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Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
Abstract
Aging skeletal muscles suffer a steady decline in mass and functional performance, and compromised muscle integrity as fibrotic invasions replace contractile tissue, accompanied by a characteristic loss in the fastest, most powerful muscle fibers. The same programmed deficits in muscle structure and function are found in numerous neurodegenerative syndromes and disease-related cachexia. We have generated a model of persistent, functional myocyte hypertrophy using a tissue-restricted transgene encoding a locally acting isoform of insulin-like growth factor-1 that is expressed in skeletal muscle (mIgf-1). Transgenic embryos developed normally, and postnatal increases in muscle mass and strength were not accompanied by the additional pathological changes seen in other Igf-1 transgenic models. Expression of GATA-2, a transcription factor normally undetected in skeletal muscle, marked hypertrophic myocytes that escaped age-related muscle atrophy and retained the proliferative response to muscle injury characteristic of younger animals. The preservation of muscle architecture and age-independent regenerative capacity through localized mIgf-1 transgene expression suggests clinical strategies for the treatment of age or disease-related muscle frailty.
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“Muscle-specific overexpression of a locally acting IGF1 isoform in mice showed that localized IGF1 expression sustains muscle growth and regeneration6.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [6]
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Cites
A Calcineurin-Dependent Transcriptional Pathway for Cardiac Hypertrophy
Molkentin, J. D., Lu, J., Antos, C. L., Markham, B. E., Richardson, J. A., Robbins, J. M., Grant, S. R., & Olson, E. N. (1998) · Cell · doi:10.1016/s0092-8674(00)81573-1 · Cited by 2,566
Growth Hormone and the Insulin-Like Growth Factor System in Myogenesis*
Florini, J. R., Ewton, D. Z., & Coolican, S. A. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-5-481 · Cited by 1,148
A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber typePreprint
Chin, E. R., Olson, E. N., Richardson, J. A., Yang, Q., Humphries, C. G., Shelton, J. M., Wu, H., Zhu, W., Bassel‐Duby, R., & Williams, R. S. (1998) · Genes & Development · doi:10.1101/gad.12.16.2499 · Cited by 1,015
Sjögren, K., Liu, J., Blad, K., Skrtic, S., Vidal, O., Wallenius, V., LeRoith, D., Törnell, J., Isaksson, O. G. P., Jansson, J., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.7088 · Cited by 940
Stewart, C. E., & Rotwein, P. S. (1996) · Physiological Reviews · doi:10.1152/physrev.1996.76.4.1005 · Cited by 785
Contractile properties of skeletal muscles from young, adult and aged mice.
Brooks, S. V., & Faulkner, J. A. (1988) · The Journal of Physiology · doi:10.1113/jphysiol.1988.sp017279 · Cited by 777
Barton-Davis, E. R., Shoturma, D. I., Musarò, A., Rosenthal, N. A., & Sweeney, H. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15603 · Cited by 700
Self-citationMusarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652
Self-citationColeman, M. E., DeMayo, F., Yin, K. C., Lee, H. M., Geske, R., Montgomery, C., & Schwartz, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.12109 · Cited by 642
CaM kinase signaling induces cardiac hypertrophy and activates the MEF2 transcription factor in vivo
Passier, R., Zeng, H., Frey, N., Naya, F. J., Nicol, R. L., McKinsey, T. A., Overbeek, P. A., Richardson, J. A., Grant, S. R., & Olson, E. N. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8551 · Cited by 521
Cited by
Sorted by citations
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
Cellular and Molecular Regulation of Muscle Regeneration
CHARGÉ, S. B. P., & Rudnicki, M. A. (2004) · Physiological Reviews · doi:10.1152/physrev.00019.2003 · Cited by 2,691
“IGF-I and IGF-II appear to ameliorate the aging muscle phenotype and the dystrophic muscle phenotype in mdx mice (25, 222, 286).”
