Submitted Successfully!
To reward your contribution, here is a gift for you: A free trial for our video production service.
Thank you for your contribution! You can also upload a video entry or images related to this topic.
Version Summary Created by Modification Content Size Created at Operation
1 Myokines are secreted in response to skeletal muscle contractions during exercise and are promising anti-aging molecules due to their benefits in age-related diseases.
Kyoung Min Moon
 + 1423 word(s) 1423 2020-10-10 05:26:53 |
2 format change
Nicole Yin
Meta information modification 1423 2020-10-14 04:24:19 |

Video Upload Options

Do you have a full video?
Send video materials Upload full video

Confirm

Are you sure to Delete?
Yes No
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Kwon, J.H.; Moon, K.M.; Min, K. Myokines. Encyclopedia. Available online: https://encyclopedia.pub/entry/2490 (accessed on 24 April 2024).
Kwon JH, Moon KM, Min K. Myokines. Encyclopedia. Available at: https://encyclopedia.pub/entry/2490. Accessed April 24, 2024.
Kwon, Jenny Hyosun, Kyoung Min Moon, Kyueng-Whan Min. "Myokines" Encyclopedia, https://encyclopedia.pub/entry/2490 (accessed April 24, 2024).
Kwon, J.H., Moon, K.M., & Min, K. (2020, October 10). Myokines. In Encyclopedia. https://encyclopedia.pub/entry/2490
Kwon, Jenny Hyosun, et al. "Myokines." Encyclopedia. Web. 10 October, 2020.
Myokines
Edit
This entry is adapted from the peer-reviewed paper 10.3390/healthcare8040378

Myokines are small proteins (5–20 kDa) and proteoglycan peptides that are produced and secreted by skeletal muscle cells in response to muscle contractions.

myokine elderly exercise physical activity aerobic anaerobic

1. Introduction

With aging, the secretion of apelin, BAIBA, BMP-7, decorin, IGF-1, IL-15, irisin, SDF-1, sestrin, SPARC, and VEGF-A decreased, while that of IL-6 and myostatin increased. Aerobic exercise upregulates apelin, BAIBA, IL-15, IL-6, irisin, SDF-1, sestrin, SPARC, and VEGF-A expression, while anaerobic exercise upregulates BMP-7, decorin, IGF-1, IL-15, IL-6, irisin, and VEGF-A expression. Myostatin is downregulated by both aerobic and anaerobic exercise.

2. Apelin

Human apelin was identified and isolated in 1998 as an endogenous ligand of the G-protein-coupled receptor APJ and was named the APJ endogenous ligand. The apelin gene located at chromosome Xq25–26.1, encodes a 77 amino acid preproprotein[1][2]. After the cleavage of the signal peptide, the protein is processed into various bioactive endogenous peptides, such as apelin-13, -16, -17, and -36[3], which are widely expressed in various organs. Apelin regulates a wide range of physiological processes, including blood pressure[4], cardiac contractility[5], and angiogenesis[6], and is involved in pathophysiological processes underlying hypoxia[7], obesity[8], diabetes[9], and various cancers[10].

3. β-aminoisobutyric Acid (BAIBA)

BAIBA (C4H9NO2) is a small, non-protein myokine with a molecular weight of 103.6 Da that was first discovered in human urine in 1951[11]. It is secreted by contracting muscles via the action of peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α) and acts in a myokine-specific manner[12][13]. It is involved in various metabolic processes, such as acting on white adipose tissue to upregulate brown adipose tissue-specific genes, enhancing PGC-1α expression to increase lipid oxidation, suppressing inflammation in skeletal muscles, inhibiting cardiometabolic risk factors, and suppressing endoplasmic reticulum stress in hepatoblastoma cells. Blood BAIBA levels increase in response to continuous exercise[12][14][15][16]. The myokine properties of BAIBA suggest that many small molecule metabolites may have myokine functions.

4. Bone Morphogenetic Protein 7 (BMP-7)

In 1965, Urist recognized BMP as an important factor in osteogenesis and bone formation[17]. BMP-7, also called osteogenic protein-1, is a member of the TGF-β superfamily of cysteine-knot fold cytokine-growth factors[18]. Human BMP-7 has been isolated and mapped to chromosome 20q13.31. This has been proposed as a possible locus for the Holt-Oram syndrome, which manifests as skeletal abnormalities of the upper limbs and hands[19][20][21]. BMP-7 is a multifunctional growth factor involved in cell proliferation, apoptosis, organ repair, and differentiation of brown adipose tissue, but its most important function is inducing cartilage and bone formation[22][23][24][25].

