PubMed HealthSearch

PubMed · 1745063

No relationship between the age-related decrease in prostacyclin production and the level of intracellular lipid peroxidation in human umbilical vein endothelial cells in culture.

Abstract

Some investigators have speculated that a decrease in prostacyclin production observed during ageing of endothelial cells is caused by an increase in intracellular lipid peroxide. We checked this speculation using an in vitro model to study the ageing of human vascular endothelial cells. For this purpose we determined the levels of intracellular lipid peroxide of endothelial cells at various culture ages, and found that the level of intracellular lipid peroxidation did not increase during in vitro ageing. Amounts of intracellular lipid peroxide also differed depending on the growth phase, the addition of heparin and the strain of endothelial cells, but the cells producing prostacyclin at a low level did not necessarily contain larger amounts of intracellular lipid peroxide. Therefore, we postulate that the age-related decrease in prostacyclin production is not due to an increase in the amount of intracellular lipid peroxide as a function of age.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

N Hasegawa, K Yamamoto. 1991. No relationship between the age-related decrease in prostacyclin production and the level of intracellular lipid peroxidation in human umbilical vein endothelial cells in culture.. https://doi.org/10.1016/0047-6374(91)90107-b

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.

Protein tyrosine phosphorylation cascades are difficult to analyze and are critical for cell signaling in higher eukaryotes. Methodology for profiling tyrosine phosphorylation, considered herein as the assignment of multiple protein tyrosine phosphorylation sites in single analyses, was reported recently (Salomon, A. R.; Ficarro, S. B.; Brill, L. M.; Brinker, A.; Phung, Q. T.; Ericson, C.; Sauer, K.; Brock, A.; Horn, D. M.; Schultz, P. G.; Peters, E. C. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 443-448). The technology platform included the use of immunoprecipitation, immobilized metal affinity chromatography (IMAC), liquid chromatography, and tandem mass spectrometry. In the present report, we show that when using complex mixtures of peptides from human cells, methylation improved the selectivity of IMAC for phosphopeptides and eliminated the acidic bias that occurred with unmethylated peptides. The IMAC procedure was significantly improved by desalting methylated peptides, followed by gradient elution of the peptides to a larger IMAC column. These improvements resulted in assignment of approximately 3-fold more tyrosine phosphorylation sites, from human cell lysates, than the previous methodology. Nearly 70 tyrosine-phosphorylated peptides from proteins in human T cells were assigned in single analyses. These proteins had unknown functions or were associated with a plethora of fundamental cellular processes. This robust technology platform should be broadly applicable to profiling the dynamics of tyrosine phosphorylation.

Cells, Cultured