in sera from rat, bovine and human using lysophosphatidylcholine as a substrate. The reaction is considered to be catalyzed by a phospholipase D -like enzyme. The naturally occurring cPA and some of their analogs showed a variety of biological activities. cPA showed an inhibitory effect on cdc25 phosphatase in vitro, while no effect on activities of cdks. It was also shown that dephosphorylated (active) form of cdk2 decreased when cPA was added into cultures of human fibroblast cells caused a decrease in dephosphorylated (active) form of cdk2. These results suggested that suppression of cell proliferation by cPA is caused by the inhibition of cdc25 phosphatase. LPA induced tumor cell invasion, whereas cPA suppressed the LPA-induced invasion. cPA containing C16:0 was most potent in inhibiting tumor cell invasion (transcellular migration) in an i\
n vitro system as compared with other molecular. These findings support the idea that cPA is formed as a physiological constituent, and functions as one of the bioactive lipids in mammalian cells.},
 pages = {45--48},
 title = {Biological Functions of a Novel Lipid Mediator, Cyclic Phosphatidic Acid (cPA)},
 volume = {53},
 year = {2002}
}