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Yıl 2019, Cilt: 11 Sayı: 3, 113 - 122, 29.06.2020

Öz

Amaç: Spor hormonu olarak adlandırılan İrisin son zamanlarda keşfedilen yeni bir moleküldür. İskelet kasının Fibronectin type III domain containing 5 (FNDC5) etki alanı içerisinde salgılanmaktadır. Beyaz adipoz dokunun kahverengi adipoz dokuya dönüştürülmesinde ve enerji metabolizmasının düzenlenmesinde önemli bir rol oynadığı ileri sürülmektedir. Ancak çalışmalarda ki çelişkili sonuçlar nedeniyle; salgılanmasında, dolaşım seviyesinde ve tespit edilmesinde bazı sorunlarla karşılaşılmaktadır.
Gereç ve Yöntem: FNDC5 / irisin hakkında mevcut bilgileri toplamak için literatür taraması yapılmıştır.
Bulgular ve sonuçlar: İrisinin keşfi, fizyolojik ve patolojik etkileri üzerine yapılan çalışmalar incelenmiş, ayrıca mevcut itirazlar ve gelecek beklentileri tartışılmıştır. İrisin üzerindeki güncel ve gelecek araştırmalar umut vadetmektedir. Tüm bu çalışmaların hastalıklara karşı ilaç hedeflerini gerçekleştirmek amacıyla yoğun bir şekilde sürdürülmesi gerekmektedir.