BackgroundSatellite Cells and the Muscle Stem Cell Niche
Yin, H., Price, F., & Rudnicki, M. A. (2013) · Physiological Reviews · doi:10.1152/physrev.00043.2011 · Cited by 2,166
“Elevation of IGF-I signaling within muscle cells in vitro results in muscle hypertrophy with increased DNA and protein content in muscle (6, 34, 87, 103, 365).”
BackgroundStitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797
Myogenic satellite cells: physiology to molecular biology
Hawke, T. J., & Garry, D. J. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.91.2.534 · Cited by 1,646
“, transgenic overexpression or knockout models), may further define the regulation and signaling pathways of the IGFs and satellite cell biology (8, 25, 132).”
BackgroundMechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284
“Indeed, treatment of muscle cultures with AICAR, an activator of AMPK, increases protein breakdown and atrogin-1 expression via the FoxO family (Nakashima and Yakabe, 2007).”
Skeletal muscle hypertrophy and atrophy signaling pathways
Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106
“…muscle (Vandenburgh, Karlisch, Shansky, & Feldstein, 1991), as was demonstrated in transgenic F nali phy a have a n ctivat tions: G targ ight, s diff red is T r w i E3 u gul the M lat of t tream o mice in which IGF-1 is overexpressed in skeletal muscle (Coleman et al., 1995; Musaro et al., 2001).”
BackgroundMechanisms of muscle atrophy and hypertrophy: implications in health and disease
Sartori, R., Romanello, V., & Sandri, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20123-1 · Cited by 940
Marquis, K., Debigaré, R., Lacasse, Y., Leblanc, P., Jobin, J., Carrier, G., & Maltais, F. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2107031 · Cited by 840
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816
“The effect of an IGF1 isoform (IGF1A) was investigated in a transgenic mouse model, in which expression of this isoform was driven by the myosin light chain 1 fast promoter [51].”
BackgroundMyostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792
Sarcopenia: etiology, clinical consequences, intervention, and assessment
Lang, T., Streeper, T., Cawthon, P. M., Baldwin, K., Taaffe, D. R., & Harris, T. B. (2009) · Osteoporosis International · doi:10.1007/s00198-009-1059-y · Cited by 820
“The other source of IGF-1 is within the skeletal muscle itself, with two primary variants [34], including one which is produced in response to physical activity and is referred to as mechano growth factor and one which is similar to the mature IGF-1 produced within the liver [35, 36].”
BackgroundThe Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
“Calcineurin appears to act as a co-regulator of muscle hypertrophy with insulin-like growth factor and may also contribute to myogenic proliferation and differentiation of satellite cells during skeletal muscle regeneration (Dunn et al. 1999; Musaro et al. 1999; Dunn et al. 2000; Sakuma et al. 2003; Scicchitano et al.…”
BackgroundUrbich, C., Aicher, A., Heeschen, C., Dernbach, E., HOFMANN, W., Zeiher, A. M., & Dimmeler, S. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.07.003 · Cited by 744
“In addition, IGF-1 plays a crucial role in muscle regeneration by promoting the proliferation and differentiation of satellite cells in the muscle, enabling them to fuse to existing muscle fibers and repair damaged regions and subsequently to enhance muscle regenerative capacity [45,46].”
BackgroundMechanisms of IGF-1-Mediated Regulation of Skeletal Muscle Hypertrophy and Atrophy
Yoshida, T., & Delafontaine, P. (2020) · Cells · doi:10.3390/cells9091970 · Cited by 772
Satellite Cells and Skeletal Muscle Regeneration
Dumont, N. A., Bentzinger, C. F., Sincennes, M., & Rudnicki, M. A. (2015) · Comprehensive Physiology · doi:10.1002/cphy.c140068 · Cited by 719
Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
Glass, D. J. (2003) · Nature Cell Biology · doi:10.1038/ncb0203-87 · Cited by 694
“Other work has focused on the phosphatidylinositol-3-OH kinase PI(3)K/Akt (PKB) pathway downstream of IGF-1, demonstrating that Akt is activated during hypertrophy and is sufficient to induce hypertrophy12,13.”
