Ontogeny of adropin and its receptor expression during postnatal development and its pro-gonadal role in the ovary of pre-pubertal mouse. | Ontogeny of adropin and its receptor expression during postnatal development and its pro-gonadal role in the ovary of pre-pubertal mouse. Maurya S, Tripathi S, Singh A. | 11/8/2023 |
Adropin attenuates pancreatitis-associated lung injury through PPARgamma phosphorylation-related macrophage polarization. | Adropin attenuates pancreatitis‑associated lung injury through PPARγ phosphorylation‑related macrophage polarization. Ding F, Liu G, Gao F, Zheng Z, Hong Y, Chen Y, Weng S., Free PMC Article | 09/21/2023 |
Selective deficiency of UCP-1 and adropin may lead to different subtypes of anti-neutrophil cytoplasmic antibody-associated vasculitis. | Selective deficiency of UCP-1 and adropin may lead to different subtypes of anti-neutrophil cytoplasmic antibody-associated vasculitis. Chen Q, Li Y, Guo X, Liu Y, Guo Y, Lv X, Lin Y, Liu Q. | 02/24/2023 |
Adropin Improves Radiation-Induced Myocardial Injury via VEGFR2/PI3K/Akt Pathway. | Adropin Improves Radiation-Induced Myocardial Injury via VEGFR2/PI3K/Akt Pathway. Li B, Wang Z, He Y, Chen T, Zhang Y, Yuan X, Li P., Free PMC Article | 08/13/2022 |
Aerobic Exercise Restores Aging-Associated Reductions in Arterial Adropin Levels and Improves Adropin-Induced Nitric Oxide-Dependent Vasorelaxation. | Aerobic Exercise Restores Aging-Associated Reductions in Arterial Adropin Levels and Improves Adropin-Induced Nitric Oxide-Dependent Vasorelaxation. Fujie S, Hasegawa N, Horii N, Uchida M, Sanada K, Hamaoka T, Padilla J, Martinez-Lemus LA, Maeda S, Iemitsu M., Free PMC Article | 10/30/2021 |
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., Free PMC Article | 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 |