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    Enho energy homeostasis associated [ Mus musculus (house mouse) ]

    Gene ID: 69638, updated on 23-Jun-2021

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Lower adropin expression is associated with oxidative stress and severity of nonalcoholic fatty liver disease.

    Lower adropin expression is associated with oxidative stress and severity of nonalcoholic fatty liver disease.
    Chen X, Sun X, Shen T, Chen Q, Chen S, Pang J, Mi J, Tang Y, You Y, Xu H, Ling W.

    05/29/2021
    Exercise suppresses NLRP3 inflammasome activation in mice with diet-induced NASH: a plausible role of adropin.

    Exercise suppresses NLRP3 inflammasome activation in mice with diet-induced NASH: a plausible role of adropin.
    Yang W, Liu L, Wei Y, Fang C, Liu S, Zhou F, Li Y, Zhao G, Guo Z, Luo Y, Li L.

    05/15/2021
    Adropin regulates hepatic glucose production via PP2A/AMPK pathway in insulin-resistant hepatocytes.

    Adropin regulates hepatic glucose production via PP2A/AMPK pathway in insulin-resistant hepatocytes.
    Chen X, Chen S, Shen T, Yang W, Chen Q, Zhang P, You Y, Sun X, Xu H, Tang Y, Mi J, Yang Y, Ling W.

    02/27/2021
    Hepatocyte expression of the micropeptide adropin regulates the liver fasting response and is enhanced by caloric restriction.

    Hepatocyte expression of the micropeptide adropin regulates the liver fasting response and is enhanced by caloric restriction.
    Banerjee S, Ghoshal S, Stevens JR, McCommis KS, Gao S, Castro-Sepulveda M, Mizgier ML, Girardet C, Kumar KG, Galgani JE, Niehoff ML, Farr SA, Zhang J, Butler AA.,

    02/6/2021
    Adropin reduced lipid accumulation as well as expression of proadipogenic genes in 3T3-L1 cells and rat preadipocytes, suggesting that this protein attenuates differentiation of preadipocytes into mature fat cells. In summary, these results show that adropin modulates proliferation and differentiation of preadipocytes.

    Effects of adropin on proliferation and differentiation of 3T3-L1 cells and rat primary preadipocytes.
    Jasaszwili M, Wojciechowicz T, Billert M, Strowski MZ, Nowak KW, Skrzypski M.

    05/30/2020
    The Adropin(34-76) directly affected liver metabolism, decreasing glucose production and reducing PKA-mediated phosphorylation in primary mouse hepatocytes in vitro Our findings indicate that major hepatic signaling pathways contribute to the improved glycemic control achieved with adropin(34-76) treatment in situations of obesity.

    The peptide hormone adropin regulates signal transduction pathways controlling hepatic glucose metabolism in a mouse model of diet-induced obesity.
    Gao S, Ghoshal S, Zhang L, Stevens JR, McCommis KS, Finck BN, Lopaschuk GD, Butler AA., Free PMC Article

    04/4/2020
    Adropin prevents atherosclerosis development by suppressing monocyte-endothelial cell adhesion and smooth muscle cell proliferation.

    Adropin Contributes to Anti-Atherosclerosis by Suppressing Monocyte-Endothelial Cell Adhesion and Smooth Muscle Cell Proliferation.
    Sato K, Yamashita T, Shirai R, Shibata K, Okano T, Yamaguchi M, Mori Y, Hirano T, Watanabe T., Free PMC Article

    09/15/2018
    An inverse correlation between serum adropin levels and mouse age that was attenuated by calorie restriction.

    Effects of Chronic and Intermittent Calorie Restriction on Adropin Levels in Breast Cancer.
    Tuna BG, Atalay PB, Altunbek M, Kalkan BM, Dogan S.

    06/30/2018
    our data suggest that adropin is a membrane-bound protein that interacts with the brain-specific Notch1 ligand NB3.

    Adropin is a brain membrane-bound protein regulating physical activity via the NB-3/Notch signaling pathway in mice.
    Wong CM, Wang Y, Lee JT, Huang Z, Wu D, Xu A, Lam KS., Free PMC Article

    02/21/2015
    these results suggest a role for adropin in regulating muscle substrate preference under various nutritional states.