BackgroundInfluentialEffects of Aging on Muscle Fibre Type and Size
Deschenes, M. R. (2004) · Sports Medicine · doi:10.2165/00007256-200434120-00002 · Cited by 671
Pope, H. G., Wood, R. I., Rogol, A. D., Nyberg, F., Bowers, L. D., & Bhasin, S. (2013) · Endocrine Reviews · doi:10.1210/er.2013-1058 · Cited by 703
Sim, F. J., Zhao, C., Penderis, J., & Franklin, R. J. M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-07-02451.2002 · Cited by 625
“Like many repair processes in the body, it becomes less efficient with age (Gilson and Blakemore, 1993; Ashcroft et al., 1995; Shields et al., 1999; Musaro et al., 2001).”
BackgroundMechanisms of muscle wasting in chronic kidney disease
Wang, X. H., & Mitch, W. E. (2014) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.112 · Cited by 630
Systemic delivery of genes to striated muscles using adeno-associated viral vectors
Gregorevic, P., Blankinship, M. J., Allen, J. M., Crawford, R. W., Meuse, L., Miller, D. G., Russell, D. W., & Chamberlain, J. S. (2004) · Nature Medicine · doi:10.1038/nm1085 · Cited by 620
Cachexia: pathophysiology and clinical relevance1,2
Morley, J. E., Thomas, D. R., & Wilson, M.-M. G. (2006) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.4.735 · Cited by 786
“Stem cells that express the muscle isoform of IGF-I prevent sarcopenia in old rodents (35, 36).”
BackgroundDeveloping a pro-regenerative biomaterial scaffold microenvironment requires T helper 2 cells
Sadtler, K., Estrellas, K., Allen, B. W., Wolf, M. T., Fan, H., Tam, A. J., Patel, C. H., Luber, B. S., Wang, H., Wagner, K. R., et al. (2016) · Science · doi:10.1126/science.aad9272 · Cited by 605
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555
“Genetic activation of IGF1 (Coleman et al., 1995; Musaro et al., 2001) or Akt (Lai et al.”
BackgroundLatres, E., Amini, A. R., Amini, A. A., Griffiths, J., Martin, F. J., Wei, Y., Lin, H. C., Yancopoulos, G. D., & Glass, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 538
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517
Peroxisome proliferator‐activated receptor δ controls muscle development and oxydative capability
Luquet, S., Lopez‐Soriano, J., Holst, D., Fredenrich, A., Melki, J., Rassoulzadegan, M., & Grimaldi, P. A. (2003) · The FASEB Journal · doi:10.1096/fj.03-0269fje · Cited by 509
“This was previously reported in exercised animals (34) or in genetically modified mice with an increased muscle mass by muscle-specific IGF-I overexpression (35) or myostatin gene inactivation (36).”
mTOR as a key regulator in maintaining skeletal muscle mass
Yoon, M.-S. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00788 · Cited by 495
“Muscle-specific expression of IGFI in transgenic mice results in at least a 2-fold increase in muscle hypertrophy (Coleman et al., 1995; Musaro et al., 2001), suggesting that the IGF-I/Akt/mTORC1 pathway is indispensable to muscle hypertrophy.”
BackgroundSatellite-cell pool size does matter: Defining the myogenic potency of aging skeletal muscle
Shefer, G., de Mark, D. P. V., Richardson, J. B., & Yablonka‐Reuveni, Z. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.02.022 · Cited by 526
“The impaired capacity of aging muscle to support satellite cell recruitment/proliferation was suggested to be a consequence of a decline in IGF-I (Barton-Davis et al., 1998; Chakravarthy et al., 2000; Musaro et al., 2001) or a reduction in notch signaling (Conboy et al., 2003; Conboy and Rando, 2002).”
BackgroundInfluentialMuscle stem cells in development, regeneration, and diseasePreprint
Shi, X., & Garry, D. J. (2006) · Genes & Development · doi:10.1101/gad.1419406 · Cited by 502
“…muscle restores the regenerative capacity of aging skeletal muscle through the promotion of satellite cell activation, satellite cell proliferation, and the recruitment of nonmuscle stem cells GENES & DEVELOPMENT 1697 from the bone marrow (Barton-Davis et al. 1998; Musaro et al. 2001, 2004).”