5. Decorin

Human decorin is a small leucine-rich proteoglycan of 90–140 kDa that is associated with collagen fibrils in all connective tissue. The gene is located on chromosome 12q23[26] and regulates transforming growth factor (TGF)-beta 1 activity as well as the cell cycle[27]. Decorin suppresses myostatin activity, which is associated with obesity and diabetes[13]. In 2014, decorin was first recognized as a myokine, and its levels in both plasma and skeletal muscle increase in response to physical activity[28].

6. Insulin-Like Growth Factor 1 (IGF-1)

In 1957, IGF-1 was first recognized by Salmon and Daughaday as a “sulfation factor” that stimulates sulfate incorporation in rat cartilage[29]. In 1978, Rinderknecht and Humbel purified a human IGF-1, a protein of 70 amino acids with structural resemblance to proinsulin[30]. In 1983, the human IGF-1 cDNA was cloned, and in 1984, IGF-1 was found to be located on chromosome 12q23.2[31][32]. Although IGF-1 is a multifunctional peptide, its main physiological function is as a growth hormone (GH) essential for normal bone and tissue growth and development[33]. In 2012, IGF-1 was recognized as a myokine produced and secreted by the muscle fibers[34].

7. Interleukin-15 (IL-15)

Human IL-15 was reported simultaneously by two groups in 1994 as a T-cell growth factor. IL-15, located on chromosome 4q31, encodes a 14–15 kDa glycoprotein incorporating a four α-helix bundle[35][36][37]. In humans, IL-15 expression is detected in various cells and tissues, including skeletal muscle, epithelial cells, monocytes, and dendritic cells[38]. The primary biological functions of IL-15 are to activate and proliferate T-cells and NK cells, inhibit apoptosis, and accelerate CD8(+) antitumor immunity[39][40][41]. Brandt and Pedersen suggested in 2010 that muscle-derived IL-15 is a myokine constitutively expressed by skeletal muscles and is regulated in response to strength training[42].

8. Interleukin-6 (IL-6)

IL-6 is a cytokine that plays multifunctional roles in the regulation of the immune system, nervous system, and glucose homeostasis[43][44]. IL-6 has several names, including interferon beta-2 (IFNB2), B-cell stimulatory factor 2 (BSF2), hepatocyte stimulatory factor, and hybridoma growth factor. Zilberstein et al. and Hirano et al. cloned full-length cDNAs encoding human IFNB2—a 23.7 kDa protein comprising 212 amino acids—and human BSF2—a novel interleukin comprising 184 amino acids—respectively[45][46]. Using in situ hybridization, Sutherland et al. identified that IFNB2 is located on chromosome 7p15.3[47]. The extramembrane (IL-6r) and intramembrane (gp130) domains of the IL-6 receptor were cloned in 1988 and 1990, respectively[48][49]. IL-6 is the first myokine produced and released into the supernatant when C2C12 myotubes and skeletal muscle fibers are induced to contract by electrical pulse stimulation[50][51].

9. Irisin (Fibronectin Type III Domain Containing 5 [FNDC5])

Irisin, which is a novel myokine discovered in 2012, is expressed in a PGC-1α-dependent manner to produce FNDC5. This is followed by cleavage of the N-terminal signal peptide and C-terminal hydrophobic domain, resulting in the production of a 12 kDa glycoprotein that is secreted into the bloodstream and is involved in fat metabolism. FNDC5 is predominantly localized in the endoplasmic reticulum[52]. Genomic sequencing analyses indicate that FNDC5 contains six exons and this gene has been mapped to chromosome 1p35.1[53]. Although the irisin receptor is unknown, irisin is highly conserved in all mammalian species, which suggests highly conserved biological functions[54]. Recently, irisin has been hypothesized to be involved in the downregulation of insulin resistance pathway (ROS → p38 MAPK → PGC-1α → irisin → insulin resistance pathway), which is positively controlled by exercise and negatively controlled by aging[55].

10. Myostatin (Growth/Differentiation Factor-8 [GDF-8])

Myostatin (GDF-8), a member of the TGF-β superfamily, plays an important role in the negative regulation of skeletal muscle growth and is specifically expressed in developmental and adult skeletal muscle[56][57]. Myostatin, inhibited by follistatin, has recently attracted attention as a useful pharmacological target for preserving muscle mass and preventing atrophy[58]. McPherron et al. and Gonzalez-Cadavid et al. isolated and characterized the mouse myostatin and human myostatin genes, respectively[56][59]. In one study, plasma myostatin concentration in three groups of subjects (19–35, 60–75, and 76–92 years) were highest in the 76–92-year-old group, which suggests that plasma myostatin could be used as a biomarker for diagnosing age-associated sarcopenia[60].

