Abstract:
:The addition of 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to peroxisomes decreased the production of acid-soluble radioactivity formed by beta-oxidation of [1-(14)C]arachidonate due to substrate removal by esterification into the acceptor. This peroxisomal-associated acyl-CoA:1-acyl-GPC acyltransferase activity was due to microsomal contamination. The production of acid-soluble radioactivity from [1-(14)C]7,10,13,16-22:4, but not from [3-(14)C]7,10,13,16-22:4 was independent of 1-acyl-GPC, with and without microsomes. By comparing rates of peroxisomal beta-oxidation with those for microsomal acylation, it was shown that the preferred metabolic fate of arachidonate, when added directly to incubations, or generated via beta-oxidation, was esterification by microsomal 1-acyl-GPC acyltransferase, rather than continued peroxisomal beta-oxidation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Baykousheva SP,Luthria DL,Sprecher Hdoi
10.1016/0014-5793(95)00565-qsubject
Has Abstractpub_date
1995-06-26 00:00:00pages
198-200issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(95)00565-Qjournal_volume
367pub_type
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