    Regulation of substrate oxidation preferences in muscle by the peptide hormone adropin.
    Gao S, McMillan RP, Jacas J, Zhu Q, Li X, Kumar GK, Casals N, Hegardt FG, Robbins PD, Lopaschuk GD, Hulver MW, Butler AA, Gao S, McMillan RP, Jacas J, Zhu Q, Li X, Kumar GK, Casals N, Hegardt FG, Robbins PD, Lopaschuk GD, Hulver MW, Butler AA., Free PMC Articles: PMC4171656, PMC4171656

    11/22/2014
    Release of adropin in the fed condition regulates fuel selection in skeletal muscle, promoting glucose oxidation over fat oxidation. The molecular mechanisms of adropin's effects involve acetylation (suggesting inhibition) of the transcriptional co-activator PGC1alpha, reducing PDK4 and CPT1B activity. Increased PGC1alpha acetylation by adropin may be mediated by inhibiting Sirtuin-1 (SIRT1), a PGC1alpha deacetylase.

    Regulation of substrate oxidation preferences in muscle by the peptide hormone adropin.
    Gao S, McMillan RP, Jacas J, Zhu Q, Li X, Kumar GK, Casals N, Hegardt FG, Robbins PD, Lopaschuk GD, Hulver MW, Butler AA, Gao S, McMillan RP, Jacas J, Zhu Q, Li X, Kumar GK, Casals N, Hegardt FG, Robbins PD, Lopaschuk GD, Hulver MW, Butler AA., Free PMC Articles: PMC4171656, PMC4171656

    07/7/2014
    a potential endothelial protective role of adropin that is likely mediated via upregulation of endothelial NO synthase expression through the VEGFR2-phosphatidylinositol 3-kinase-Akt and VEGFR2-extracellular signal regulated kinase 1/2 pathways.

    Adropin is a novel regulator of endothelial function.
    Lovren F, Pan Y, Quan A, Singh KK, Shukla PC, Gupta M, Al-Omran M, Teoh H, Verma S, Lovren F, Pan Y, Quan A, Singh KK, Shukla PC, Gupta M, Al-Omran M, Teoh H, Verma S.

    10/4/2010
    Adropin has an endothelial protective function mediated via upregulation of eNOS expression through the VEGFR2-PI3K-Akt and VEGFR2-ERK1/2 pathways. Adropin therapy may thus be useful for limiting diseases characterized by endothelial dysfunction.

    Adropin is a novel regulator of endothelial function.
    Lovren F, Pan Y, Quan A, Singh KK, Shukla PC, Gupta M, Al-Omran M, Teoh H, Verma S, Lovren F, Pan Y, Quan A, Singh KK, Shukla PC, Gupta M, Al-Omran M, Teoh H, Verma S.

    09/30/2010
    Adropin regulated expression of hepatic lipogenic genes and adipose tissue peroxisome proliferator-activated receptor gamma, a major regulator of lipogenesis.

    Identification of adropin as a secreted factor linking dietary macronutrient intake with energy homeostasis and lipid metabolism.
    Kumar KG, Trevaskis JL, Lam DD, Sutton GM, Koza RA, Chouljenko VN, Kousoulas KG, Rogers PM, Kesterson RA, Thearle M, Ferrante AW Jr, Mynatt RL, Burris TP, Dong JZ, Halem HA, Culler MD, Heisler LK, Stephens JM, Butler AA, Kumar KG, Trevaskis JL, Lam DD, Sutton GM, Koza RA, Chouljenko VN, Kousoulas KG, Rogers PM, Kesterson RA, Thearle M, Ferrante AW Jr, Mynatt RL, Burris TP, Dong JZ, Halem HA, Culler MD, Heisler LK, Stephens JM, Butler AA., Free PMC Articles: PMC2746325, PMC2746325

    01/21/2010
    Adropin is the name given to the secreted peptide encoded by human C9orf165. In mice, it is abundant in liver where it is regulated by dietary macronutrients. Adropin regulates expression of genes involved in lipogenesis and adipogenesis.

    Identification of adropin as a secreted factor linking dietary macronutrient intake with energy homeostasis and lipid metabolism.
    Kumar KG, Trevaskis JL, Lam DD, Sutton GM, Koza RA, Chouljenko VN, Kousoulas KG, Rogers PM, Kesterson RA, Thearle M, Ferrante AW Jr, Mynatt RL, Burris TP, Dong JZ, Halem HA, Culler MD, Heisler LK, Stephens JM, Butler AA, Kumar KG, Trevaskis JL, Lam DD, Sutton GM, Koza RA, Chouljenko VN, Kousoulas KG, Rogers PM, Kesterson RA, Thearle M, Ferrante AW Jr, Mynatt RL, Burris TP, Dong JZ, Halem HA, Culler MD, Heisler LK, Stephens JM, Butler AA., Free PMC Articles: PMC2746325, PMC2746325

    12/4/2008
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