11. Stromal Cell-Derived Factor 1 (SDF-1)

The expression of SDF-1—also called CXC motif chemokine ligand 12 (CXCL12), intercrine reduced in hepatomas (IRH), and pre-B cell growth-stimulating factor—is expressed in many cell types (i.e., fibroblasts, myoblasts, muscle fibers)[61]. This chemokine was originally described as a B-cell precursor stimulating growth factor secreted by a bone marrow stromal cell line[62]. CXCR4 and CXCR7 are the primary physiological receptors of SDF-1[63][64], and the gene coding for this protein is located on chromosome 10q11.1[65][66]. SDF-1-CXCR4 signaling occurs in the mesenchyme of limbs during early development and is directly responsible for the development of appropriately sized muscles[67], which indicates its important role in skeletal muscle regeneration[68][69].

12. Sestrin

Sestrin was first discovered in 1994 as a target of the tumor suppressor p53 and was referred to as p53-activated gene 26 (PA26). The gene coding for sestrin is located on chromosome 6q21[70][71]. In mammalian cells, three different sestrin isoforms, which share high sequence homology, are encoded by genes located on different chromosomes, Sestrin1 on chromosome 6, Sestrin2 on chromosome 1, and Sestrin3 on chromosome 11[72]. Sestrin acts as an intracellular leucine sensor to negatively regulate the target of rapamycin complex 1 (TORC-1) signaling by activating AMP-dependent protein kinase (AMPK), which prevents the development of sarcopenia and extends the life span[73]. Pathophysiological stressors, such as DNA damage and oxidative stress, upregulate sestrin expression, which negatively regulates aging by activating the AMPK/autophagy pathway and inhibiting the TORC1 signaling[74].

13. Secreted Protein, Acidic, Rich in Cysteine (SPARC; Osteonectin/Basement-Membrane Protein 40)

In 1989, the human SPARC was first demonstrated to be located on chromosome 5q33.1[75], and since then, it has been confirmed that the SPARC protein functions in a Ca2+-ion-dependent manner[76]. SPARC is a 43 kDa secretory matricellular glycoprotein that has multiple biological functions, including tumor-suppressing activity, cell differentiation, and cell adhesion in several organs and cell types[77][78][79]. SPARC was first recognized as a myokine in 2013 as a result of cell-stretching stimulation experiments on C2C12 myocytes[80].

14. Vascular Endothelial Growth Factor A (VEGF-A)

VEGF-A, first discovered in 1983[81], is encoded by a gene located on chromosome 6p21.1; the cDNA encoding VEGF-A was isolated in 1989[82]. VEGF-A is a secreted, 46 kDa homodimer glycoprotein containing a highly conserved receptor-binding cysteine-knot structure. VEGF-A is one of the most important factors in the growth and survival of skeletal muscle in humans and animals[83].

