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Title: Fatty acyl delta 6 desaturation activity of cultured human endothelial cells. Modulation by fetal bovine serum. Author: Rosenthal MD, Whitehurst MC. Journal: Biochim Biophys Acta; 1983 Mar 01; 750(3):490-6. PubMed ID: 6297606. Abstract: Human endothelial cells from umbilical vein actively desaturate [14C]linoleate and synthesize icosatrienoate, arachidonate and docosatetraenoate. Desaturation and chain elongation of 9,12,15-[14 C]linolenate (n - 3) by these cells is more extensive than that of [14 C]linoleate. Both confluent primary monolayers and subconfluent subcultures exhibit greater fatty acyl CoA delta 6-desaturase activity when growth and incubation media contain 2.5% fetal bovine serum instead of 10%. Prior growth with 20% serum diminishes the extent of subsequent linoleate desaturation. Use of medium supplemented with 20-100 microM oleate results in up to 67% inhibition of [14 C]arachidonate synthesis. These results indicate that, despite previously published reports to the contrary, human vascular endothelial cells are similar to other normal mammalian cells in having fatty acyl delta 6-desaturase activity. Suppression of endogenous arachidonate synthesis by elevated levels of serum lipids may impair endothelial cell function.[Abstract] [Full Text] [Related] [New Search]