The Emerging Role of Adropin in Neurological Health: A Systematic Review
-
Rooban Sivakumar
,
Arul Senghor Kadalangudi Aravaanan
,
Vinodhini Vellore Mohanakrishnan
,
Janardhanan Kumar
Abstract
Background: Adropin, a peptide hormone has role in various various physiological processes, including metabolic regulation and cardiovascular health. This systematic review aimed to synthesize findings from observational studies on the involvement of adropin in neurological disorders and cognitive performance.
Methods: An extensive literature search was conducted across PubMed, Scopus, Web of Science, Embase, CORE, and Google Scholar using terms such as "adropin," "Neurological Disorders," "cognitive function," "Alzheimer's disease," "Parkinson's disease," "cognition," and "brain function." Studies published from 2020 to 2024 were selected and reviewed. The search and selection process adhered to the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) guidelines. Out of 127 screened articles, 5 met the inclusion criteria for this review.
Results: The combined research findings suggest a consistent link between decreased adropin levels and a range of neurological disorders and cognitive impairments. In particular, reduced adropin levels were seen in individuals with dementia, cognitive impairment, bipolar disorder, Parkinson's disease, and multiple sclerosis. These findings highlight adropin's potential role in modulating neurological health and cognitive function.
Conclusion: This systematic review underscores the importance of adropin in neurological health and its potential as a therapeutic agent. Based on the observed connections, adropin might serve as a new focus for treating neurological disorders, prompting the need for more research and trials.
1. Kumar KG, Trevaskis JL, Lam DD, et al (2008). Identification of adropin as a se-creted factor linking dietary macronu-trient intake with energy homeostasis and lipid metabolism. Cell Metab, 8(6):468-481.
2. Stein LM, Yosten GL, Samson WK (2016). Adropin acts in the brain to inhibit wa-ter drinking: potential interaction with the orphan G protein-coupled receptor, GPR19. Am J Physiol Regul Integr Comp Physiol, 310(6):R476-R480.
3. Gao S, McMillan RP, Zhu Q, et al (2015). Therapeutic effects of adropin on glu-cose tolerance and substrate utilization in diet-induced obese mice with insulin resistance. Mol Metab, 4(4):310-324.
4. Rooban S, Arul Senghor KA, Vinodhini VM, et al (2024). Adropin: A crucial regu-lator of cardiovascular health and met-abolic balance. Metabolism Open, 100299-100299.
5. Yosaee S, Soltani S, Sekhavati E, et al (2016). Adropin – A novel biomarker of heart disease: A systematic review article. Iran J Public Health, 45(12):1568-1576.
6. Kritsilis M, Rizou SV, Koutsoudaki PN, et al (2018). Ageing, cellular senescence and neurodegenerative disease. Int J Mol Sci, 19(10):2937.
7. Butler AA, St-Onge MP, Siebert EA, et al (2015). Differential responses of plasma adropin concentrations to dietary glu-cose or fructose consumption in hu-mans. Sci Rep, 5:14691.
8. Aggarwal G, Morley JE, Vellas B, et al (2024). Low circulating adropin concen-trations predict an increased risk of cognitive decline in community-dwelling older adults. Geroscience, 46(1):897-911.
9. Hayashi MA, Ducancel F, Konno K (2012). Natural peptides with potential applica-tions in drug development, diagnosis, and/or biotechnology. Int J Peptides, 2012:757838.
10. Elabadlah H, Hameed R, D'Souza C, et al (2020). Exogenous ghrelin increases plasma insulin levels in diabetic rats. Bi-omolecules, 10(4):633.
11. Adeghate E, Lotfy M, D'Souza C, et al (2020). Hypocretin/orexin modulates body weight and the metabolism of glu-cose and insulin. Diabetes Metab Syndr Obes, 36(3):e3229.
12. Adeghate E, Fernandez-Cabezudo M, Hameed R, et al (2010). Orexin-1 recep-tor co-localizes with pancreatic hor-mones in islet cells and modulates the outcome of streptozotocin-induced dia-betes mellitus. PLoS One, 5(1):e8587.
13. Mahgoub MO, D'Souza C, Al Darmaki RSMH, et al (2018). An update on the role of irisin in the regulation of endo-crine and metabolic functions. Peptides, 104:15-23.