References

  1. Tatemoto, K.; Hosoya, M.; Habata, Y.; Fujii, R.; Kakegawa, T.; Zou, M.X.; Kawamata, Y.; Fukusumi, S.; Hinuma, S.; Kitada, C.; et al. Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor. Biochem. Biophys. Res. Commun. 1998, 251, 471–476.
  2. Lee, D.K.; Cheng, R.; Nguyen, T.; Fan, T.; Kariyawasam, A.P.; Liu, Y.; Osmond, D.H.; George, S.R.; O’Dowd, B.F. Characterization of apelin, the ligand for the APJ receptor. J. Neurochem. 2000, 74, 34–41.
  3. Yugo Habata; Ryo Fujii; Masaki Hosoya; Shoji Fukusumi; Yuji Kawamata; Shuji Hinuma; Chieko Kitada; Naoki Nishizawa; Shinji Murosaki; Tsutomu Kurokawa; et al.Haruo OndaKazuhiko TatemotoMasahiko Fujino Apelin, the natural ligand of the orphan receptor APJ, is abundantly secreted in the colostrum. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1999, 1452, 25-35, 10.1016/s0167-4889(99)00114-7.
  4. Kazuhiko Tatemoto; Kiyoshige Takayama; Min-Xu Zou; Iku Kumaki; Wei Zhang; Kimitsuka Kumano; M. Fujimiya; The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism. Regulatory Peptides 2001, 99, 87-92, 10.1016/s0167-0115(01)00236-1.
  5. István Szokodi; Pasi Tavi; Gábor Földes; Sari Voutilainen-Myllylä; Mika Ilves; Heikki Tokola; Sampsa Pikkarainen; Jarkko Piuhola; Jaana Rysä; Miklós Tóth; et al.Heikki Ruskoaho Apelin, the Novel Endogenous Ligand of the Orphan Receptor APJ, Regulates Cardiac Contractility. Circulation Research 2002, 91, 434-440, 10.1161/01.res.0000033522.37861.69.
  6. Li Zhang; Kazuhiro Takara; Daishi Yamakawa; Hiroyasu Kidoya; Nobuyuki Takakura; Apelin as a marker for monitoring the tumor vessel normalization window during antiangiogenic therapy. Cancer Science 2015, 107, 36-44, 10.1111/cas.12836.
  7. Jingchang Zhang; Qiming Liu; Zhenfei Fang; XinQun Hu; Feng Huang; Liang Tang; Shenghua Zhou; Hypoxia induces the proliferation of endothelial progenitor cells via upregulation of Apelin/APLNR/MAPK signaling. Molecular Medicine Reports 2015, 13, 1801-1806, 10.3892/mmr.2015.4691.
  8. Jérémie Boucher; Bernard Masri; Danièle Daviaud; Stéphane Gesta; Charlotte Guigné; Anne Mazzucotelli; Isabelle Castan-Laurell; Ivan Tack; Bernard Knibiehler; Christian Carpéné; et al.Yves AudigierJean-Sébastien Saulnier-BlachePhilippe Valet Apelin, a Newly Identified Adipokine Up-Regulated by Insulin and Obesity. Endocrinology 2005, 146, 1764-1771, 10.1210/en.2004-1427.
  9. L. Li; G. Yang; Q. Li; Y. Tang; M. Yang; H. Yang; K. Li; Changes and Relations of Circulating Visfatin, Apelin, and Resistin Levels in Normal, Impaired Glucose Tolerance, and Type 2 Diabetic Subjects. Experimental and Clinical Endocrinology & Diabetes 2006, 114, 544-548, 10.1055/s-2006-948309.
  10. Javad Masoumi; Abdollah Jafarzadeh; Hossein Khorramdelazad; Morteza Abbasloui; Jalal Abdolalizadeh; Najmeh Jamali; Role of Apelin/APJ axis in cancer development and progression. Advances in Medical Sciences 2020, 65, 202-213, 10.1016/j.advms.2020.02.002.
  11. H. R. Crumpler; C. E. Dent; H. Harris; R. G. Westall; β-Aminoisobutyric Acid (α-Methyl-β-Alanine): A New Amino-Acid Obtained from Human Urine. Nature 1951, 167, 307-308, 10.1038/167307a0.
  12. Roberts, L.D.; Bostrom, P.; O’Sullivan, J.F.; Schinzel, R.T.; Lewis, G.D.; Dejam, A.; Lee, Y.K.; Palma, M.J.; Calhoun, S.; Georgiadi, A.; et al. beta-Aminoisobutyric acid induces browning of white fat and hepatic beta-oxidation and is inversely correlated with cardiometabolic risk factors. Cell Metab. 2014, 19, 96–108.
  13. Schnyder, S.; Handschin, C. Skeletal muscle as an endocrine organ: PGC-1alpha, myokines and exercise. Bone 2015, 80, 115–125.
  14. Kammoun, H.L.; Febbraio, M.A. Come on BAIBA light my fire. Cell Metab. 2014, 19, 1–2.
  15. Shi, C.X.; Zhao, M.X.; Shu, X.D.; Xiong, X.Q.; Wang, J.J.; Gao, X.Y.; Chen, Q.; Li, Y.H.; Kang, Y.M.; Zhu, G.Q. β-aminoisobutyric acid attenuates hepatic endoplasmic reticulum stress and glucose/lipid metabolic disturbance in mice with type 2 diabetes. Sci. Rep. 2016, 6, 21924.