BackgroundSuppression of body fat accumulation in myostatin-deficient mice
McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505
Inhibition of myostatin in adult mice increases skeletal muscle mass and strength
Whittemore, L.-A., Song, K., Li, X., Aghajanian, J. D., Davies, M. V., Girgenrath, S., Hill, J. J., Jalenak, M., Kelley, P. E., Knight, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02953-4 · Cited by 512
“In addition, the myostatin knockout mice accumulate less fat than their wild type littermates [5,6], which may be a secondary consequence of increased muscle mass since a similar effect is seen in other genetic models of muscle hypertrophy [7,8].”
BackgroundLenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 498
“At least in transgenic mice overexpressing IGF-1 specifically in the skeletal muscle, it was evident that the age-related sarcopenia was prevented [28].”
BackgroundDuan, C., Ren, H., & Gao, S. (2010) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2010.04.009 · Cited by 502
“Musaro et al. (2001) generated transgenic mice with a locally acting isoform of IGF-I expressed in skeletal muscle.”
BackgroundEndocrine Control of Body Composition in Infancy, Childhood, and Puberty
Veldhuis, J. D., Roemmich, J. N., Richmond, E. J., Rogol, A. D., Lovejoy, J. C., Sheffield-Moore, M., Mauras, N., & Bowers, C. Y. (2005) · Endocrine Reviews · doi:10.1210/er.2003-0038 · Cited by 452
Muscle-specific expression of insulin-like growth factor I counters muscle decline in mdx mice
Barton, E. R., Morris, L. D., Musarò, A., Rosenthal, N. A., & Sweeney, H. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108071 · Cited by 450
“growth and repair-inducing growth factors, including IGF-I and hepatocyte growth factor (HGF) (Barton-Davis et al., 1998; Chakravarthy et al., 2000b; Musaro et al., 2001).”
BackgroundMethodResultInfluentialSelf-citationRegulation of muscle mass by growth hormone and IGF‐I
Velloso, C. P. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.153 · Cited by 456
“This contrasts sharply with animals in which IGF-I is expressed in muscle without leading to concomitant increases in serum IGF-I (Coleman et al., 1995; Musaro et al., 2001).”
BackgroundConditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Lai, K.-M. V., Gonzalez, M., Poueymirou, W. T., Kline, W. O., Na, E., Zlotchenko, E., Stitt, T. N., Economides, A. N., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9295-9304.2004 · Cited by 442
“When IGF-1 levels were enhanced by using a musclespecific promoter in transgenic mice, increased muscle size resulted (4, 13).”
BackgroundMolecular mechanisms modulating muscle mass
Glass, D. J. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00138-2 · Cited by 444
The contribution of reactive oxygen species to sarcopenia and muscle ageing
Fulle, S., Protasi, F., Tano, G. D., Pietrangelo, T., Beltramin, A., Boncompagni, S., Vecchiet, L., & Fanò, G. (2003) · Experimental Gerontology · doi:10.1016/j.exger.2003.09.012 · Cited by 451
New fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437
“Transgenic mice engineered to overexpress systemic or liver type IGF-1 under the control of a muscle-speciWc promoter have skeletal muscles that are twofold greater in mass than those seen in normal mice (Coleman et al. 1995; Musaro et al. 2001).”
BackgroundMethodInfluentialLack of myostatin results in excessive muscle growth but impaired force generation
Amthor, H., Macharia, R., Navarrete, R., Schuelke, M., Brown, S., Otto, A., Voït, T., Muntoni, F., Vrbovà, G., Partridge, T. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604893104 · Cited by 438
Mechanisms Regulating Neuromuscular Junction Development and Function and Causes of Muscle Wasting
Tintignac, L. A. J., Brenner, H.-R., & Rüegg, M. A. (2015) · Physiological Reviews · doi:10.1152/physrev.00033.2014 · Cited by 449
“Activation of the mTORC1 pathway by infection of skeletal muscle with IGF1-expressing viruses (27) or transgenic expression of IGF1 (316) induces a strong muscle hypertrophy in young and old mice.”