14. Chen X, Chen S, Shen T, et al (2020). Adropin regulates hepatic glucose pro-duction via PP2A/AMPK pathway in in-sulin-resistant hepatocytes. FASEB J, 34(8):10056-10072.
15. Kuloglu T, Aydin S (2014). Immunohisto-chemical expressions of adropin and inducible nitric oxide synthase in renal tissues of rats with streptozotocin-induced experimental diabetes. Biotechnic Histochem, 89(2):104-110.
16. Levy OA, Malagelada C, Greene LA (2009). Cell death pathways in Parkinson's dis-ease: proximal triggers, distal effectors, and final steps. Apoptosis, 14(4):478-500.
17. Yang C, DeMars KM, Candelario-Jalil E (2018). Age-dependent decrease in adropin is associated with reduced lev-els of endothelial nitric oxide synthase and increased oxidative stress in the rat brain. Aging Dis, 9(2):322-330.
18. Yang C, Lavayen BP, Liu L, et al (2021). Neurovascular protection by adropin in experimental ischemic stroke through an endothelial nitric oxide synthase-dependent mechanism. Redox Biol, 48:102197.
19. Foster SR, Hauser AS, Vedel L, et al (2019). Discovery of human signaling systems: pairing peptides to G protein-coupled receptors. Cell, 179(4):895-908.
20. Wong CM, Wang Y, Lee JT, et al (2014). Adropin is a brain membrane-bound protein regulating physical activity via the NB-3/Notch signaling pathway in mice. J Biol Chem, 289(37):25976-25986.
21. Lovren F, Pan Y, Quan A, et al (2010). Adropin is a novel regulator of endothe-lial function. Circulation, 122(Suppl 11):S185-S192.
22. Wu L, Fang J, Yuan X, et al (2019). Adropin reduces hypoxia/reoxygenation-induced myocardial injury via the reperfusion in-jury salvage kinase pathway. Exp Ther Med, 18(5):3307-3314.
23. Shahjouei S, Ansari S, Pourmotabbed T, et al (2016). Potential roles of adropin in the central nervous system: review of current literature. Front Mol Biosci, 3:25.
24. Forstermann U, Munzel T (2006). Central role of eNOS in the maintenance of endothelial homeostasis. Antioxid Redox Signal, 22(14):1230-1242.
25. Zu L, Ren C, Pan B, et al (2016). Endotheli-al microparticles after antihypertensive and lipid-lowering therapy inhibit the adhesion of monocytes to endothelial cells. Int J Cardiol, 202:756-759.
26. Heiss C, Rodriguez-Mateos A, Kelm M (2015). Central role of eNOS in the maintenance of endothelial homeosta-sis. Antioxid Redox Signal, 22(14):1230-1242.
27. Thapa D, Stoner MW, Zhang M, et al (2018). Adropin regulates pyruvate dehy-drogenase in cardiac cells via a novel GPCR-MAPK-PDK4 signaling pathway. Redox Biol, 18:25-32.
28. Thibodeau A, Geng X, Previch LE, et al (2016). Pyruvate dehydrogenase complex in cerebral ischemia-reperfusion injury. Brain Circ, 2(2):61-66.
29. Patel MS, Nemeria NS, Furey W, et al (2014). The pyruvate dehydrogenase complexes: structure-based function and regulation. J Biol Chem, 289(24):16615-16623.
30. Zanotti S, Canalis E (2016). Notch signaling and the skeleton. Endocr Rev, 37(3):223-253.
31. Lai EC (2004). Notch signaling: control of cell communication and cell fate. Devel-opment, 131(5):965-973.
32. Banerjee S, Ghoshal S, Girardet C, et al (2021). Adropin correlates with aging-related neuropathology in humans and improves cognitive function in aging mice. npj Aging Mech Dis, 7:23.
33. Page MJ, McKenzie JE, Bossuyt PM, et al (2021). The PRISMA 2020 statement: an updated guideline for reporting system-atic reviews. BMJ, 372:n71.
34. Lo CKL, Mertz D, Loeb M (2014). Newcas-tle-Ottawa Scale: comparing reviewers' to authors' assessments. BMC Med Res Methodol, 14:45.
35. Stang A (2010). Critical evaluation of the Newcastle-Ottawa scale for the assess-ment of the quality of nonrandomized studies in meta-analyses. Eur J Epidemiol, 25:603-605.
36. Aggarwal G, Malmstrom TK, Morley JE, et al (2023). Low circulating adropin levels in late-middle aged African Americans with poor cognitive performance. NPJ Aging, 9(1).