Kaynakça

  • 1. Spiegelman BM, A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy, Cell, 2012, 151, 1319–1331.
  • 2. Boström P, Wu J, Jedrychowski MP, Korde A, Ye L, Lo JC, Rasbach KA,Bostrom EA, Choi JH, Long JZ et al. A PGC1-α-dependent myokine that drives brown-fat-like development of white fat andthermogenesis. Nature 2012 481 463–468. (doi:10.1038/nature10777)
  • 3. Pedersen BK, Muscle as a secretory organ. Com Physiol 2013, 3, 1337-1362.
  • 4. Casteilla L, Blondel O, Klaus S, Raimbault S, Diolezt P, Moreaut F, Bouillaud F, Ricquier D, Stable expression of functional mitochondrial uncoupling protein in Chinese hamster ovary cells, Proc Natl Acad Sci 1990 , 87, 5124-5128.
  • 5. Wu Z, Puigserver P, Andersson U, Zhang C, Adelmant G, Mootha V, Troy A, Cinti S, Lowell B, Scarpulla RC, Spiegelman BM, Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1, Cell,1999, 98, 115–124.
  • 6. Pilegaard H, Saltin B, Neufer DP, Exercise induces transient transcriptional activation of the PGC-1 α gene in human skeletal muscle, J Physiol 2003, 546, 3, 851–858.
  • 7. Baar K, Wende AR, Jones ET, Marrison M, Nolte LA, Chen M, Kelly DP, Holloszy JO, Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1 α, FASEB Journal 2002. 16, 1879–1886.
  • 8. Rodgers JT, Lerin C, Hines ZG, Puigserver P, Metabolic adaptations through the PGC-1α and SIRT1 pathways, FEBS Lett, 2008, 582, 46–53.
  • 9. Eisele PS, Furrer R, Beer M, Handschin C, 2015. The PGC-1 coactivators promote an anti-inflammatory environment in skeletal muscle in vivo, Biochem Biophys Res Commun,2015, , 464, 3, 692-697.
  • 10. Courage KH, Newly discovered hormone boosts effects of exercise, could help fend off diabetes, 2012, Observations Scientific American Retrieved, January 12.
  • 11. Park A, Brown Fat: A fat that helps you lose weight?, Retrieved January 2009, 12, 2012.
  • 12. Kelly DP, Irisin, light my fire, Science, 2012, 336, 42-43.
  • 13. Castillo-Quan JI, From white to brown fat trough the PCG 1 α –dependent myokine irisin: Implications for diabetes and obesity, Dis Model Mech, 2012, 5,293-295.
  • 14. Erickson HP, Irisin and FNDC5 in retrospect: an exercise hormone or a transmembrane receptor?, Adipocytes 2013, 2 289–293. (doi:10.4161/adip. 26082)
  • 15. Raschke S, Elsen M, Gassenhuber H, Sommerfeld M, Schwahn U, Brockmann B, Jung R, Wisloff U, Tjonna AE, Raastad T et al. Evidence against a beneficial effect of irisin in humans, PLoS ONE, 2013, 8 e73680. (doi:10.1371/journal.pone.0073680)
  • 16. Kraemer RR, Shockett P, Webb ND, Shah U & Castracane VD, Atransient elevated irisin blood concentration in response to prolonged,moderate aerobic exercise in young men and women, Hormone and Metabolic Research, 2014 46 150–154. (doi:10.1055/s-0033-1355381)
  • 17. Huh JY, Panagiotou G, Mougios V, Brinkoetter M, Vamvini MT, Schneider BE & Mantzoros CS, FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise, Metabolism, 2012, 61 1725–1738. (doi:10.1016/j.metabol.2012.09.002)
  • 18. Norheim F, Langleite TM, Hjorth M, Holen T, Kielland A, Stadheim HK, Gulseth HL, Birkeland KI, Jensen J & Drevon CA, The effects of acute and chronic exercise on PGC-1a, irisin and browning of subcutaneous adipose tissue in humans, FEBS Letters, 2014, 281 739–749. (doi:10.1111/febs.12619)
  • 19. Aydin S, Kuloglu T, Yilmaz M, Kalayci M, Sahin I & Cicek D [Alterations of irisin concentrations in saliva and serum of obese and normal-weight subjects, before and after 45 min of a Turkish bath or running], Peptides 2013, 50, 13–18. doi:10.1016/j.peptides.2013.09.011
