We present a case of a 57-year-old woman with an unremarkable medical history except for a continuous cardiac murmur at the left second and third interspaces. Transthoracic echocardiography revealed an unusual chamber in front of the heart. To evaluate the precise anatomy of this abnormality, multi-slice computed tomographic (MSCT) imaging was performed. MSCT angiography with retrospective ECG gating showed a coronary arterial malformation with fistulous communications to the coronary artery, pulmonary artery and the root of aorta. Images from MSCT coronary angiography can be helpful in understanding the tortuous configuration of the coronary arterial malformation.

The aim of this study was to investigate the effect of fasting on in vivo plasma levels of lysophosphatidic acid (LPA), a physiologically important lysophospholipid mediator. We assayed to measure activities of an LPA-producing enzyme (lysophospholipase D) and LPA-degrading enzyme activities (lysophspholipase A, lipid phosphate phosphatase) in rat plasma or blood, by measuring choline, fatty acid and inorganic phosphate, respectively. Both LPA and its precursor lysophosphatidylcholine (LPC) were quantified by liquid chromatography-tandem mass spectrometry. Fasting of rats for 24 h decreased plasma concentrations of oleoyl-, linoleoyl-, arachidonoyl-and docosahexaenoyl-LPAs, but not palmitoyl-and stearoyl-LPAs, possibly due to decreased levels of corresponding LPCs in the plasma and elevated lipid phosphate phosphatase activity for LPAs in the blood. Our results indicate that the in vivo circulating levels of LPAs in rats are affected by fasting.Key words autotaxin; lysophospholipase D; lysophosphatidylcholine; lysophospholipase A; lipid phosphate phosphatase; plasma Lysophosphatidic acid (LPA) is well-known as the first lipidic intermediate of the de novo synthetic pathway for glycero phospholipids. Increasing interest is currently being directed toward its extracellular actions through at least six specific G-protein coupled receptors.1) Both circulating and local levels of LPA are regulated tightly by LPA-producing enzymes, LPA-degrading enzymes and LPA-binding proteins.2,3) Both abnormal production and degradation of LPA are assumed to be relevant to pathophysiological conditions of human such as cancer metastasis, 4) atherosclerosis, 5) organ fibrosis 6) and pain. 7) Although LPA-producing enzymatic activity in human plasma and bovine fetal serum was demonstrated to be largely due to autotaxin (ATX), 8,9) physiological regulation of the circulating LPA level is not yet well understood. 3,10) In this study, we focused our inquiry on whether the stress of nutritional restriction affected the in vivo plasma level and molecular species composition of LPA using quantifying lysophosphatidylcholine (LPC) and LPA by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and its mechanism by comparing LPA-producing and -degrading enzymatic activities during 12 and 24 h fasting. MATERIALS AND METHODSLysophospholipids Fatty acyl moieties of lysophospholipids are designated in terms of the combined number of carbon atoms : the combined number of double bonds. Palmitoyl (16 : 0)-, heptadecanoyl (17 : 0)-and linoleoyl (18 : 2)-LPCs were purchased from Avanti Polar Lipids (Alabaster, AL, U.S.A.). LPA having a heptadecanoyl group was prepared as described previously. 11)Animals Control male Wistar rats (9 wks old) were freely fed a standard chow (Japan SLC, Shizuoka, Japan) until experiments, whereas test rats of the same age were subjected to fasting for 12 h or 24 h. For blood collection, fasted and non-fasted rats were anesthetized with diethyl ether and blood was withdrawn from a catheter inserted into an abdominal a...

No abstract

No abstract

No abstract