37. Li X (2023). Serum adropin level as a pre-dictor of cognitive impairment in pa-tients. J Nat Sci Biol Med, 14:105-114.
38. Erşan S, Kurt A (2021). Evaluation of gluca-gon-like peptide-1, adropin, and desnu-trin levels, and related factors in pa-tients with bipolar disorder. Anatolian J Psychiatry, p. 1.
39. Lama MA, Uloom MT (2022). The role of adropin as a novel biomarker in Iraqi patients with Parkinson’s disease and os-teoporosis. Neuroquantology, 20(4):429-433.
40. Cinkir U, Bir LS, Topsakal S, et al (2021). Investigation of blood leptin and adropin levels in patients with multiple sclerosis: a CONSORT-clinical study. Medicine, 100(37):e27247.
41. Wang H, Wang G, Yu Y, et al (2009). The role of phosphoinositide-3-kinase/Akt pathway in propofol-induced postcondi-tioning against focal cerebral ischemia-reperfusion injury in rats. Brain Res, 1297:177-184.
42. Annovazzi L, Mellai M, Caldera V, et al (2009). mTOR, S6 and AKT expression in relation to proliferation and apopto-sis/autophagy in glioma. Anticancer Res, 29(8):3087-3094.
43. Chen H, Qu Y, Tang B, et al (2012). Role of mammalian target of rapamycin in hy-poxic or ischemic brain injury: potential neuroprotection and limitations. Rev Neurosci, 23(3):279-287.
44. Yang W, Hu Z, Ling S, et al (2015). Neuro-protective effects of DAHP and Trip-tolide in focal cerebral ischemia via apoptosis inhibition and PI3K/Akt/mTOR pathway activation. Front Neuroanat, 9:48.
45. Colin E, Régulier E, Perrin V, et al (2005). Akt is altered in an animal model of Huntington’s disease and in patients. Eur J Neurosci, 21:1478-1488.
46. Griffin RJ, Moloney A, Kelliher M, et al (2005). Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer’s dis-ease pathology. J Neurochem, 93:105-117.
47. Timmons S, Coakley MF, Moloney AM, et al (2009). Akt signal transduction dys-function in Parkinson’s disease. Neurosci Lett, 467(1):30-35.
48. Jope RS (2011). Glycogen synthase kinase-3 in the etiology and treatment of mood disorders. Front Mol Neurosci, 4:16.
49. Emamian ES, Hall D, Birnbaum MJ, et al (2004). Convergent evidence for im-paired AKT1-GSK3beta signaling in schizophrenia. Nature Genet, 36(2):131-137.
50. Karege F, Méary A, Perroud N, et al (2012). Genetic overlap between schizophrenia and bipolar disorder: a study with AKT1 gene variants and clinical phenotypes. Schizophr Res, 135(1):8-14.
51. Ali II, D'Souza C, Singh J, et al (2022). Adropin's role in energy homeostasis and metabolic disorders. Int J Mol Sci, 23(15):8318.
52. Rajan S, Dickson LM, Mathew E, et al (2015). Chronic hyperglycemia down-regulates GLP-1 receptor signaling in pancreatic β-cells via protein kinase A. Mol Metab, 4(4):265-276.
53. Woods SC, Seeley RJ, Porte D, et al (1998). Signals that regulate food intake and en-ergy homeostasis. Science, 280(5368):1378-1383.
54. Yadav AM, Bagade MM, Ghumnani S, et al (2021). The phytochemical plumbagin reciprocally modulates osteoblasts and osteoclasts. Biol Chem, 403(2):211-229.
55. Butler AA, Zhang J, Price CA, et al (2019). Low plasma adropin concentrations in-crease risks of weight gain and metabol-ic dysregulation in response to a high-sugar diet in male nonhuman primates. J Biol Chem, 294(25):9706-9719.
56. Gao S, McMillan RP, Jacas J, et al (2014). Regulation of substrate oxidation pref-erences in muscle by the peptide hor-mone adropin. Diabetes, 63(10):3242-3252.
57. Wu Z, Puigserver P, Andersson U, et al (1999). Mechanisms controlling mito-chondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell, 98(1):115-124.
58. Wei W, Liu H, Qiu X, et al (2022). The as-sociation between serum adropin and carotid atherosclerosis in patients with type 2 diabetes mellitus: a cross-sectional study. Diabetol Metab Syndr, 14(1):27.