  • 20. Hecksteden A, Wegmann M, Steffen A, Kraushaar J, Morsch A, Ruppenthal S, Kaestner L & Meyer T, Irisin and exercise training in humans – results from a randomized controlled training trial. BMC Medicine, 2013, 11 235. (doi:10.1186/1741-7015-11-235)
  • 21. Moraes C, Leal VO, Marinho SM, Barroso SG, Rocha GS, Boaventura GT & Mafra D, Resistance exercise training does not affect plasma irisin levels of hemodialysis patients, Hormone and Metabolic Research 2013, 45 900–904.
  • 22. Pekkala S, Wiklund PK, Hulmi JJ, Ahtiainen JP, Horttanainen M, Pollanen E, Makela KA, Kainulainen H, Hakkinen K, Nyman K et al. Are skeletal muscle FNDC5 gene expression and irisin release regulated by exercise and related to health? Journal of Physiology, 2013, 591 5393–5400. (doi:10.1113/jphysiol.2013.263707)
  • 23. Kurdiova T, Balaz M, Vician M, Maderova D, Vlcek M, Valkovic L, Srbecky M, Imrich R, Kyselovicova O, Belan V et al. Effects of obesity, diabetes and exercise on Fndc5 gene expression and irisin release in human skeletal muscle and adipose tissue: in vivo and in vitro studies. Journal of Physiology, 2014, 592 1091–1107. (doi:10.1113/jphysiol.2013.264655)
  • 24. Tımmons JA, Wennmalm K, Larsson O, Walden TB, Lassmann T, Petrovıc N, Hamılton DL, Gımeno RE, Wahlestedt C, Baar K, Nedergaard J, Cannon B. Myogenic gene expression signature establishes that brown and white adipocytes originate from distinct cell lineages. Proc Natl Acad Sci U S A 2007; 104: 4401-4406.
  • 25. Vırtanen KA. BAT thermogenesis: Linking shivering to exercise. Cell Metab 2014; 19: 352-354.
  • 26. Lean ME. Brown adipose tissue in humans. Proc Nutr Soc 1989; 48: 243-256.
  • 27. Cannon B, Nedergaard J. Brown adipose tissue: function and physiological significance. Physiol Rev 2004; 84: 277-359.
  • 28. Nedergaard J, Bengtsson T, Cannon B. Unexpected evidence for active brown adipose tissue in adult humans. Am J Physiol Endocrinol Metab 2007; 293: E444-452.
  • 29. Vırtanen KA, Lıdell ME, Orava J, Heglınd M, Westergren R, Nıemı T, Taıttonen M, Laıne J, Savısto NJ, Enerback S, Nuutıla P. Functional brown adipose tissue in healthy adults. N Engl J Med 2009; 360:1518-1525.
  • 30. Seale P, Kajımura S, Spıegelman BM. Transcriptional control of brown adipocyte development and physiological function--of mice and men. Genes Dev 2009; 23: 788-797.
  • 31. Cousın B, Cıntı S, Morronı M, Raımbault S, Rıcquıer D, Penıcaud L, Casteılla L. Occurrence of Brown adipocytes in rat white adipose tissue: molecular and morphological characterization. J Cell Sci 1992; 103: 931-942.
  • 32. Petrovıc N, Walden TB, Shabalına IG, Tımmons JA, Cannon B, Nedergaard J. Chronic peroxisome prol i ferator -act ivated receptor gamma (PPARgamma) activation of epididymally derived white adipocyte cultures reveals a population of thermogenically competent, UCP1-containing adipocytes molecularly distinct from classic brown adipocytes. J Biol Chem 2010; 285: 7153-7164.
  • 33. Shan T, Lıang X, , Kuang S. Myostatin knockout drives browning of white adipose tissue through activating the AMPK-PGC1alpha-Fndc5 pathway in muscle. FASEB J 2013; 27: 1981-1989.
  • 34. Zhang Y, Lı R, Meng Y, Lı S, Donelan W, Zhao Y, Qı L, Zhang M, Wang X, Cuı T, Yang LJ, Tang D. Irisin stimulates browning of white adipocytes through mitogen-activated protein kinase p38 MAP kinase and ERK MAP kinase signaling. Diabetes 2014;63: 514-525.
  • 35. Poher AL, Altırrıba J, Veyrat-Durebex C, Rohnerjeanrenaud F. Brown adipose tissue activity as a target for the treatment of obesity/insulin resistance. Front Physiol 2015; 6:4.
  • 36. Choi YK, Kim MK, Bae KH, Seo HA, Jeong JY, Lee WK, Kim JG, Lee IK & Park KG, Serum irisin levels in new-onset type 2 diabetes, Diabetes Research and Clinical Practice, 2013, 100 96–101. (doi:10.1016/j.diabres.2013. 01.007)