BackgroundCellular and molecular mechanisms underlying age-related skeletal muscle wasting and weakness
Ryall, J. G., Schertzer, J. D., & Lynch, G. S. (2008) · Biogerontology · doi:10.1007/s10522-008-9131-0 · Cited by 423
“…activity and is called ‘mechano growth factor’ or MGF and the other is similar to the systemic or liver type (IGF-IEa) important for providing the mature IGF-I required to up-regulate protein synthesis (Musarò et al. 2001; Barton et al. 2002; Goldspink and Harridge 2004; Petrella et al. 2006).”
BackgroundHameed, M., Orrell, R. W., COBBOLD, M., Goldspink, G., & Harridge, S. D. R. (2002) · The Journal of Physiology · doi:10.1111/j.1469-7793.2003.00247.x · Cited by 420
“It is the cDNA of this isoform that has been used for gene transfer into muscles or to generate transgenic mice (Barton-Davies et al. 1998; Musaro et al. 2001).”
BackgroundThe “Dying-Back” Phenomenon of Motor Neurons in ALS
Dadon-Nachum, M., Melamed, E., & Offen, D. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9467-1 · Cited by 404
Regulation of PI3-kinase/Akt signaling by muscle-enriched microRNA-486
Small, E. M., O'Rourke, J. R., Moresi, V., Sutherland, L. B., McAnally, J., Gerard, R. D., Richardson, J. A., & Olson, E. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000300107 · Cited by 417
Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004937 · Cited by 402
“Several other transgenic mouse models that have increased muscle mass, including some using muscle-specific promoters to drive expression of genes that cause muscle hypertrophy, also have decreased adiposity demonstrating that changes in adipose tissue size can be indirectly caused by changes in skeletal muscle size […”
Regeneration of Mammalian Skeletal Muscle: Basic Mechanisms and Clinical Implications
Ciciliot, S., & Schiaffino, S. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210790883453 · Cited by 402
“IGF-1 overexpression in transgenic mice was found to enhance the regenerative capacity of aged skeletal muscle [71].”
BackgroundAging and disease as modifiers of efficacy of cell therapy
Dimmeler, S., & Leri, A. (2008) · Circulation Research · doi:10.1161/circresaha.108.175943 · Cited by 379
Environment and plasticity of myogenesis in teleost fish
Johnston, I. A. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02153 · Cited by 406
“In mammals, the calcineurin signalling pathway is thought to play a role in regulating hypertrophic growth of skeletal muscle (Musaro et al., 2001).”
BackgroundMolecular and cellular mechanisms of skeletal muscle atrophy: an update
Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 386
“fiber growth [13, 14], and regeneration [13].”
BackgroundBiomarkers shared by frailty and sarcopenia in older adults: A systematic review and meta-analysis
Picca, A., Coelho‐Júnior, H. J., Calvani, R., Marzetti, E., & Vetrano, D. L. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101530 · Cited by 383
Atrogin-1, MuRF-1, and sarcopenia
Gumucio, J. P., & Mendias, C. L. (2012) · Endocrine · doi:10.1007/s12020-012-9751-7 · Cited by 378
“Compared with wild-type controls, transgenic mice that overexpress IGF-1 under the control of muscle-specific promoters has increased muscle mass, CSA, and maximum isometric force [25].”
Looking back to the embryo: defining transcriptional networks in adult myogenesis
Parker, M. H., Seale, P., & Rudnicki, M. A. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1109 · Cited by 366
Signaling pathways perturbing muscle mass.
Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359
Zanou, N., & Gailly, P. L. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1330-4 · Cited by 378
“IGFs are involved at different steps of myogenesis and muscle regeneration: they activate satellite cell proliferation (hyperplasia), increase protein synthesis (hypertrophy), and promote differentiation [28, 93, 107–109].”
