Follistatin Links to Articles

“Evaluation of follistatin as a therapeutic in models of skeletal muscle atrophy associated with denervation and tenotomy Patricio V. Sepulveda https://www.nature.com/articles/srep17535 WEB 2015

Abellan van Kan, G. “Epidemiology and consequences of sarcopenia.” The journal of nutrition, health & aging 13.8 (2009): 708-712.

Amthor, Helge, et al. “Lack of myostatin results in excessive muscle growth but impaired force generation.” Proceedings of the National Academy of Sciences 104.6 (2007): 1835-1840.

Amthor, Helge, and Willem MH Hoogaars. “Interference with myostatin/ActRIIB signaling as a therapeutic strategy for Duchenne muscular dystrophy.” Current gene therapy 12.3 (2012): 245-259.

Anker SD, Negassa A, Coats AJ, et al. Prognostic importance of weight loss in chronic heart failure and the effect of treatment with angiotensin-converting-enzyme inhibitors: an observational study. Lancet 2003;361:1077–83.

Argiles JM, Anker SD, Evans WJ, et al. Consensus on cachexia definitions. J Am Med Dir Assoc 2010;11:229–30

Artaza JN, Singh R, Ferrini MG, Braga M, Tsao J, Gonzalez-Cadavid NF. Myostatin

promotes a fibrotic phenotypic switch in multipotent C3H 10T1/2 cells without affecting

their differentiation into myofibroblasts. J Endocrinol 2008;196:235–49

Barns, Mitchell, et al. “Molecular analyses provide insight into mechanisms underlying sarcopenia and myofibre denervation in old skeletal muscles of mice.” The international journal of biochemistry & cell biology 53 (2014): 174-185.

Bartke, Andrzej. “Growth hormone and aging: a challenging controversy.” Clin Interv Aging 3.4 (2008): 659-665.

Becker, Clemens, et al. “Myostatin antibody (LY2495655) in older weak fallers: a proof-of-concept, randomised, phase 2 trial.” The lancet Diabetes & endocrinology 3.12 (2015): 948-957.

Benny Klimek ME, Aydogdu T, Link MJ, Pons M, Koniaris LG, Zimmers TA. Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia. Biochem Biophys Res Commun. 2010;391:1548–54.

Berardi, Emanuele, et al. “Molecular and cell-based therapies for muscle degenerations: a road under construction.” Frontiers in physiology 5 (2014): 119.

Bernardo BL, Wachtmann TS, Cosgrove PG, et al. Postnatal PPARdelta activation and

myostatin inhibition exert distinct yet complimentary effects on the metabolic pro-

file of obese insulin-resistant mice. PLoS One 2010;5:e11307.

Bogdanovich, Sasha, et al. “Myostatin propeptide-mediated amelioration of dystrophic pathophysiology.” The FASEB Journal 19.6 (2005): 543-549.

Bogdanovich, S., Krag, T. O., Barton, E. R., Morris, L. D., Whittemore, L. A., Ahima, R. S., and Khurana, T. S. (2002) Functional improvement of dystrophic muscle by myostatin blockade. Nature (London) 420, 418–421.

Bowser, Matthew, et al. “Effects of the activin A–myostatin–follistatin system on aging bone and muscle progenitor cells.” Experimental gerontology 48.2 (2013): 290-297.

Brioche, T., et al. “Growth hormone replacement therapy prevents sarcopenia by a dual mechanism: improvement of protein balance and of antioxidant defenses.” The Journals of Gerontology Series A: Biological Sciences and Medical Sciences (2013): glt187.

Brose, Andrea, Gianni Parise, and Mark A. Tarnopolsky. “Creatine supplementation enhances isometric strength and body composition improvements following strength exercise training in older adults.” The Journals of Gerontology Series A: Biological Sciences and Medical Sciences 58.1 (2003): B11-B19.

Burton, Louise A., and Deepa Sumukadas. “Optimal management of sarcopenia.” Clin Interv Aging 5.217 (2010): 2938029.