  • 37. Moreno-Navarrete JM,Ortega F, Serrano M, Guerra E, Pardo G, Tinahones F, RicartW& Fernandez-Real JM, Irisin is expressed and produced by human muscle and adipose tissue in association with obesity and insulin resistance. Journal of Clinical Endocrinology and Metabolism, 2013, 98 E769–E778. (doi:10.1210/jc.2012-2749)
  • 38. Polyzos SA, Kountouras J, Anastasilakis AD, Geladari EV & Mantzoros CS Irisin in patients with nonalcoholic fatty liver disease. Metabolism, 2014, 63 207–217. (doi:10.1016/j.metabol.2013.09.013)
  • 39. Liu JJ, Wong MD, Toy WC, Tan CS, Liu S, Ng XW, Tavintharan S, Sum CF & Lim SC, Lower circulating irisin is associated with type 2 diabetes mellitus, Journal of Diabetes and its Complications, 2013 27 365–369. (doi:10.1016/j.jdiacomp.2013.03.002)
  • 40. Stengel A, Hofmann T, Goebel-Stengel M, Elbelt U, Kobelt P & Klapp BF Circulating levels of irisin in patients with anorexia nervosa and different stages of obesity – correlation with body mass index. Peptides, 2013, 39 125–130. (doi:10.1016/j.peptides.2012.11.014)
  • 41. Crujeiras AB, Pardo M, Arturo RR, Santiago NC, Zulet MA, Martinez JA & Casanueva FF Longitudinal variation of circulating irisin after an energy restriction-induced weight loss and following weight regain in obese men and women. American Journal of Human Biology 2014a, 26 198–207. (doi:10.1002/ajhb.22493)
  • 42. Liu JJ, Liu S, Wong MD, Tan CS, Tavintharan S, Sum CF & Lim SC Relationship between circulating irisin, renal function and body composition in type 2 diabetes. Journal of Diabetes and its Complications 2014, 28 208–213. (doi:10.1016/j.jdiacomp.2013.09.011)
  • 43. Park KH, Zaichenko L, Peter P, Davis CR, Crowell JA & Mantzoros CS Diet quality is associated with circulating C-reactive protein but not irisin levels in humans. Metabolism, 2014, 63 233–241. (doi:10.1016/j. metabol.2013.10.011).
  • 44. J. Y.Huh,G. Panagiotou,V.Mougios et al.“FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise,” Metabolism, vol. 2012, 61, no. 12, pp. 1725–1738.
  • 45. Gouni-Berthold I, Berthold HK, Huh JY, Berman R, Spenrath N, KroneW& Mantzoros CS Effects of lipid-lowering drugs on irisin in human subjects in vivo and in human skeletal muscle cells ex vivo. PLoS ONE 2013, 8 e72858. (doi:10.1371/journal. pone.0072858).
  • 46. de la Iglesia R, Lopez-Legarrea P, Crujeiras AB, Pardo M, Casanueva FF, Zulet MA & Martinez JA Plasma irisin depletion under energy restriction is associated with improvements in lipid profile inmetabolic syndrome patients. Clinical Endocrinology 2013, [in press]. (doi:10.1111/cen. 12383)
  • 47. Crujeiras AB, Zulet MA, Lopez-Legarrea P, de la Iglesia I, Pardo M, Carreira MC, Martinez JA & Casanueva FF Association between circulating irisin levels and the promotion of insulin resistance during the weight maintenance period after a dietary weight lowering program in obese patients. Metabolism, 2014b, 63 520–531. (doi:10.1016/j.metabol.2013.12.007)
  • 48. A. Roca-Rivada, C. Castelao, L. L. Senin et al., “FNDC5/irisin is not only a myokine but also an adipokine,” PLoS One, vol. 8, Article 2013, ID e60563.
  • 49. A. G. Swick, S. Orena, and A. O’Connor, “Irisin levels correlate with energy expenditure in a subgroup of humans with energy expenditure greater than predicted by fat free mass,” Metabolism, 2013, vol. 62, no. 8, pp. 1070–1073.
  • 50. B. M. Spiegelman, “Banting lecture regulation of adipogenesis: toward new therapeutics for metabolic disease,” Diabetes,2012, vol. 62, no. 6, pp. 1774–1782, 2013.

