Musclin is an activity-stimulated myokine that enhances physical endurance

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 52, 2015, Pages 16042-16047

  Subbotina, Ekaterina ^a   Sierra, Ana ^a   Zhu, Zhiyong ^a   Gao, Zhan ^a   Koganti, Siva Rama Krishna ^a   Reyes, Santiago ^b   Stepniak, Elizabeth ^a   Walsh, Susan A ^a   Acevedo, Michael R ^a   Perez Terzic, Carmen M ^b   Hodgson Zingman, Denice M ^a   Zingman, Leonid V ^a,c  

^a UNIVERSITY OF IOWA   (United States)

^b MAYO CLINIC   (United States)

^c DEPARTMENT OF VETERANS AFFAIRS   (United States)

Author keywords

Exercise; Mitochondria; Natriuretic peptide; Osteocrin; Skeletal muscle

Indexed keywords

CYCLIC GMP; MITOCHONDRIAL PROTEIN; MUSCLIN PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PROTEIN; SUCCINATE DEHYDROGENASE; TRANSCRIPTION FACTOR FKHR; UNCLASSIFIED DRUG; AKT1 PROTEIN, MOUSE; ATRIAL NATRIURETIC FACTOR; CALCIMYCIN; CALCIUM; CALCIUM IONOPHORE; FORKHEAD TRANSCRIPTION FACTOR; FOXO1 PROTEIN, MOUSE; MUSCLE PROTEIN; OSTN PROTEIN, MOUSE; PROTEIN KINASE B; TRANSCRIPTION FACTOR;

ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; ENDURANCE; EXERCISE; EXERCISE TOLERANCE; GASTROCNEMIUS MUSCLE; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; MITOCHONDRIAL BIOGENESIS; MOUSE; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SECRETION; SIGNAL TRANSDUCTION; SKELETAL MUSCLE; SKELETON MALFORMATION; TREADMILL EXERCISE; VELOCITY; ANIMAL; C57BL MOUSE; CELL CULTURE; CYTOLOGY; DRUG EFFECTS; FEMALE; GENETICS; KNOCKOUT MOUSE; MALE; METABOLISM; PHOSPHORYLATION; WESTERN BLOTTING;

ANIMALS; ATRIAL NATRIURETIC FACTOR; BLOTTING, WESTERN; CALCIMYCIN; CALCIUM; CALCIUM IONOPHORES; CELLS, CULTURED; CYCLIC GMP; FEMALE; FORKHEAD BOX PROTEIN O1; FORKHEAD TRANSCRIPTION FACTORS; HUMANS; MALE; MICE, INBRED C57BL; MICE, KNOCKOUT; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOBLASTS; PHOSPHORYLATION; PHYSICAL CONDITIONING, ANIMAL; PROTO-ONCOGENE PROTEINS C-AKT; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS;

EID: 84952673488     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1514250112     Document Type: Article

References (41)