59. Burillo J, Marqués P, Jiménez B, et al (2021). Insulin resistance and diabetes mellitus in Alzheimer’s disease. Cells, 10(5):1236.
60. Thapa D, Xie B, Manning JR, et al (2019). Adropin reduces blood glucose levels in mice by limiting hepatic glucose pro-duction. Physiol Rep, 7(8):e14043.
61. Machado-Vieira R, Frey BN, Andreazza AC, et al (2015). Translational research in bipolar disorders. Neural Plast, 2015:1-3.
2. Stein LM, Yosten GL, Samson WK (2016). Adropin acts in the brain to inhibit wa-ter drinking: potential interaction with the orphan G protein-coupled receptor, GPR19. Am J Physiol Regul Integr Comp Physiol, 310(6):R476-R480.
3. Gao S, McMillan RP, Zhu Q, et al (2015). Therapeutic effects of adropin on glu-cose tolerance and substrate utilization in diet-induced obese mice with insulin resistance. Mol Metab, 4(4):310-324.
4. Rooban S, Arul Senghor KA, Vinodhini VM, et al (2024). Adropin: A crucial regu-lator of cardiovascular health and met-abolic balance. Metabolism Open, 100299-100299.
5. Yosaee S, Soltani S, Sekhavati E, et al (2016). Adropin – A novel biomarker of heart disease: A systematic review article. Iran J Public Health, 45(12):1568-1576.
6. Kritsilis M, Rizou SV, Koutsoudaki PN, et al (2018). Ageing, cellular senescence and neurodegenerative disease. Int J Mol Sci, 19(10):2937.
7. Butler AA, St-Onge MP, Siebert EA, et al (2015). Differential responses of plasma adropin concentrations to dietary glu-cose or fructose consumption in hu-mans. Sci Rep, 5:14691.
8. Aggarwal G, Morley JE, Vellas B, et al (2024). Low circulating adropin concen-trations predict an increased risk of cognitive decline in community-dwelling older adults. Geroscience, 46(1):897-911.
9. Hayashi MA, Ducancel F, Konno K (2012). Natural peptides with potential applica-tions in drug development, diagnosis, and/or biotechnology. Int J Peptides, 2012:757838.
10. Elabadlah H, Hameed R, D'Souza C, et al (2020). Exogenous ghrelin increases plasma insulin levels in diabetic rats. Bi-omolecules, 10(4):633.
11. Adeghate E, Lotfy M, D'Souza C, et al (2020). Hypocretin/orexin modulates body weight and the metabolism of glu-cose and insulin. Diabetes Metab Syndr Obes, 36(3):e3229.
12. Adeghate E, Fernandez-Cabezudo M, Hameed R, et al (2010). Orexin-1 recep-tor co-localizes with pancreatic hor-mones in islet cells and modulates the outcome of streptozotocin-induced dia-betes mellitus. PLoS One, 5(1):e8587.
13. Mahgoub MO, D'Souza C, Al Darmaki RSMH, et al (2018). An update on the role of irisin in the regulation of endo-crine and metabolic functions. Peptides, 104:15-23.
14. Chen X, Chen S, Shen T, et al (2020). Adropin regulates hepatic glucose pro-duction via PP2A/AMPK pathway in in-sulin-resistant hepatocytes. FASEB J, 34(8):10056-10072.
15. Kuloglu T, Aydin S (2014). Immunohisto-chemical expressions of adropin and inducible nitric oxide synthase in renal tissues of rats with streptozotocin-induced experimental diabetes. Biotechnic Histochem, 89(2):104-110.
16. Levy OA, Malagelada C, Greene LA (2009). Cell death pathways in Parkinson's dis-ease: proximal triggers, distal effectors, and final steps. Apoptosis, 14(4):478-500.
17. Yang C, DeMars KM, Candelario-Jalil E (2018). Age-dependent decrease in adropin is associated with reduced lev-els of endothelial nitric oxide synthase and increased oxidative stress in the rat brain. Aging Dis, 9(2):322-330.
18. Yang C, Lavayen BP, Liu L, et al (2021). Neurovascular protection by adropin in experimental ischemic stroke through an endothelial nitric oxide synthase-dependent mechanism. Redox Biol, 48:102197.