BackgroundThe Neuromuscular Junction: Aging at the Crossroad between Nerves and Muscle
González‐Freire, M., de Cabo, R., Studenski, S. A., & Ferrucci, L. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00208 · Cited by 386
“In accordance with this hypothesis, in mouse models, the overexpression of musclespecific IGF-1 reverses sarcopenia (Musaro et al., 2001), prevents the age-dependent decrease in type IIB and increase in type IIA fibers (Messi and Delbono, 2003), and also leads to improved nerve regeneration by…”
BackgroundMuscle expression of a local Igf-1 isoform protects motor neurons in an ALS mouse model
Dobrowolny, G., Giacinti, C., Pelosi, L., Nicoletti, C., Winn, N., Barberi, L., Molinaro, M., Rosenthal, N. A., & Musarò, A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200407021 · Cited by 352
“In contrast, the mIgf-1 isoform used in our present and previous studies (Barton-Davis et al., 1998; Musarò et al., 2001; Barton et al., 2002; Musarò et al., 2004) does not enter the circulation, but accumulates in the tissue of synthesis where its autocrine/paracrine function is concentrated.”
BackgroundMethodInfluentialSelf-citationRoles of insulin-like growth factor (IGF) binding proteins in regulating IGF actions
Duan, C., & Xu, Q. (2005) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2004.12.022 · Cited by 354
“, 1993), while enhanced local IGF-1 expression maintains muscle mass and strength during aging (Musaro et al., 2001).”
BackgroundKunkel, S. D., Suneja, M., Ebert, S. M., Bongers, K. S., Fox, D. K., Malmberg, S. E., Alipour, F., Shields, R. K., & Adams, C. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.020 · Cited by 345
“, 2005) and stimulatesmuscle hypertrophy (Barton-Davis et al., 1998; Musaro et al., 2001).”
The role of myostatin in muscle wasting: an overview
Elkina, Y., von Haehling, S., Anker, S. D., & Springer, J. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0035-5 · Cited by 371
“Reduced adiposity was observed in different transgenic mouse models of muscle hypertrophy [33–35].”
BackgroundMuscle-specific expression of IGF-1 blocks angiotensin II–induced skeletal muscle wasting
Song, Y., Li, Y., Du, J., Mitch, W. E., Rosenthal, N. A., & Delafontaine, P. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22324 · Cited by 352
“Transgene expression is reduced in slow muscles such as the soleus, where the MLC regulatory cassette is characteristically expressed at very low levels (32).”
BackgroundMethodSelf-citationSandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340
“…mass divided by total body mass in percentage pMex plasmid containing the 1,500-bp fragment of the MLC promoter, an 840-bp fragment of SV40 poly(A), and a 900-bp fragment from the 3 0 end of the MLC1f/3f gene, which acts as an enhancer, described in (Grieshammer et al. 1992; Musaro et al. 2001).”
BackgroundMethodInfluentialSelf-citationPI3 Kinase Regulation of Skeletal Muscle Hypertrophy and Atrophy
Glass, D. J. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_78 · Cited by 343
“1991), as was demonstrated in transgenic mice in which IGF-1 is overexpressed in skeletal muscle (Coleman et al. 1995; Musaro et al. 2001).”
BackgroundDrug‐screening platform based on the contractility of tissue‐engineered muscle
Vandenburgh, H. H., Shansky, J., Benesch, F., Barbata, V., Reid, J., Thorrez, L., Valentini, R. F., & Crawford, G. (2008) · Muscle & Nerve · doi:10.1002/mus.20931 · Cited by 324
Yang, S. Y., & Goldspink, G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02918-6 · Cited by 321
Rapid formation of functional muscle in vitro using fibrin gels
Huang, Y., Dennis, R. G., Larkin, L. M., & Baar, K. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00273.2004 · Cited by 316
“The importance of IGF-I in muscle growth is most strikingly demonstrated by the twofold increase in muscle size in mice carrying a transgene for muscle-specific overexpression of IGF-I (6, 19).”
BackgroundMourkioti, F., Kratsios, P., Luedde, T., Song, Y.-H., Delafontaine, P., Adami, R., Parente, V., Bottinelli, R., Pasparakis, M., & Rosenthal, N. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28721 · Cited by 326
Self-citationHill, M., & Goldspink, G. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.035832 · Cited by 313
“Similar experiments by other groups have also been carried out using a viral construct containing the liver type of IGF-I, which resulted in a 25 % increase in muscle mass, but this took over 4 months to develop (Musaro et al. 2001).”
