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- W1551032425 abstract "Pyruvate carboxylase (PC) catalyzes oxaloacetate (OAA) synthesis and ostensibly links gluconeogenesis and fatty acid (FA) metabolism. Previous work in our laboratory demonstrates activation of bovine PC mRNA in Madin-Darby bovine kidney (MDBK) cells in response to a PPAR agonist but a decrease with saturated FA. Our objective was to determine effects of chain length and degree of saturation through copresence of saturated and unsaturated FA on PC mRNA. Cells at 80% confluence were exposed to either individual FA bound to BSA (C16:0, C18:0, C18:1n-9 cis or C18:3n-3 cis) or FA cocktails in 25:75, 50:50 or 75:25 for combinations of C16:0: C18:3n-3 cis or C18:0: C18:3n-3 cis or C18:1n-9 cis: C18:3n-3 cis. Total FA concentration was 1 mM. Both C16:0 and C18:0 independently decreased (P < 0.05) PC mRNA (0.70, 0.18, 2.53 ± 0.41; C16:0, C18:0, control, respectively). The ratio of 25:75 C18:3n-3 cis: C18:0 increased PC expression compared to C18:0 (1.97, 0.18 ± 0.41; P < 0.05) but only 75:25 C18:3n-3 cis: C16:0 could recover PC expression to levels similar to control (1.55, 2.53 ± 0.41; P > 0.1). Results indicate that C18:3n-3 cis is a more potent alleviator of PC depression in C18:0 treated cells compared to C16:0: C18:3n-3 cis treatments. C18:1n-9 cis treatments did not depress PC (P > 0.10), revealing FA saturation is key in PC expression. PC activation by unsaturated FA may play a critical role in setting the capacity for OAA synthesis." @default.
- W1551032425 created "2016-06-24" @default.
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- W1551032425 date "2014-04-01" @default.
- W1551032425 modified "2023-10-14" @default.
- W1551032425 title "Fatty acid chain length and degree of saturation regulate expression of pyruvate carboxylase in Madin‐Darby bovine kidney cells (821.9)" @default.
- W1551032425 doi "https://doi.org/10.1096/fasebj.28.1_supplement.821.9" @default.
- W1551032425 hasPublicationYear "2014" @default.
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