Camporez, João-Paulo G., et al. “Anti-myostatin antibody increases muscle mass and strength and improves insulin sensitivity in old mice.” Proceedings of the National Academy of Sciences 113.8 (2016): 2212-2217.

Candow, Darren G. “Sarcopenia: current theories and the potential beneficial effect of creatine application strategies.” Biogerontology 12.4 (2011): 273-281.

Candow, Darren G., et al. “Strategic creatine supplementation and resistance training in healthy older adults.” Applied Physiology, Nutrition, and Metabolism 40.7 (2015): 689-694.

Check, Erika. “Gene therapy: a tragic setback.” Nature 420.6912 (2002): 116-118.

Colussi, C., C. Gaetano, and M. C. Capogrossi. “Follistatin strikes back at muscular dystrophy.” Gene therapy 15.15 (2008): 1075-1077.

Cruz-Jentoft, Alfonso J., et al. “Sarcopenia: European consensus on definition and diagnosis Report of the European Working Group on Sarcopenia in Older People.” Age and ageing 39.4 (2010): 412-423.

Cruz-Jentoft AJ, Landi F, Schneider SM, et al. Prevalence of and interventions for sarcopenia in ageing adults: a systematic review. Report of the International Sarcopenia Initiative (EWGSOP and IWGS). Age and Ageing. 2014;43(6):748-759.

Davison KK, Ford ES, Cogswell ME, et al. Percentage of body fat and body mass index are associated with mobility limitations in people aged 70 and older from NHANES III. J Am Geriatr Soc. 2002 Nov;50(11):1802–9

Dschietzig, Thomas Bernd. “Myostatin—from the mighty mouse to cardiovascular disease and cachexia.” Clinica Chimica Acta 433 (2014): 216-224.

Eijken, Marco, et al. “The activin A-follistatin system: potent regulator of human extracellular matrix mineralization.” The FASEB Journal 21.11 (2007): 2949-2960.

Emery, Alan EH. “The muscular dystrophies.” The Lancet 359.9307 (2002): 687-695.

Fielding RA, Vellas B, Evans WJ, et al. Sarcopenia: an undiagnosed condition in older adults. Current consensus definition: prevalence, etiology, and consequences. International Working Group on Sarcopenia. J Am Med Dir Assoc. 2011;12:249–56.

Frontera WR, Hughes VA, Fielding RA, et al. Aging of skeletal muscle: a 12–yr longitudinal study. Journal of Applied Physiology. 2000;88(4):1321–6.

Fry, Christopher S., et al. “Inducible depletion of satellite cells in adult, sedentary mice impairs muscle regenerative capacity without affecting sarcopenia.” Nature medicine 21.1 (2015): 76-80.

Gaudet, Daniel, et al. “Efficacy and long-term safety of alipogene tiparvovec (AAV1-LPLS447X) gene therapy for lipoprotein lipase deficiency: an open-label trial.” Gene therapy 20.4 (2013): 361-369.

Giresi, Paul G., et al. “Identification of a molecular signature of sarcopenia.” Physiological genomics 21.2 (2005): 253-263.

Gonzalez-Cadavid NF, Taylor WE, Yarasheski K, et al. Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Proc Natl Acad Sci U S A 1998;95:14938–43.

Grounds, Miranda D. “Therapies for sarcopenia and regeneration of old skeletal muscles: more a case of old tissue architecture than old stem cells.” Bioarchitecture 4.3 (2014): 81-87.

Gruenewald, David A., and Alvin M. Matsumoto. “Testosterone supplementation therapy for older men: potential benefits and risks.” Journal of the American Geriatrics Society 51.1 (2003): 101-115.

Gualano, Bruno, et al. “Creatine supplementation in the aging population: effects on skeletal muscle, bone and brain.” Amino acids 48.8 (2016): 1793-1805.

Gueta, I., A. Altman, and Y. Shoenfeld. “The effect of blocking TNF-alpha in patients with cancer-related cachexia and anorexia.” Harefuah 149.8 (2010): 512-4.