  16. Tanianskii, D.A.; Jarzebska, N.; Birkenfeld, A.L.; O’Sullivan, J.F.; Rodionov, R.N. Beta-aminoisobutyric acid as a novel regulator of carbohydrate and lipid metabolism. Nutrients 2019, 11, 524.
  17. Marshall R. Urist; Bone: Formation by Autoinduction. Science 1965, 150, 893-899, 10.1126/science.150.3698.893.
  18. Grace Mitu; Raimund Hirschberg; Bone morphogenetic protein-7 (BMP7) in chronic kidney disease.. null 2008, 13, 4726–4739.
  19. Pesonen, E.; Merritt, A.T.; Heldt, G.; Sahn, D.J.; Elias, W.; Tikkanen, I.; Fyhrquist, F.; Andersson, S. Correlation of patent ductus arteriosus shunting with plasma atrial natriuretic factor concentration in preterm infants with respiratory distress syndrome. Pediatr. Res. 1990, 27, 137–139.
  20. Ozkaynak, E.; Rueger, D.C.; Drier, E.A.; Corbett, C.; Ridge, R.J.; Sampath, T.K.; Oppermann, H. OP-1 cDNA encodes an osteogenic protein in the TGF-beta family. EMBO J. 1990, 9, 2085–2093.
  21. Hahn, G.V.; Cohen, R.B.; Wozney, J.M.; Levitz, C.L.; Shore, E.M.; Zasloff, M.A.; Kaplan, F.S. A bone morphogenetic protein subfamily: Chromosomal localization of human genes for BMP5, BMP6, and BMP7. Genomics 1992, 14, 759–762.
  22. Ripamonti, U.; Reddi, A.H. Tissue engineering, morphogenesis, and regeneration of the periodontal tissues by bone morphogenetic proteins. Crit. Rev. Oral Biol. Med. 1997, 8, 154–163.
  23. Chen, D.; Zhao, M.; Mundy, G.R. Bone morphogenetic proteins. Growth Fact. 2004, 22, 233–241.
  24. Schulz, T.J.; Huang, T.L.; Tran, T.T.; Zhang, H.; Townsend, K.L.; Shadrach, J.L.; Cerletti, M.; McDougall, L.E.; Giorgadze, N.; Tchkonia, T.; et al. Identification of inducible brown adipocyte progenitors residing in skeletal muscle and white fat. Proc. Natl. Acad. Sci. USA 2011, 108, 143–148.
  25. Saini, S.; Duraisamy, A.J.; Bayen, S.; Vats, P.; Singh, S.B. Role of BMP7 in appetite regulation, adipogenesis, and energy expenditure. Endocrine 2015, 48, 405–409.
  26. Ulrich Vetter; Walther Vogel; Walter Just; Marian F. Young; Larry W. Fisher; Human Decorin Gene: Intron-Exon Junctions and Chromosomal Localization. Genomics 1993, 15, 161-168, 10.1006/geno.1993.1023.
  27. Rebeca Droguett; Claudio Cabello-Verrugio; Cecilia Riquelme; Enrique Brandan; Extracellular proteoglycans modify TGF-β bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biology 2006, 25, 332-341, 10.1016/j.matbio.2006.04.004.
  28. Timo Kanzleiter; Michaela Rath; Sven W. Görgens; Jørgen Jensen; Daniel S. Tangen; Anders J. Kolnes; Kristoffer J. Kolnes; Sindre Lee; Jürgen Eckel; Annette Schürmann; et al.Kristin Eckardt The myokine decorin is regulated by contraction and involved in muscle hypertrophy. Biochemical and Biophysical Research Communications 2014, 450, 1089-1094, 10.1016/j.bbrc.2014.06.123.
  29. W D Salmon; W H Daughaday; A hormonally controlled serum factor which stimulates sulfate incorporation by cartilage in vitro.. Journal of Laboratory and Clinical Medicine 1957, 49, 825-836.
  30. E Rinderknecht; R E Humbel; The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin.. Journal of Biological Chemistry 1978, 253, 2769-2776.
  31. Jansen, M.; van Schaik, F.M.; Ricker, A.T.; Bullock, B.; Woods, D.E.; Gabbay, K.H.; Nussbaum, A.L.; Sussenbach, J.S.; Van den Brande, J.L. Sequence of cDNA encoding human insulin-like growth factor I precursor. Nature 1983, 306, 609–611.
  32. Hoppener, J.W.; de Pagter-Holthuizen, P.; Geurts van Kessel, A.H.; Jansen, M.; Kittur, S.D.; Antonarakis, S.E.; Lips, C.J.; Sussenbach, J.S. The human gene encoding insulin-like growth factor I is located on chromosome 12. Hum. Genet. 1985, 69, 157–160.
  33. Yasmine Neirijnck; Marilena D. Papaioannou; Serge Nef; Nef; The Insulin/IGF System in Mammalian Sexual Development and Reproduction. International Journal of Molecular Sciences 2019, 20, 4440, 10.3390/ijms20184440.
