2. Pechova A, Pavlata L. Chromium as an essential nutrient: a review. Vet Med (Praha) 2007; 52:1
5. Lien TF, Wu CP, Wang BJ, et al. Effect of supplemental levels of chromium picolinate on the growth performance, serum traits, carcass characteristics and lipid metabolism of growing-finishing pigs. Anim Sci 2001; 72:289–96.
https://doi.org/10.1017/S1357729800055788
6. US Food and Drug Administration. CFR-code of federal regulations title 21 Part 556 tolerances for residues of new animal drugs in food. Rockville, MD, USA: US Food and Drug Administration; 2017.
7. Spears JW. Chromium supplementation in cattle diets. In : Florida Rumint Nutrion Symphosium; Gainesville, FL, USA. 2010. p. 143–55.
18. Janovick-Guretzky N, Dann H, Carlson D, Murphy M, Loor J, Drackley J. Housekeeping gene expression in bovine liver is affected by physiological state, feed intake, and dietary treatment. J Dairy Sci 2007; 90:2246–52.
https://doi.org/10.3168/jds.2006-640
19. Spears JW, Whisnant CS, Huntington GB, et al. Chromium propionate enhances insulin sensitivity in growing cattle. J Dairy Sci 2012; 95:2037–45.
https://doi.org/10.3168/jds.2011-4845
22. Anderson RA, Bryden NA, Evock-Clover CM, Steele NC. Beneficial effects of chromium on glucose and lipid variables in control and somatotropin-treated pigs are associated with increased tissue chromium and altered tissue copper, iron, and zinc. J Anim Sci 1997; 75:657–61.
https://doi.org/10.2527/1997.753657x
23. Kanai F, Ito K, Todaka M, et al. Insulin-stimulated GLUT4 translocation is relevant to the phosphorylation of IRS-1 and the activity of PI3 kinase. Biochem Biophys Res Commun 1993; 195:762–8.
https://doi.org/10.1006/bbrc.1993.2111
31. Smith S, Lin K, Wilson J, Lunt D, Cross H. Starvation depresses acylglycerol biosynthesis in bovine subcutaneous but not intramuscular adipose tissue homogenates. Comp Biochem Physiol B Biochem Mol Biol 1998; 120:165–74.
https://doi.org/10.1016/S0305-0491(98)10005-6
34. Park H, Kaushik VK, Constant S, et al. Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise. J Biol Chem 2002; 277:32571–7.
https://doi.org/10.1074/jbc.M201692200
35. Kelly M, Keller C, Avilucea PR, et al. AMPK activity is diminished in tissues of IL-6 knockout mice: the effect of exercise. Biochem Biophys Res Commun 2004; 320:449–54.
https://doi.org/10.1016/j.bbrc.2004.05.188
37. Sakoda H, Ogihara T, Anai M, et al. Activation of AMPK is essential for AICAR-induced glucose uptake by skeletal muscle but not adipocytes. Am J Physiol Endocrinol Metab 2002; 282:E1239–E44.
https://doi.org/10.1152/ajpendo.00455.2001
38. Salt IP, Connell JM, Gould GW. 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) inhibits insulin-stimulated glucose transport in 3T3-L1 adipocytes. Diabetes 2000; 49:1649–56.
https://doi.org/10.2337/diabetes.49.10.1649
40. Hawley SA, Davison M, Woods A, et al. Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J Biol Chem 1996; 271:27879–87.
https://doi.org/10.1074/jbc.271.44.27879