Guiraud, Simon, et al. “Identification of decorin derived peptides with a zinc dependent anti-myostatin activity.” Neuromuscular Disorders 22.12 (2012): 1057-1068.

Guo, Qiuxia, et al. “Overexpression of mouse follistatin causes reproductive defects in transgenic mice.” Molecular Endocrinology 12.1 (1998): 96-106.

Guo T, Jou W, Chanturiya T, Portas J, Gavrilova O, McPherron AC. Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity.

PLoS One 2009;4:e4937

Greenlund LJ, Nair KS (2003) Sarcopenia—consequences, mechanisms, and potential therapies. Mech Ageing Dev 124:287–299

Han, H. Q., and William E. Mitch. “Targeting the myostatin signaling pathway to treat muscle wasting diseases.” Current opinion in supportive and palliative care 5.4 (2011): 334.

Haidet, Amanda M., et al. “Long-term enhancement of skeletal muscle mass and strength by single gene administration of myostatin inhibitors.” Proceedings of the National Academy of Sciences 105.11 (2008): 4318-4322.

Hardy, Charles L., et al. “The activin A antagonist follistatin inhibits cystic fibrosis-like lung inflammation and pathology.” Immunology and cell biology 93.6 (2015): 567-574.

Hauck, Bernd, and Weidong Xiao. “Characterization of tissue tropism determinants of adeno-associated virus type 1.” Journal of virology 77.4 (2003): 2768-2774.

Heineke J, Auger-Messier M, Xu J, Sargent M, York A, Welle S, et al. Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure. Circulation. 2010;121:419–25.

Hittel DS, Berggren JR, Shearer J, Boyle K, Houmard JA. Increased secretion and expression

of myostatin in skeletal muscle from extremely obese women. Diabetes

2009;58:30–8.

Hittel, Dustin S., et al. “Myostatin decreases with aerobic exercise and associates with insulin resistance.” Medicine and science in sports and exercise 42.11 (2010): 2023.

Hughes, Virginia A., et al. “Anthropometric assessment of 10-y changes in body composition in the elderly.” The American journal of clinical nutrition 80.2 (2004): 475-482.

Ibebunjo, Chikwendu, et al. “Genomic and proteomic profiling reveals reduced mitochondrial function and disruption of the neuromuscular junction driving rat sarcopenia.” Molecular and cellular biology 33.2 (2013): 194-212.

Janssen I, Heymsfield SB, Ross R. Low relative skeletal muscle mass (sarcopenia) in older persons is associated with functional impairment and physical disability. J Am Geriatr Soc. 2002 May;50(5):889–96.

Janssen I, Baumgartner RN, Ross R, et al. Skeletal muscle outpoints associated with elevated physical disability risk in older men and women. Am J Epidemiol. 2004 Feb 15;159(4):413–21.

Janssen I. Influence of sarcopenia on the development of physical disability: the Cardiovascular Health Study. J Am Geriatr Soc. 2006 Jan;54(1):56–62.

Jones, Kristian L., et al. “Activin A is a critical component of the inflammatory response, and its binding protein, follistatin, reduces mortality in endotoxemia.” Proceedings of the National Academy of Sciences 104.41 (2007): 16239-16244.

Kim TN, Park MS, Lim KI, Choi HY, Yang SJ, Yoo HJ, Kang HJ, Song W, Choi H, Baik SH, Choi DS, Choi KM. Relationships between sarcopenic obesity and insulin resistance, inflammation, and vitamin D status: the Korean Sarcopenic Obesity Study. Clin Endocrinol (Oxf). 2013;78:525–32.

Kohara, Katsuhiko, et al. “Leptin in sarcopenic visceral obesity: possible link between adipocytes and myocytes.” PLoS One 6.9 (2011): e24633.

Kota, Janaiah, et al. “Follistatin gene delivery enhances muscle growth and strength in nonhuman primates.” Science translational medicine 1.6 (2009): 6ra15-6ra15.