19. Foster SR, Hauser AS, Vedel L, et al (2019). Discovery of human signaling systems: pairing peptides to G protein-coupled receptors. Cell, 179(4):895-908.
20. Wong CM, Wang Y, Lee JT, et al (2014). Adropin is a brain membrane-bound protein regulating physical activity via the NB-3/Notch signaling pathway in mice. J Biol Chem, 289(37):25976-25986.
21. Lovren F, Pan Y, Quan A, et al (2010). Adropin is a novel regulator of endothe-lial function. Circulation, 122(Suppl 11):S185-S192.
22. Wu L, Fang J, Yuan X, et al (2019). Adropin reduces hypoxia/reoxygenation-induced myocardial injury via the reperfusion in-jury salvage kinase pathway. Exp Ther Med, 18(5):3307-3314.
23. Shahjouei S, Ansari S, Pourmotabbed T, et al (2016). Potential roles of adropin in the central nervous system: review of current literature. Front Mol Biosci, 3:25.
24. Forstermann U, Munzel T (2006). Central role of eNOS in the maintenance of endothelial homeostasis. Antioxid Redox Signal, 22(14):1230-1242.
25. Zu L, Ren C, Pan B, et al (2016). Endotheli-al microparticles after antihypertensive and lipid-lowering therapy inhibit the adhesion of monocytes to endothelial cells. Int J Cardiol, 202:756-759.
26. Heiss C, Rodriguez-Mateos A, Kelm M (2015). Central role of eNOS in the maintenance of endothelial homeosta-sis. Antioxid Redox Signal, 22(14):1230-1242.
27. Thapa D, Stoner MW, Zhang M, et al (2018). Adropin regulates pyruvate dehy-drogenase in cardiac cells via a novel GPCR-MAPK-PDK4 signaling pathway. Redox Biol, 18:25-32.
28. Thibodeau A, Geng X, Previch LE, et al (2016). Pyruvate dehydrogenase complex in cerebral ischemia-reperfusion injury. Brain Circ, 2(2):61-66.
29. Patel MS, Nemeria NS, Furey W, et al (2014). The pyruvate dehydrogenase complexes: structure-based function and regulation. J Biol Chem, 289(24):16615-16623.
30. Zanotti S, Canalis E (2016). Notch signaling and the skeleton. Endocr Rev, 37(3):223-253.
31. Lai EC (2004). Notch signaling: control of cell communication and cell fate. Devel-opment, 131(5):965-973.
32. Banerjee S, Ghoshal S, Girardet C, et al (2021). Adropin correlates with aging-related neuropathology in humans and improves cognitive function in aging mice. npj Aging Mech Dis, 7:23.
33. Page MJ, McKenzie JE, Bossuyt PM, et al (2021). The PRISMA 2020 statement: an updated guideline for reporting system-atic reviews. BMJ, 372:n71.
34. Lo CKL, Mertz D, Loeb M (2014). Newcas-tle-Ottawa Scale: comparing reviewers' to authors' assessments. BMC Med Res Methodol, 14:45.
35. Stang A (2010). Critical evaluation of the Newcastle-Ottawa scale for the assess-ment of the quality of nonrandomized studies in meta-analyses. Eur J Epidemiol, 25:603-605.
36. Aggarwal G, Malmstrom TK, Morley JE, et al (2023). Low circulating adropin levels in late-middle aged African Americans with poor cognitive performance. NPJ Aging, 9(1).
37. Li X (2023). Serum adropin level as a pre-dictor of cognitive impairment in pa-tients. J Nat Sci Biol Med, 14:105-114.
38. Erşan S, Kurt A (2021). Evaluation of gluca-gon-like peptide-1, adropin, and desnu-trin levels, and related factors in pa-tients with bipolar disorder. Anatolian J Psychiatry, p. 1.
39. Lama MA, Uloom MT (2022). The role of adropin as a novel biomarker in Iraqi patients with Parkinson’s disease and os-teoporosis. Neuroquantology, 20(4):429-433.
40. Cinkir U, Bir LS, Topsakal S, et al (2021). Investigation of blood leptin and adropin levels in patients with multiple sclerosis: a CONSORT-clinical study. Medicine, 100(37):e27247.
41. Wang H, Wang G, Yu Y, et al (2009). The role of phosphoinositide-3-kinase/Akt pathway in propofol-induced postcondi-tioning against focal cerebral ischemia-reperfusion injury in rats. Brain Res, 1297:177-184.