İrisin Irisin: A New Molecule

Yıl 2019, Cilt: 11 Sayı: 3, 113 - 122, 29.06.2020

Öz

Aim: Irisin, which is called as sports hormone, is a recently discovered new molecule.. It has been secreted within the domain of Fibronectin type III domain containing 5 (FNDC5) of the skeletal muscle. It is said that irisin has played an important role in converting white adipose tissue to brown adipose tissue and regulating energy metabolism. However, due to the conflicting results of the studies, it has encountered secretion, level of circulation, and detection of some problems.
Material and method: Literature search was conducted to get the current information about FNDC5 / Irisin.
Findings and results: Studies on the discovery, physiological and pathological effects of the irisin were examined, also present objections, and expectations for the future were discussed. The current and future research on the irisin promises hope. All of these studies with the aim of drug development against diseases must be maintained.

Kaynakça

  • 1. Spiegelman BM, A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy, Cell, 2012, 151, 1319–1331.
  • 2. Boström P, Wu J, Jedrychowski MP, Korde A, Ye L, Lo JC, Rasbach KA,Bostrom EA, Choi JH, Long JZ et al. A PGC1-α-dependent myokine that drives brown-fat-like development of white fat andthermogenesis. Nature 2012 481 463–468. (doi:10.1038/nature10777)
  • 3. Pedersen BK, Muscle as a secretory organ. Com Physiol 2013, 3, 1337-1362.
  • 4. Casteilla L, Blondel O, Klaus S, Raimbault S, Diolezt P, Moreaut F, Bouillaud F, Ricquier D, Stable expression of functional mitochondrial uncoupling protein in Chinese hamster ovary cells, Proc Natl Acad Sci 1990 , 87, 5124-5128.
  • 5. Wu Z, Puigserver P, Andersson U, Zhang C, Adelmant G, Mootha V, Troy A, Cinti S, Lowell B, Scarpulla RC, Spiegelman BM, Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1, Cell,1999, 98, 115–124.
  • 6. Pilegaard H, Saltin B, Neufer DP, Exercise induces transient transcriptional activation of the PGC-1 α gene in human skeletal muscle, J Physiol 2003, 546, 3, 851–858.
  • 7. Baar K, Wende AR, Jones ET, Marrison M, Nolte LA, Chen M, Kelly DP, Holloszy JO, Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1 α, FASEB Journal 2002. 16, 1879–1886.
  • 8. Rodgers JT, Lerin C, Hines ZG, Puigserver P, Metabolic adaptations through the PGC-1α and SIRT1 pathways, FEBS Lett, 2008, 582, 46–53.
  • 9. Eisele PS, Furrer R, Beer M, Handschin C, 2015. The PGC-1 coactivators promote an anti-inflammatory environment in skeletal muscle in vivo, Biochem Biophys Res Commun,2015, , 464, 3, 692-697.
  • 10. Courage KH, Newly discovered hormone boosts effects of exercise, could help fend off diabetes, 2012, Observations Scientific American Retrieved, January 12.
  • 11. Park A, Brown Fat: A fat that helps you lose weight?, Retrieved January 2009, 12, 2012.
  • 12. Kelly DP, Irisin, light my fire, Science, 2012, 336, 42-43.
  • 13. Castillo-Quan JI, From white to brown fat trough the PCG 1 α –dependent myokine irisin: Implications for diabetes and obesity, Dis Model Mech, 2012, 5,293-295.
  • 14. Erickson HP, Irisin and FNDC5 in retrospect: an exercise hormone or a transmembrane receptor?, Adipocytes 2013, 2 289–293. (doi:10.4161/adip. 26082)
  • 15. Raschke S, Elsen M, Gassenhuber H, Sommerfeld M, Schwahn U, Brockmann B, Jung R, Wisloff U, Tjonna AE, Raastad T et al. Evidence against a beneficial effect of irisin in humans, PLoS ONE, 2013, 8 e73680. (doi:10.1371/journal.pone.0073680)
  • 16. Kraemer RR, Shockett P, Webb ND, Shah U & Castracane VD, Atransient elevated irisin blood concentration in response to prolonged,moderate aerobic exercise in young men and women, Hormone and Metabolic Research, 2014 46 150–154. (doi:10.1055/s-0033-1355381)
  • 17. Huh JY, Panagiotou G, Mougios V, Brinkoetter M, Vamvini MT, Schneider BE & Mantzoros CS, FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise, Metabolism, 2012, 61 1725–1738. (doi:10.1016/j.metabol.2012.09.002)