Kozaki, Koichi, et al. “Role of activin-A and follistatin in foam cell formation of THP-1 macrophages.” Arteriosclerosis, thrombosis, and vascular biology 17.11 (1997): 2389-2394.

Kozaki, Koichi, and Yasuyoshi Ouchi. “Activin/follistatin and atherosclerosis-a review.” Journal of atherosclerosis and thrombosis 5.1 (1998): 36-40.

Lang, T., et al. “Sarcopenia: etiology, clinical consequences, intervention, and assessment.” Osteoporosis international 21.4 (2010): 543-559.

Langley B, Thomas M, Bishop A, Sharma M, Gilmour S, Kambadur R. Myostatin inhibits myoblast differentiation by down-regulating MyoD expression. J Biol Chem 2002;277:49831–40.

Lee SJ, McPherron AC. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci U S A 2001;98:9306–11.

Lee SJ. Regulation of muscle mass by myostatin. 2004. Annu Rev Cell Dev Biol 20:61–86.

Lee SJ, Reed LA, Davies MV, Girgenrath S, Goad ME, Tomkinson KN, et al. Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Proc Natl Acad Sci USA. 2005;102:18117–22

Lee, Se-Jin. “Quadrupling muscle mass in mice by targeting TGF-ß signaling pathways.” PloS one 2.8 (2007): e789.

Lee SJ. Genetic analysis of the role of proteolysis in the activation of latent myostatin. PLoS One (2008);3:e1628.

Lee, Antonio SJ, et al. “Aged skeletal muscle retains the ability to fully regenerate functional architecture.” Bioarchitecture 3.2 (2013): 25-37.

Léger, Bertrand, et al. “Human sarcopenia reveals an increase in SOCS-3 and myostatin and a reduced efficiency of Akt phosphorylation.” Rejuvenation research 11.1 (2008): 163-175B.

Lexell, Jan, and D. Y. Downham. “The occurrence of fibre-type grouping in healthy human muscle: a quantitative study of cross-sections of whole vastus lateralis from men between 15 and 83 years.” Acta neuropathologica 81.4 (1991): 377-381.

Li, Zhao Bo, Jiangyang Zhang, and Kathryn R. Wagner. “Inhibition of myostatin reverses muscle fibrosis through apoptosis.” J Cell Sci 125.17 (2012): 3957-3965.

Liu, Shu, et al. “FRP inhibits ox-LDL-induced endothelial cell apoptosis through an Akt-NF-κB-Bcl-2 pathway and inhibits endothelial cell apoptosis in an apoE-knockout mouse model.” American Journal of Physiology-Endocrinology and Metabolism 299.3 (2010): E351-E363.

Louboutin, Jean‐Pierre, Lili Wang, and James M. Wilson. “Gene transfer into skeletal muscle using novel AAV serotypes.” The journal of gene medicine 7.4 (2005): 442-451.

AAV8

Maeshima, Akito, et al. “Follistatin, an activin antagonist, ameliorates renal interstitial fibrosis in a rat model of unilateral ureteral obstruction.” BioMed research international 2014 (2014).

Maguire, Albert M., et al. “Safety and efficacy of gene transfer for Leber’s congenital amaurosis.” New England Journal of Medicine 358.21 (2008): 2240-2248.

McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 1997;387:83–90.

Megeney LA, Kablar B, Garrett K, Anderson JE, Rudnicki MA. MyoD is required for myogenic stem cell function in adult skeletal muscle. Genes Dev 1996;10:1173–83

Melton LJ, 3rd, Khosla S, Crowson CS, et al. Epidemiology of sarcopenia. Journal of the American Geriatrics Society. 2000;48(6):625–30

Mendell, Jerry R., et al. “A phase 1/2a follistatin gene therapy trial for becker muscular dystrophy.” Molecular Therapy 23.1 (2015): 192-201.

Miljkovic, Iva, and Joseph M. Zmuda. “Epidemiology of myosteatosis.” Current opinion in clinical nutrition and metabolic care 13.3 (2010): 260.

