PubMed · 7383118
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P J Spagnuolo. 1980-07-31. Complement-induced granulocyte aggregation.. https://doi.org/10.1056/nejm198007313030518
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A fused-silica capillary high-performance liquid chromatography column (i.d. 0.25 mm) packed with octadecylsilane-bonded silica has been used on-line with continuous-flow negative-ion fast-atom bombardment (FAB) mass spectrometry for the separation and structural analysis of series of fatty acids and arachidonic acid metabolites derivatized with 4-aminobenzenesulphonic acid. Negative-ion FAB spectra of the derivatized lipids showed strong [M-H] pseudomolecular ions. Collision-induced dissociation of these anions produced structurally informative daughter ions, arising from charge-remote fragmentations.
The mechanism responsible for the rapid increase of thromboxane A2 synthesis by cells of the human monoblastoid cell line U937, which were differentiated with 12-O-tetradecanoyl-phorbol-13-acetate, induced by lipopolysaccharide (LPS) was studied. Both RNA blot and immunoblot analyses showed that LPS increased the levels of prostaglandin endoperoxide synthase-1 (PES-1) and -2 (PES-2) in a time-dependent manner, and the modes of induction of the two isozymes differed. The maximum PES-1 mRNA level was 1.6 times higher 36 h after than before stimulation by LPS, and that of PES-2 mRNA was elevated about 20-fold at its peak at 12 h after stimulation. Consequently, the immunoreactive PES-1 and PES-2 protein levels also increased time-dependently after LPS stimulation. However, the effects of LPS on the thromboxane synthase mRNA and protein levels were much less marked. These results indicate that LPS-induced thromboxane synthesis by the differentiated cells was regulated at the levels of the two PES isozymes, predominantly at the PES-2 level.