  34. B. K. Pedersen; Mark A. Febbraio; Muscles, exercise and obesity: skeletal muscle as a secretory organ. Nature Reviews Endocrinology 2012, 8, 457-465, 10.1038/nrendo.2012.49.
  35. Burton, J.D.; Bamford, R.N.; Peters, C.; Grant, A.J.; Kurys, G.; Goldman, C.K.; Brennan, J.; Roessler, E.; Waldmann, T.A. A lymphokine, provisionally designated interleukin T and produced by a human adult T-cell leukemia line, stimulates T-cell proliferation and the induction of lymphokine-activated killer cells. Proc. Natl. Acad. Sci. USA 1994, 91, 4935–4939.
  36. Grabstein, K.H.; Eisenman, J.; Shanebeck, K.; Rauch, C.; Srinivasan, S.; Fung, V.; Beers, C.; Richardson, J.; Schoenborn, M.A.; Ahdieh, M.; et al. Cloning of a T cell growth factor that interacts with the beta chain of the interleukin-2 receptor. Science 1994, 264, 965–968.
  37. Steel, J.C.; Waldmann, T.A.; Morris, J.C. Interleukin-15 biology and its therapeutic implications in cancer. Trends Pharmacol. Sci. 2012, 33, 35–41.
  38. LeBris S. Quinn; Barbara G. Anderson; Interleukin-15, IL-15 Receptor-Alpha, and Obesity: Concordance of Laboratory Animal and Human Genetic Studies. Journal of Obesity 2011, 2011, 1-8, 10.1155/2011/456347.
  39. Klebanoff, C.A.; Finkelstein, S.E.; Surman, D.R.; Lichtman, M.K.; Gattinoni, L.; Theoret, M.R.; Grewal, N.; Spiess, P.J.; Antony, P.A.; Palmer, D.C.; et al. IL-15 enhances the in vivo antitumor activity of tumor-reactive CD8+ T cells. Proc. Natl. Acad. Sci. USA 2004, 101, 1969–1974.
  40. Malamut, G.; El Machhour, R.; Montcuquet, N.; Martin-Lanneree, S.; Dusanter-Fourt, I.; Verkarre, V.; Mention, J.J.; Rahmi, G.; Kiyono, H.; Butz, E.A.; et al. IL-15 triggers an antiapoptotic pathway in human intraepithelial lymphocytes that is a potential new target in celiac disease-associated inflammation and lymphomagenesis. J. Clin. Investig. 2010, 120, 2131–2143.
  41. Wu, J. IL-15 agonists: The cancer cure cytokine. J. Mol. Genet. Med. 2013, 7, 85.
  42. Claus Brandt; Bente K. Pedersen; The Role of Exercise-Induced Myokines in Muscle Homeostasis and the Defense against Chronic Diseases. Journal of Biomedicine and Biotechnology 2010, 2010, 1-6, 10.1155/2010/520258 Epub 2010 Mar 9..
  43. Brown, J.A.; Sherrod, S.D.; Goodwin, C.R.; Brewer, B.; Yang, L.; Garbett, K.A.; Li, D.; McLean, J.A.; Wikswo, J.P.; Mirnics, K. Metabolic consequences of interleukin-6 challenge in developing neurons and astroglia. J. Neuroinflamm. 2014, 11, 183.
  44. Kouda, K.; Furusawa, K.; Sugiyama, H.; Sumiya, T.; Ito, T.; Tajima, F.; Shimizu, K. Does 20-min arm crank ergometer exercise increase plasma interleukin-6 in individuals with cervical spinal cord injury? Eur. J. Appl. Physiol. 2012, 112, 597–604.
  45. Zilberstein, A.; Ruggieri, R.; Korn, J.H.; Revel, M. Structure and expression of cDNA and genes for human interferon-beta-2, a distinct species inducible by growth-stimulatory cytokines. EMBO J. 1986, 5, 2529–2537.
  46. Hirano, T.; Yasukawa, K.; Harada, H.; Taga, T.; Watanabe, Y.; Matsuda, T.; Kashiwamura, S.; Nakajima, K.; Koyama, K.; Iwamatsu, A.; et al. Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin. Nature 1986, 324, 73–76.
  47. G R Sutherland; E Baker; D. F. Callen; V J Hyland; G Wong; S Clark; S S Jones; L K Eglinton; M F Shannon; A F Lopez; et al. Interleukin 4 is at 5q31 and interleukin 6 is at 7p15.. Human Genetics 1988, 79, 335–337.
  48. Yamasaki, K.; Taga, T.; Hirata, Y.; Yawata, H.; Kawanishi, Y.; Seed, B.; Taniguchi, T.; Hirano, T.; Kishimoto, T. Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor. Science 1988, 241, 825–828.
  49. Hibi, M.; Murakami, M.; Saito, M.; Hirano, T.; Taga, T.; Kishimoto, T. Molecular cloning and expression of an IL-6 signal transducer, gp130. Cell 1990, 63, 1149–1157.
  50. Nedachi, T.; Fujita, H.; Kanzaki, M. Contractile C2C12 myotube model for studying exercise-inducible responses in skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 2008, 295, E1191–E1204.
