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Fatty acid chain length and degree of saturation regulate expression of pyruvate carboxylase in Madin‐Darby bovine kidney cells (821.9)
Author(s) -
Boesche Katherine,
Koser Stephanie,
Donkin Shawn
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.821.9
Subject(s) - pyruvate carboxylase , chemistry , fatty acid , microbiology and biotechnology , messenger rna , gluconeogenesis , biochemistry , metabolism , medicine , biology , gene , enzyme
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.