  • 18. Norheim F, Langleite TM, Hjorth M, Holen T, Kielland A, Stadheim HK, Gulseth HL, Birkeland KI, Jensen J & Drevon CA, The effects of acute and chronic exercise on PGC-1a, irisin and browning of subcutaneous adipose tissue in humans, FEBS Letters, 2014, 281 739–749. (doi:10.1111/febs.12619)
  • 19. Aydin S, Kuloglu T, Yilmaz M, Kalayci M, Sahin I & Cicek D [Alterations of irisin concentrations in saliva and serum of obese and normal-weight subjects, before and after 45 min of a Turkish bath or running], Peptides 2013, 50, 13–18. doi:10.1016/j.peptides.2013.09.011
  • 20. Hecksteden A, Wegmann M, Steffen A, Kraushaar J, Morsch A, Ruppenthal S, Kaestner L & Meyer T, Irisin and exercise training in humans – results from a randomized controlled training trial. BMC Medicine, 2013, 11 235. (doi:10.1186/1741-7015-11-235)
  • 21. Moraes C, Leal VO, Marinho SM, Barroso SG, Rocha GS, Boaventura GT & Mafra D, Resistance exercise training does not affect plasma irisin levels of hemodialysis patients, Hormone and Metabolic Research 2013, 45 900–904.
  • 22. Pekkala S, Wiklund PK, Hulmi JJ, Ahtiainen JP, Horttanainen M, Pollanen E, Makela KA, Kainulainen H, Hakkinen K, Nyman K et al. Are skeletal muscle FNDC5 gene expression and irisin release regulated by exercise and related to health? Journal of Physiology, 2013, 591 5393–5400. (doi:10.1113/jphysiol.2013.263707)
  • 23. Kurdiova T, Balaz M, Vician M, Maderova D, Vlcek M, Valkovic L, Srbecky M, Imrich R, Kyselovicova O, Belan V et al. Effects of obesity, diabetes and exercise on Fndc5 gene expression and irisin release in human skeletal muscle and adipose tissue: in vivo and in vitro studies. Journal of Physiology, 2014, 592 1091–1107. (doi:10.1113/jphysiol.2013.264655)
  • 24. Tımmons JA, Wennmalm K, Larsson O, Walden TB, Lassmann T, Petrovıc N, Hamılton DL, Gımeno RE, Wahlestedt C, Baar K, Nedergaard J, Cannon B. Myogenic gene expression signature establishes that brown and white adipocytes originate from distinct cell lineages. Proc Natl Acad Sci U S A 2007; 104: 4401-4406.
  • 25. Vırtanen KA. BAT thermogenesis: Linking shivering to exercise. Cell Metab 2014; 19: 352-354.
  • 26. Lean ME. Brown adipose tissue in humans. Proc Nutr Soc 1989; 48: 243-256.
  • 27. Cannon B, Nedergaard J. Brown adipose tissue: function and physiological significance. Physiol Rev 2004; 84: 277-359.
  • 28. Nedergaard J, Bengtsson T, Cannon B. Unexpected evidence for active brown adipose tissue in adult humans. Am J Physiol Endocrinol Metab 2007; 293: E444-452.
  • 29. Vırtanen KA, Lıdell ME, Orava J, Heglınd M, Westergren R, Nıemı T, Taıttonen M, Laıne J, Savısto NJ, Enerback S, Nuutıla P. Functional brown adipose tissue in healthy adults. N Engl J Med 2009; 360:1518-1525.
  • 30. Seale P, Kajımura S, Spıegelman BM. Transcriptional control of brown adipocyte development and physiological function--of mice and men. Genes Dev 2009; 23: 788-797.
  • 31. Cousın B, Cıntı S, Morronı M, Raımbault S, Rıcquıer D, Penıcaud L, Casteılla L. Occurrence of Brown adipocytes in rat white adipose tissue: molecular and morphological characterization. J Cell Sci 1992; 103: 931-942.
  • 32. Petrovıc N, Walden TB, Shabalına IG, Tımmons JA, Cannon B, Nedergaard J. Chronic peroxisome prol i ferator -act ivated receptor gamma (PPARgamma) activation of epididymally derived white adipocyte cultures reveals a population of thermogenically competent, UCP1-containing adipocytes molecularly distinct from classic brown adipocytes. J Biol Chem 2010; 285: 7153-7164.
  • 33. Shan T, Lıang X, , Kuang S. Myostatin knockout drives browning of white adipose tissue through activating the AMPK-PGC1alpha-Fndc5 pathway in muscle. FASEB J 2013; 27: 1981-1989.
  • 34. Zhang Y, Lı R, Meng Y, Lı S, Donelan W, Zhao Y, Qı L, Zhang M, Wang X, Cuı T, Yang LJ, Tang D. Irisin stimulates browning of white adipocytes through mitogen-activated protein kinase p38 MAP kinase and ERK MAP kinase signaling. Diabetes 2014;63: 514-525.