  51. Farmawati, A.; Kitajima, Y.; Nedachi, T.; Sato, M.; Kanzaki, M.; Nagatomi, R. Characterization of contraction-induced IL-6 up-regulation using contractile C2C12 myotubes. Endocr. J. 2013, 60, 137–147.
  52. Andreas Teufel; Nasir Malik; Mahua Mukhopadhyay; Heiner Westphal; Frcp1 and Frcp2, two novel fibronectin type III repeat containing genes. Gene 2002, 297, 79-83, 10.1016/s0378-1119(02)00828-4.
  53. Harald Staiger; Anja Böhm; Mika Scheler; Lucia Berti; Jürgen Machann; Fritz Schick; Fausto Machicao; Andreas Fritsche; Norbert Stefan; Cora Weigert; et al.Anna KrookHans-Ulrich HäringMartin De Angelis Common Genetic Variation in the Human FNDC5 Locus, Encoding the Novel Muscle-Derived ‘Browning’ Factor Irisin, Determines Insulin Sensitivity. PLOS ONE 2013, 8, e61903, 10.1371/journal.pone.0061903.
  54. Marta G. Novelle; Cristina Contreras; Amparo Romero-Picó; Miguel López; Carlos Dieguez; Irisin, Two Years Later. International Journal of Endocrinology 2013, 2013, 1-8, 10.1155/2013/746281.
  55. Fabian Sanchis-Gomar; Carme Perez-Quilis; The p38-PGC-1α-irisin-betatrophin axis: Exploring new pathways in insulin resistance.. Adipocyte 2013, 3, 67-68, 10.4161/adip.27370.
  56. McPherron, A.C.; Lawler, A.M.; Lee, S.J. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 1997, 387, 83–90.
  57. Sharma, M.; Kambadur, R.; Matthews, K.G.; Somers, W.G.; Devlin, G.P.; Conaglen, J.V.; Fowke, P.J.; Bass, J.J. Myostatin, a transforming growth factor-beta superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct. J. Cell. Physiol. 1999, 180, 1–9.
  58. Se-Jin Lee; Yun-Sil Lee; Teresa A. Zimmers; Arshia Soleimani; Martin M. Matzuk; Kunihiro Tsuchida; Ronald D. Cohn; Elisabeth R. Barton; Regulation of Muscle Mass by Follistatin and Activins. Molecular Endocrinology 2010, 24, 1998-2008, 10.1210/me.2010-0127.
  59. N. F. Gonzalez-Cadavid; W. E. Taylor; K. Yarasheski; I. Sinha-Hikim; K. Ma; S. Ezzat; R. Shen; R. Lalani; S. Asa; M. Mamita; et al.G. NairS. ArverS. Bhasin Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Proceedings of the National Academy of Sciences 1998, 95, 14938-14943, 10.1073/pnas.95.25.14938.
  60. Kevin E. Yarasheski; Shalender Bhasin; I Sinha-Hikim; J Pak-Loduca; N F Gonzalez-Cadavid; Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting.. The journal of nutrition, health & aging 2002, 6, 343–348.
  61. Conny Hunger; Veysel Ödemis; Jürgen Engele; Expression and function of the SDF-1 chemokine receptors CXCR4 and CXCR7 during mouse limb muscle development and regeneration. Experimental Cell Research 2012, 318, 2178-2190, 10.1016/j.yexcr.2012.06.020.
  62. K Tashiro; H Tada; R Heilker; M Shirozu; T Nakano; T Honjo; Signal sequence trap: a cloning strategy for secreted proteins and type I membrane proteins. Science 1993, 261, 600-603, 10.1126/science.8342023.
  63. Bleul, C.C.; Farzan, M.; Choe, H.; Parolin, C.; Clark-Lewis, I.; Sodroski, J.; Springer, T.A. The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry. Nature 1996, 382, 829–833.
  64. Adlere, I.; Caspar, B.; Arimont, M.; Dekkers, S.; Visser, K.; Stuijt, J.; de Graaf, C.; Stocks, M.; Kellam, B.; Briddon, S.; et al. Modulators of CXCR4 and CXCR7/ACKR3 Function. Mol. Pharmacol. 2019, 96, 737–752.
  65. Nagasawa, T.; Kikutani, H.; Kishimoto, T. Molecular cloning and structure of a pre-B-cell growth-stimulating factor. Proc. Natl. Acad. Sci. USA 1994, 91, 2305–2309.
  66. Shirozu, M.; Nakano, T.; Inazawa, J.; Tashiro, K.; Tada, H.; Shinohara, T.; Honjo, T. Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene. Genomics 1995, 28, 495–500.
  67. Elena Vasyutina; Jürg Stebler; Beate Brand-Saberi; Stefan Schulz; Erez Raz; Carmen Birchmeier; CXCR4 and Gab1 cooperate to control the development of migrating muscle progenitor cells. Genes & Development 2005, 19, 2187-2198, 10.1101/gad.346205.
