首页   按字顺浏览 期刊浏览 卷期浏览 Regulation of lysophosphatidylcholine-metabolizing enzymes in isolated myocardial cells...
Regulation of lysophosphatidylcholine-metabolizing enzymes in isolated myocardial cells from rat heart

 

作者: David L. Severson,   Thea Fletcher,  

 

期刊: Canadian Journal of Physiology and Pharmacology  (NRC Available online 1985)
卷期: Volume 63, issue 8  

页码: 944-951

 

ISSN:0008-4212

 

年代: 1985

 

DOI:10.1139/y85-156

 

出版商: NRC Research Press

 

数据来源: NRC

 

摘要:

Enzymatic pathways involved in the metabolism of lysophosphatidylcholine were investigated in rat heart myocardial cells. Acyl CoA-dependent acyltransferase activity was localized in microsomes, and was much greater than lysophospholipase activity in either cytosolic or microsomal fractions. The cytosolic lysophospholipase was more sensitive to inhibition by palmitylcarnitine in comparison to free fatty acids. In contrast, free fatty acids (oleate and palmitate) produced a greater inhibition of the microsomal acyltransferase and lysophospholipase than did palmitylcarnitine. A reduction in the assay pH to 6.5 resulted in an increase in microsomal acyltransferase and cytosolic lysophospholipase activities, but brought about a marked reduction in the microsomal lysophospholipase activity. At pH 6.5, the percentage inhibition of the microsomal acyltransferase by palmitylcarnitine was reduced, whereas the inhibition by palmitic acid was enhanced. The inhibition of the microsomal lysophospholipase by both palmitylcarnitine and palmitic acid was reduced at pH 6.5. With respect to myocardial ischemia, the inhibition of microsomal acyltransferase by free fatty acids and the reduction in microsomal lysophospholipase activity due to acidosis may contribute to the elevation of cellular lysophosphoglycerides which are arrhythmogenic.

 

点击下载:  PDF (1629KB)



返 回