  • 35. Poher AL, Altırrıba J, Veyrat-Durebex C, Rohnerjeanrenaud F. Brown adipose tissue activity as a target for the treatment of obesity/insulin resistance. Front Physiol 2015; 6:4.
  • 36. Choi YK, Kim MK, Bae KH, Seo HA, Jeong JY, Lee WK, Kim JG, Lee IK & Park KG, Serum irisin levels in new-onset type 2 diabetes, Diabetes Research and Clinical Practice, 2013, 100 96–101. (doi:10.1016/j.diabres.2013. 01.007)
  • 37. Moreno-Navarrete JM,Ortega F, Serrano M, Guerra E, Pardo G, Tinahones F, RicartW& Fernandez-Real JM, Irisin is expressed and produced by human muscle and adipose tissue in association with obesity and insulin resistance. Journal of Clinical Endocrinology and Metabolism, 2013, 98 E769–E778. (doi:10.1210/jc.2012-2749)
  • 38. Polyzos SA, Kountouras J, Anastasilakis AD, Geladari EV & Mantzoros CS Irisin in patients with nonalcoholic fatty liver disease. Metabolism, 2014, 63 207–217. (doi:10.1016/j.metabol.2013.09.013)
  • 39. Liu JJ, Wong MD, Toy WC, Tan CS, Liu S, Ng XW, Tavintharan S, Sum CF & Lim SC, Lower circulating irisin is associated with type 2 diabetes mellitus, Journal of Diabetes and its Complications, 2013 27 365–369. (doi:10.1016/j.jdiacomp.2013.03.002)
  • 40. Stengel A, Hofmann T, Goebel-Stengel M, Elbelt U, Kobelt P & Klapp BF Circulating levels of irisin in patients with anorexia nervosa and different stages of obesity – correlation with body mass index. Peptides, 2013, 39 125–130. (doi:10.1016/j.peptides.2012.11.014)
  • 41. Crujeiras AB, Pardo M, Arturo RR, Santiago NC, Zulet MA, Martinez JA & Casanueva FF Longitudinal variation of circulating irisin after an energy restriction-induced weight loss and following weight regain in obese men and women. American Journal of Human Biology 2014a, 26 198–207. (doi:10.1002/ajhb.22493)
  • 42. Liu JJ, Liu S, Wong MD, Tan CS, Tavintharan S, Sum CF & Lim SC Relationship between circulating irisin, renal function and body composition in type 2 diabetes. Journal of Diabetes and its Complications 2014, 28 208–213. (doi:10.1016/j.jdiacomp.2013.09.011)
  • 43. Park KH, Zaichenko L, Peter P, Davis CR, Crowell JA & Mantzoros CS Diet quality is associated with circulating C-reactive protein but not irisin levels in humans. Metabolism, 2014, 63 233–241. (doi:10.1016/j. metabol.2013.10.011).
  • 44. J. Y.Huh,G. Panagiotou,V.Mougios et al.“FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise,” Metabolism, vol. 2012, 61, no. 12, pp. 1725–1738.
  • 45. Gouni-Berthold I, Berthold HK, Huh JY, Berman R, Spenrath N, KroneW& Mantzoros CS Effects of lipid-lowering drugs on irisin in human subjects in vivo and in human skeletal muscle cells ex vivo. PLoS ONE 2013, 8 e72858. (doi:10.1371/journal. pone.0072858).
  • 46. de la Iglesia R, Lopez-Legarrea P, Crujeiras AB, Pardo M, Casanueva FF, Zulet MA & Martinez JA Plasma irisin depletion under energy restriction is associated with improvements in lipid profile inmetabolic syndrome patients. Clinical Endocrinology 2013, [in press]. (doi:10.1111/cen. 12383)
  • 47. Crujeiras AB, Zulet MA, Lopez-Legarrea P, de la Iglesia I, Pardo M, Carreira MC, Martinez JA & Casanueva FF Association between circulating irisin levels and the promotion of insulin resistance during the weight maintenance period after a dietary weight lowering program in obese patients. Metabolism, 2014b, 63 520–531. (doi:10.1016/j.metabol.2013.12.007)
  • 48. A. Roca-Rivada, C. Castelao, L. L. Senin et al., “FNDC5/irisin is not only a myokine but also an adipokine,” PLoS One, vol. 8, Article 2013, ID e60563.
  • 49. A. G. Swick, S. Orena, and A. O’Connor, “Irisin levels correlate with energy expenditure in a subgroup of humans with energy expenditure greater than predicted by fat free mass,” Metabolism, 2013, vol. 62, no. 8, pp. 1070–1073.
  • 50. B. M. Spiegelman, “Banting lecture regulation of adipogenesis: toward new therapeutics for metabolic disease,” Diabetes,2012, vol. 62, no. 6, pp. 1774–1782, 2013.
Toplam 50 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Klinik Tıp Bilimleri
Bölüm Derleme
Yazarlar

