Preferential hydrolysis of phosphatidylethanolamine in rat ischemic heart homogenates during in vitro incubation.
Phospholipid-hydrolyzing activities were examined in rat hearts with ischemia induced by occlusion of the left main coronary artery. When homogenates of ischemic heart were incubated in vitro at 37 degrees C, a significant amount of phosphatidylethanolamine (PE) was degraded, whereas the contents of other phospholipids did not change significantly. During the incubation, a stoichiometrical amount of lysoPE was concomitantly formed. The lysoPE formed had mainly saturated fatty acids and its composition resembled that of fatty acids detected at the sn-1 position in the glycerol backbone of heart PE. No appreciable PE degradation was observed in homogenates prepared from nonischemic rat heart. No difference in phospholipase activities was found between ischemic and nonischemic heart homogenates when exogenous radioactive phospholipids were used as substrates. Rabbit anti-rat 14-kDa type II phospholipase A2 antibody suppressed the degradation of PE observed in ischemic heart homogenates. These findings indicate that the type II phospholipase A2 activity may be involved in the breakdown of endogenous PE in ischemic heart homogenates.
Kikuchi-Yanoshita
R
R
Faculty of Pharmaceutical Sciences, University of Tokyo.
Yanoshita
R
R
Kudo
I
I
Arai
H
H
Takamura
T
T
Nomoto
K
K
Inoue
K
K
D000818:Animals; D006868:Hydrolysis; D066298:In Vitro Techniques; D008297:Male; D017202:Myocardial Ischemia / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D010743:Phospholipids / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar
D010714:Phosphatidylethanolamines; D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2