1. Lee IM, et al.; Lancet Physical Activity Series Working Group (2012) Effect of physical inactivity on major non-communicable diseases worldwide: An analysis of burden of disease and life expectancy. Lancet 380(9838):219-229.
2. Pedersen BK, Akerström TC, Nielsen AR, Fischer CP (2007) Role of myokines in exercise and metabolism. J Appl Physiol (1985) 103(3):1093-1098.
3. Pedersen BK, et al. (2004) The metabolic role of IL-6 produced during exercise: Is IL-6 an exercise factor? Proc Nutr Soc 63(2):263-267.
4. Nishizawa H, et al. (2004) Musclin, a novel skeletal muscle-derived secretory factor. J Biol Chem 279(19):19391-19395.
5. Thomas G, et al. (2003) Osteocrin, a novel bone-specific secreted protein that modulates the osteoblast phenotype. J Biol Chem 278(50):50563-50571.
6. Yasui A, et al. (2007) Foxo1 represses expression of musclin, a skeletal muscle-derived secretory factor. Biochem Biophys Res Commun 364(2):358-365.
7. Potter LR, Abbey-Hosch S, Dickey DM (2006) Natriuretic peptides, their receptors, and cyclic guanosine monophosphate-dependent signaling functions. Endocr Rev 27(1):47-72.
8. Kita S, et al. (2009) Competitive binding of musclin to natriuretic peptide receptor 3 with atrial natriuretic peptide. J Endocrinol 201(2):287-295.
9. Moffatt P, et al. (2007) Osteocrin is a specific ligand of the natriuretic Peptide clearance receptor that modulates bone growth. J Biol Chem 282(50):36454-36462.
10. Suda M, et al. (1998) Skeletal overgrowth in transgenic mice that overexpress brain natriuretic peptide. Proc Natl Acad Sci USA 95(5):2337-2342.
11. Yasoda A, et al. (2004) Overexpression of CNP in chondrocytes rescues achondroplasia through a MAPK-dependent pathway. Nat Med 10(1):80-86.
12. Jaubert J, et al. (1999) Three new allelic mouse mutations that cause skeletal overgrowth involve the natriuretic peptide receptor C gene (Npr3). Proc Natl Acad Sci USA 96(18):10278-10283.
13. Matsukawa N, et al. (1999) The natriuretic peptide clearance receptor locally modulates the physiological effects of the natriuretic peptide system. Proc Natl Acad Sci USA 96(13):7403-7408.
14. Catoire M, Kersten S (2015) The search for exercise factors in humans. FASEB J 29(5):1615-1628.
15. Gross DN, Wan M, Birnbaum MJ (2009) The role of FOXO in the regulation of metabolism. Curr Diab Rep 9(3):208-214.
16. Stitt TN, et al. (2004) The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophyinduced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 14(3):395-403.
17. Wu M, Falasca M, Blough ER (2011) Akt/protein kinase B in skeletal muscle physiology and pathology. J Cell Physiol 226(1):29-36.
18. Shaw M, Cohen P, Alessi DR (1998) The activation of protein kinase B by H2O2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2. Biochem J 336(Pt 1):241-246.
19. Coffer PJ, Jin J, Woodgett JR (1998) Protein kinase B (c-Akt): A multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochem J 335(Pt 1):1-13.
20. Vanhaesebroeck B, Alessi DR (2000) The PI3K-PDK1 connection: More than just a road to PKB. Biochem J 346(Pt 3):561-576.
21. Sable CL, Filippa N, Hemmings B, Van Obberghen E (1997) cAMP stimulates protein kinase B in a Wortmannin-insensitive manner. FEBS Lett 409(2):253-257.
22. Yano S, Tokumitsu H, Soderling TR (1998) Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway. Nature 396(6711):584-587.
23. Nader GA, Esser KA (2001) Intracellular signaling specificity in skeletal muscle in response to different modes of exercise. J Appl Physiol (1985) 90(5):1936-1942.
24. Sakamoto K, Hirshman MF, Aschenbach WG, Goodyear LJ (2002) Contraction regulation of Akt in rat skeletal muscle. J Biol Chem 277(14):11910-11917.
25. Turinsky J, Damrau-Abney A (1999) Akt kinases and 2-deoxyglucose uptake in rat skeletal muscles in vivo: Study with insulin and exercise. Am J Physiol 276 (1 Pt 2):R277-R282.
26. Brunet A, et al. (1999) Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96(6):857-868.
27. Zois NE, et al. (2014) Natriuretic peptides in cardiometabolic regulation and disease. Nat Rev Cardiol 11(7):403-412.
28. Miyashita K, et al. (2009) Natriuretic peptides/cGMP/cGMP-dependent protein kinase cascades promote muscle mitochondrial biogenesis and prevent obesity. Diabetes 58(12):2880-2892.
29. Engeli S, et al. (2012) Natriuretic peptides enhance the oxidative capacity of human skeletal muscle. J Clin Invest 122(12):4675-4679.
30. Shephard RJ (1984) Tests of maximum oxygen intake. A critical review. Sports Med 1(2):99-124.
31. Bord S, Ireland DC, Moffatt P, Thomas GP, Compston JE (2005) Characterization of osteocrin expression in human bone. J Histochem Cytochem 53(10):1181-1187.
32. Gruden G, Landi A, Bruno G (2014) Natriuretic peptides, heart, and adipose tissue: New findings and future developments for diabetes research. Diabetes Care 37(11):2899-2908.
33. Brown GC (2007) Nitric oxide and mitochondria. Front Biosci 12:1024-1033.
34. Nisoli E, et al. (2003) Mitochondrial biogenesis in mammals: The role of endogenous nitric oxide. Science 299(5608):896-899.
35. Nisoli E, et al. (2004) Mitochondrial biogenesis by NO yields functionally active mitochondria in mammals. Proc Natl Acad Sci USA 101(47):16507-16512.
36. Haas B, et al. (2009) Protein kinase G controls brown fat cell differentiation and mitochondrial biogenesis. Sci Signal 2(99): ra78.
37. Committee on Care and Use of Laboratory Animals (1996) Guide for the Care and Use of Laboratory Animals (Natl Inst Health, Bethesda), DHHS Publ No (NIH) 85-23.
38. He BJ, et al. (2011) Oxidation of CaMKII determines the cardiotoxic effects of aldosterone. Nat Med 17(12):1610-1618.
39. Alekseev AE, et al. (2010) Sarcolemmal ATP-sensitive K (+) channels control energy expenditure determining body weight. Cell Metab 11(1):58.
40. Zhu Z, et al. (2014) Sarcolemmal ATP-sensitive potassium channels modulate skeletal muscle function under low-intensity workloads. J Gen Physiol 143(1):119-134.
41. Zingman LV, et al. (2002) Kir6.2 is required for adaptation to stress. Proc Natl Acad Sci USA 99(20):13278-13283.