Banu Kabak Bu kişi benim

Belma Haner Bu kişi benim

Abdullah Genç Bu kişi benim

Yayımlanma Tarihi 29 Haziran 2020
Yayımlandığı Sayı Yıl 2019 Cilt: 11 Sayı: 3

Kaynak Göster

APA Kabak, B., Haner, B., & Genç, A. (2020). Yeni Bir Molekül. Gaziosmanpaşa Üniversitesi Tıp Fakültesi Dergisi, 11(3), 113-122.
AMA Kabak B, Haner B, Genç A. Yeni Bir Molekül. Gaziosmanpaşa Tıp Dergisi. Haziran 2020;11(3):113-122.
Chicago Kabak, Banu, Belma Haner, ve Abdullah Genç. “Yeni Bir Molekül”. Gaziosmanpaşa Üniversitesi Tıp Fakültesi Dergisi 11, sy. 3 (Haziran 2020): 113-22.
EndNote Kabak B, Haner B, Genç A (01 Haziran 2020) Yeni Bir Molekül. Gaziosmanpaşa Üniversitesi Tıp Fakültesi Dergisi 11 3 113–122.
IEEE B. Kabak, B. Haner, ve A. Genç, “Yeni Bir Molekül”, Gaziosmanpaşa Tıp Dergisi, c. 11, sy. 3, ss. 113–122, 2020.
ISNAD Kabak, Banu vd. “Yeni Bir Molekül”. Gaziosmanpaşa Üniversitesi Tıp Fakültesi Dergisi 11/3 (Haziran 2020), 113-122.
JAMA Kabak B, Haner B, Genç A. Yeni Bir Molekül. Gaziosmanpaşa Tıp Dergisi. 2020;11:113–122.
MLA Kabak, Banu vd. “Yeni Bir Molekül”. Gaziosmanpaşa Üniversitesi Tıp Fakültesi Dergisi, c. 11, sy. 3, 2020, ss. 113-22.
Vancouver Kabak B, Haner B, Genç A. Yeni Bir Molekül. Gaziosmanpaşa Tıp Dergisi. 2020;11(3):113-22.

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