Miljkovic, Iva, et al. “Myosteatosis increases with aging and is associated with incident diabetes in African ancestry men.” Obesity 24.2 (2016): 476-482.

Milman, Sofiya, et al. “Low insulin‐like growth factor‐1 level predicts survival in humans with exceptional longevity.” Aging cell 13.4 (2014): 769-771.

Mingozzi, Federico, and Katherine A. High. “Immune responses to AAV in clinical trials.” Current gene therapy 7.5 (2007): 316-324.

Mingozzi, Federico, et al. “AAV-1–mediated gene transfer to skeletal muscle in humans results in dose-dependent activation of capsid-specific T cells.” Blood 114.10 (2009): 2077-2086.

Miura T, Kishioka Y, Wakamatsu J, et al. Decorin binds myostatin and modulates its

activity to muscle cells. Biochem Biophys Res Commun 2006;340:675–80

Monestier, Olivier, et al. “Ubiquitous Gasp1 overexpression in mice leads mainly to a hypermuscular phenotype.” BMC genomics 13.1 (2012): 541.

Morissette MR, Stricker JC, Rosenberg MA, et al. Effects of myostatin deletion in

aging mice. Aging Cell 2009;8:573–83.

Morley, John E., et al. “Nutritional recommendations for the management of sarcopenia.” Journal of the American Medical Directors Association 11.6 (2010): 391-396.

Morley, John E. “Sarcopenia in the elderly.” Family practice 29.suppl 1 (2012): i44-i48.

Mosher DS, Quignon P, Bustamante CD, Sutter NB, Mellersh CS, Parker HG, Ostrander EA. A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs. PLoS Genet. 2007;3(5):e79.

Mueller, Christian, and Terence R. Flotte. “Clinical gene therapy using recombinant adeno-associated virus vectors.” Gene therapy 15.11 (2008): 858-863.

Newman AB, Kupelian V, Visser M, et al. Sarcopenia: alternative definitions and associations with lower extremity function. J Am Geriatr Soc. 2003 Nov;51(11):1602–9.

Ogawa, Sumito, Mitsutaka Yakabe, and Masahiro Akishita. “Age-related sarcopenia and its pathophysiological bases.” Inflammation and Regeneration 36.1 (2016): 17.

Patella, Shane, et al. “Follistatin attenuates early liver fibrosis: effects on hepatic stellate cell activation and hepatocyte apoptosis.” American Journal of Physiology-Gastrointestinal and Liver Physiology 290.1 (2006): G137-G144.

Phillips, David J., and David M. de Kretser. “Follistatin: a multifunctional regulatory protein.” Frontiers in neuroendocrinology 19.4 (1998): 287-322.

Pussinen PJ, Tuomisto K, Jousilahti P, Havulinna AS, Sundvall J, Salomaa V. Endotoxemia, immune response to periodontal pathogens, and systemic inflammation associate with incident cardiovascular disease events. Arterioscler Thromb Vasc Biol 2007; 27: 1433–9.

Rasmussen, Blake B., et al. “Insulin resistance of muscle protein metabolism in aging.” The FASEB journal 20.6 (2006): 768-769.

Reinders, Ilse, et al. “Muscle Quality and Myosteatosis: Novel Associations With Mortality Risk The Age, Gene/Environment Susceptibility (AGES)-Reykjavik Study.” American journal of epidemiology 183.1 (2016): 53-60.

Rodino‐Klapac, Louise R., et al. “Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease.” Muscle & nerve 39.3 (2009): 283-296.

Samaras, Nikolaos, et al. “Off-label use of hormones as an antiaging strategy: a review.” Clinical interventions in aging 9 (2014): 1175-86.

Schuelke, Markus, et al. “Myostatin mutation associated with gross muscle hypertrophy in a child.” New England Journal of Medicine 350.26 (2004): 2682-2688.

Schneider EL, Guralnik JM. The aging of America: impact on health care costs. JAMA 1990;263:2335-40.