42. Annovazzi L, Mellai M, Caldera V, et al (2009). mTOR, S6 and AKT expression in relation to proliferation and apopto-sis/autophagy in glioma. Anticancer Res, 29(8):3087-3094.
43. Chen H, Qu Y, Tang B, et al (2012). Role of mammalian target of rapamycin in hy-poxic or ischemic brain injury: potential neuroprotection and limitations. Rev Neurosci, 23(3):279-287.
44. Yang W, Hu Z, Ling S, et al (2015). Neuro-protective effects of DAHP and Trip-tolide in focal cerebral ischemia via apoptosis inhibition and PI3K/Akt/mTOR pathway activation. Front Neuroanat, 9:48.
45. Colin E, Régulier E, Perrin V, et al (2005). Akt is altered in an animal model of Huntington’s disease and in patients. Eur J Neurosci, 21:1478-1488.
46. Griffin RJ, Moloney A, Kelliher M, et al (2005). Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer’s dis-ease pathology. J Neurochem, 93:105-117.
47. Timmons S, Coakley MF, Moloney AM, et al (2009). Akt signal transduction dys-function in Parkinson’s disease. Neurosci Lett, 467(1):30-35.
48. Jope RS (2011). Glycogen synthase kinase-3 in the etiology and treatment of mood disorders. Front Mol Neurosci, 4:16.
49. Emamian ES, Hall D, Birnbaum MJ, et al (2004). Convergent evidence for im-paired AKT1-GSK3beta signaling in schizophrenia. Nature Genet, 36(2):131-137.
50. Karege F, Méary A, Perroud N, et al (2012). Genetic overlap between schizophrenia and bipolar disorder: a study with AKT1 gene variants and clinical phenotypes. Schizophr Res, 135(1):8-14.
51. Ali II, D'Souza C, Singh J, et al (2022). Adropin's role in energy homeostasis and metabolic disorders. Int J Mol Sci, 23(15):8318.
52. Rajan S, Dickson LM, Mathew E, et al (2015). Chronic hyperglycemia down-regulates GLP-1 receptor signaling in pancreatic β-cells via protein kinase A. Mol Metab, 4(4):265-276.
53. Woods SC, Seeley RJ, Porte D, et al (1998). Signals that regulate food intake and en-ergy homeostasis. Science, 280(5368):1378-1383.
54. Yadav AM, Bagade MM, Ghumnani S, et al (2021). The phytochemical plumbagin reciprocally modulates osteoblasts and osteoclasts. Biol Chem, 403(2):211-229.
55. Butler AA, Zhang J, Price CA, et al (2019). Low plasma adropin concentrations in-crease risks of weight gain and metabol-ic dysregulation in response to a high-sugar diet in male nonhuman primates. J Biol Chem, 294(25):9706-9719.
56. Gao S, McMillan RP, Jacas J, et al (2014). Regulation of substrate oxidation pref-erences in muscle by the peptide hor-mone adropin. Diabetes, 63(10):3242-3252.
57. Wu Z, Puigserver P, Andersson U, et al (1999). Mechanisms controlling mito-chondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell, 98(1):115-124.
58. Wei W, Liu H, Qiu X, et al (2022). The as-sociation between serum adropin and carotid atherosclerosis in patients with type 2 diabetes mellitus: a cross-sectional study. Diabetol Metab Syndr, 14(1):27.
59. Burillo J, Marqués P, Jiménez B, et al (2021). Insulin resistance and diabetes mellitus in Alzheimer’s disease. Cells, 10(5):1236.
60. Thapa D, Xie B, Manning JR, et al (2019). Adropin reduces blood glucose levels in mice by limiting hepatic glucose pro-duction. Physiol Rep, 7(8):e14043.
61. Machado-Vieira R, Frey BN, Andreazza AC, et al (2015). Translational research in bipolar disorders. Neural Plast, 2015:1-3.
| Files | ||
| Issue | Vol 54 No 4 (2025) | |
| Section | Review Article(s) | |
| Keywords | ||
| Adropin Neurological disorders Cognitive function Neuroprotection Systematic review | ||
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How to Cite
1.
Sivakumar R, Senghor Kadalangudi Aravaanan A, Vellore Mohanakrishnan V, Kumar J. The Emerging Role of Adropin in Neurological Health: A Systematic Review. Iran J Public Health. 2025;54(4):675-687.