  68. Brzoska, E.; Kowalewska, M.; Markowska-Zagrajek, A.; Kowalski, K.; Archacka, K.; Zimowska, M.; Grabowska, I.; Czerwinska, A.M.; Czarnecka-Gora, M.; Streminska, W.; et al. Sdf-1 (CXCL12) improves skeletal muscle regeneration via the mobilisation of Cxcr4 and CD34 expressing cells. Biol. Cell 2012, 104, 722–737.
  69. Bobadilla, M.; Sainz, N.; Abizanda, G.; Orbe, J.; Rodriguez, J.A.; Paramo, J.A.; Prosper, F.; Perez-Ruiz, A. The CXCR4/SDF1 axis improves muscle regeneration through MMP-10 activity. Stem Cells Dev. 2014, 23, 1417–1427.
  70. Buckbinder, L.; Talbott, R.; Seizinger, B.R.; Kley, N. Gene regulation by temperature-sensitive p53 mutants: Identification of p53 response genes. Proc. Natl. Acad. Sci. USA 1994, 91, 10640–10644.
  71. Velasco-Miguel, S.; Buckbinder, L.; Jean, P.; Gelbert, L.; Talbott, R.; Laidlaw, J.; Seizinger, B.; Kley, N. PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes. Oncogene 1999, 18, 127–137.
  72. Parmigiani, A.; Budanov, A.V. Sensing the environment through sestrins: Implications for cellular metabolism. In International Review of Cell and Molecular Biology; Academic Press: Cambridge, MA, USA, 2016; Volume 327, pp. 1–42.
  73. Jun Hee Lee; Andrei V. Budanov; Michael Karin; Sestrins Orchestrate Cellular Metabolism to Attenuate Aging. Cell Metabolism 2013, 18, 792-801, 10.1016/j.cmet.2013.08.018.
  74. Jun Hee Lee; Rolf Bodmer; Ethan Bier; Michael Karin; Sestrins at the crossroad between stress and aging. Aging 2010, 2, 369-374, 10.18632/aging.100157.
  75. Xavier C. Villarreal; Kenneth G. Mann; George L. Long; Structure of human osteonectin based upon analysis of cDNA and genomic sequences. Biochemistry 1989, 28, 6483-6491, 10.1021/bi00441a049.
  76. James A. Bassuk; François Baneyx; Robert B. Vernon; Sarah E. Funk; E.Helene Sage; Expression of Biologically Active Human SPARC inEscherichia coli. Archives of Biochemistry and Biophysics 1996, 325, 8-19, 10.1006/abbi.1996.0002.
  77. Mok, S.C.; Chan, W.Y.; Wong, K.K.; Muto, M.G.; Berkowitz, R.S. SPARC, an extracellular matrix protein with tumor-suppressing activity in human ovarian epithelial cells. Oncogene 1996, 12, 1895–1901.
  78. Brekken, R.A.; Sage, E.H. SPARC, a matricellular protein: At the crossroads of cell-matrix communication. Matrix Biol. 2001, 19, 816–827.
  79. Kos, K.; Wilding, J.P. SPARC: A key player in the pathologies associated with obesity and diabetes. Nat. Rev. Endocrinol. 2010, 6, 225–235.
  80. Wataru Aoi; Yuji Naito; Tomohisa Takagi; Yuko Tanimura; Yoshikazu Takanami; Yukari Kawai; Kunihiro Sakuma; Liu Po Hang; Katsura Mizushima; Yasuko Hirai; et al.Ryota KoyamaSayori WadaAkane HigashiSatoshi KokuraHiroshi IchikawaToshikazu Yoshikawa A novel myokine, secreted protein acidic and rich in cysteine (SPARC), suppresses colon tumorigenesis via regular exercise. Gut 2012, 62, 882-889, 10.1136/gutjnl-2011-300776.
  81. D R Senger; S J Galli; A M Dvorak; C A Perruzzi; V S Harvey; H F Dvorak; Tumor cells secrete a vascular permeability factor that promotes accumulation of ascites fluid. Science 1983, 219, 983-985, 10.1126/science.6823562.
  82. D W Leung; G Cachianes; W J Kuang; D V Goeddel; N Ferrara; Vascular endothelial growth factor is a secreted angiogenic mitogen. Science 1989, 246, 1306-1309, 10.1126/science.2479986.
  83. Marc G. Achen; S A Stacker; The vascular endothelial growth factor family; proteins which guide the development of the vasculature.. International Journal of Experimental Pathology 1998, 79, 255–265.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license; additional terms may apply. By using this site, you agree to the Terms and Conditions and Privacy Policy.
Upload a video for this entry
Information
Subjects: Biochemistry & Molecular Biology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
Jenny Hyosun Kwon
,
Kyoung Min Moon
,
Kyueng-Whan Min
View Times: 1.2K
Entry Collection: Peptides for Health Benefits
Revisions: 2 times (View History)
Update Date: 14 Oct 2020
Table of Contents
    1000/1000
    Hot Most Recent
    Feedback