Sharma M, Kambadur R, Matthews KG, et al. 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.

Shimasaki, Shunichi, et al. “Primary structure of the human follistatin precursor and its genomic organization.” Proceedings of the National Academy of Sciences 85.12 (1988): 4218-4222.

Smith, Rosamund C., and Boris K. Lin. “Myostatin inhibitors as therapies for muscle wasting associated with cancer and other disorders.” Current opinion in supportive and palliative care 7.4 (2013): 352-360.

Springer J, Adams V, Anker SD. Myostatin: regulator of muscle wasting in heart failure and treatment target for cardiac cachexia. Circulation. 2010;121:354–6.

Snyder, Peter J., et al. “Effects of Testosterone Replacement in Hypogonadal Men 1.” The Journal of Clinical Endocrinology & Metabolism 85.8 (2000): 2670-2677.

Szeto, Cheuk-Chun, et al. “Endotoxemia is related to systemic inflammation and atherosclerosis in peritoneal dialysis patients.” Clinical Journal of the American Society of Nephrology 3.2 (2008): 431-436.

Taaffe, DENNIS R., et al. “Estrogen replacement, muscle composition, and physical function: The Health ABC Study.” Medicine and science in sports and exercise 37.10 (2005): 1741-1747.

Tu P, Bhasin S, Hruz PW, et al. Genetic disruption of myostatin reduces the development

of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice. Diabetes 2009;58:1739–48.

Wagner, Kathryn R., et al. “A phase I/IItrial of MYO‐029 in adult subjects with muscular dystrophy.” Annals of neurology 63.5 (2008): 561-571.

Tu, Powen, et al. “Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice.” Diabetes 58.8 (2009): 1739-1748.

Wang, Zhong, et al. “Adeno-associated virus serotype 8 efficiently delivers genes to muscle and heart.” Nature biotechnology 23.3 (2005): 321-328.

Wiedermann, Christian J., et al. “Association of endotoxemia with carotid atherosclerosis and cardiovascular disease: prospective results from the Bruneck Study.” Journal of the American College of Cardiology 34.7 (1999): 1975-1981.

Wilkes, Jason J., David J. Lloyd, and Nick Gekakis. “Loss-of-function mutation in myostatin reduces tumor necrosis factor α production and protects liver against obesity-induced insulin resistance.” Diabetes 58.5 (2009): 1133-1143.

Yang W, Zhang Y, Li Y, Wu Z, Zhu D. Myostatin induces cyclin D1 degradation to cause cell cycle arrest through a phosphatidylinositol 3-kinase/AKT/GSK-3 beta pathway and is antagonized by insulin-like growth factor 1. J Biol Chem 2007;282:3799–808.

Yarasheski, K. E., et al. “Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting.” Journal of Nutrition Health and Aging 6.5 (2002): 343-348.

Zamora E, Simo R, Lupon J, et al. Serum myostatin levels in chronic heart failure.

Rev Esp Cardiol 2010;63:992–6

Zhang, Liping, et al. “Pharmacological inhibition of myostatin suppresses systemic inflammation and muscle atrophy in mice with chronic kidney disease.” The FASEB Journal 25.5 (2011): 1653-1663.

Zhao B, Wall RJ, Yang J. Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance. Biochem Biophys Res Commun 337: 248–255, 2005.

Zhou, Wei, et al. “Role of NF-kappaB and cytokine in experimental cancer cachexia.” World journal of gastroenterology 9.7 (2003): 1567-1570.

Zhou X, Wang JL, Lu J, Song Y, Kwak KS, Jiao Q, et al. Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival. Cell. 2010;142:531–43.

Zimmers TA, Davies MV, Koniaris LG, et al. Induction of cachexia in mice by systemically administered myostatin. Science 2002;296:1486–8.

Zoico, Elena, et al. “Myosteatosis and myofibrosis: relationship with aging, inflammation and insulin resistance.” Archives of gerontology and geriatrics 57.3 (2013): 411-416.