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• W1973509519 endingPage "219" @default.
• W1973509519 startingPage "215" @default.
• W1973509519 abstract "As serum amyloid A (SAA), an apolipoprotein associated with HDL during the acute‐phase reaction may induce Ca 2+ mobilization in human monocytes we raised the question whether SAA 1 the predominant isoform of human acute‐phase SAA is able to alter eicosanoid formation. In resting monocytes SAA 1 was without effect on the secretion of cyclooxygenase metabolites while in calcium ionophore A 23187 ‐ (0.5 and 2.5 μM) stimulated cells SAA 1 led to a pronounced dose‐dependent increase of TXA 2 , PGE 2 , and PGF 2α . In addition a time‐dependent increase of cyclooxygenase metabolites in between 1.5‐ and 3‐fold in the presence of SAA 1 was observed; apo A‐I, the main HDL‐apolipoprotein under non‐acute‐phase conditions, had no effect. Using sequence‐specific anti‐human SAA 1 peptide (40–63) F(ab) 2 fragments we could show that the proposed Ca 2+ ‐binding tetrapeptide Gly 48 ‐Pro 49 ‐Gly 50 ‐Gly 51 of SAA 1 is not responsible for enhanced biosynthesis of cyclooxygenase metabolites. Finally, we could demonstrate that human SAA 1 is unable to bind Ca 2+ ‐ions, suggesting that SAA 1 does not directly enhance eicosanoid biosynthesis via Ca 2+ mobilization leading to enhanced phospholipase A 2 activity." @default.
• W1973509519 created "2016-06-24" @default.
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• W1973509519 date "1997-12-15" @default.
• W1973509519 modified "2023-10-02" @default.
• W1973509519 title "Serum amyloid A (SAA) protein enhances formation of cyclooxygenase metabolites of activated human monocytes" @default.
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• W1973509519 doi "https://doi.org/10.1016/s0014-5793(97)01459-2" @default.
• W1973509519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9428637" @default.
• W1973509519 hasPublicationYear "1997" @default.
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