BackgroundMethodAdvances in signaling in vertebrate regeneration as a prelude to regenerative medicinePreprint
Stoick-Cooper, C. L., Moon, R. T., & Weidinger, G. (2007) · Genes & Development · doi:10.1101/gad.1540507 · Cited by 309
“While loss-of-function evidence for an in vivo requirement of IGF signaling in muscle regeneration is not available, targeted overexpression of IGF in muscle has spectacular beneficial effects on regeneration after injury, muscle degeneration in muscular dystrophy mdx model mice, and on agerelated muscular atrophy and…”
BackgroundChronic inflammation and the effect of IGF-I on muscle strength and power in older persons
Barbieri, M., Ferrucci, L., Ragno, E., Corsi, A., Bandinelli, S., Bonafè, M., Olivieri, F., Giovagnetti, S., Franceschi, C., Guralnik, J. M., et al. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00319.2002 · Cited by 303
“Several studies suggest that insulin-like growth factor I (IGF-I) is an important modulator of muscle mass and function not only during the developmental period but across the entire life span (8, 23).”
BackgroundEffects of Resistance Exercise on Bone Health
Hong, A. R., & Kim, S. W. (2018) · Endocrinology and Metabolism · doi:10.3803/enm.2018.33.4.435 · Cited by 291
Lifelong physical exercise delays age-associated skeletal muscle decline
Zampieri, S., Pietrangelo, L., Loefler, S., Fruhmann, H., Vogelauer, M., Burggraf, S., Pond, A., Grim-Stieger, M., Cvecka, J., Sedliak, M., et al. (2015) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu006 · Cited by 282
Self-citationThe muscle fiber type–fiber size paradox: hypertrophy or oxidative metabolism?
Wessel, T. V., HAAN, A. D., van der Laarse, W. J., & Jaspers, R. T. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1545-0 · Cited by 303
“In contrast, other studies using various models of hypertrophy did not show an active role for calcineurin in increasing fiber size in muscles of mice and rats (Bodine et al. 2001b; Musaro et al. 2001; Serrano et al. 2001).”
ResultMuscle injuries and strategies for improving their repair
Laumonier, T., & Ménétrey, J. (2016) · Journal of Experimental Orthopaedics · doi:10.1186/s40634-016-0051-7 · Cited by 297
“Gene therapy may be an effective method by which to deliver high, maintainable concentrations of growth factor to injured muscle (Barton-Davis et al. 1998; Barton et al. 2002; Musaro et al. 2001).”
IGF-1, inflammation and stem cells: interactions during muscle regeneration
Mourkioti, F., & Rosenthal, N. A. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.08.002 · Cited by 279
Self-citationPelosi, L., Giacinti, C., Nardis, C., Borsellino, G., Rizzuto, E., Nicoletti, C., Wannenes, F., Battistini, L., Rosenthal, N. A., Molinaro, M., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7690com · Cited by 268
“cated as a central regulator of muscle regeneration (8).”
BackgroundMethodInfluentialSelf-citationSerrano, A. L., Murgia, M., Pallafacchina, G., Calabria, E., Coniglio, P., Lømo, T., & Schiaffino, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231148598 · Cited by 265
Invited Review: Autocrine/paracrine IGF-I and skeletal muscle adaptation
Adams, G. R. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01264.2001 · Cited by 266
Lu, H., Huang, D., Saederup, N., Charo, I. F., Ransohoff, R. M., & Zhou, L. (2010) · The FASEB Journal · doi:10.1096/fj.10-171579 · Cited by 279
“Transgenic mice overexpressing IGF-I in skeletal muscle displayed marked muscle hypertrophy and sustained hypertrophy and regeneration in senescent muscle (47).”
BackgroundThe Potential of Muscle Stem Cells
Seale, P., Asakura, A., & Rudnicki, M. A. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00049-1 · Cited by 258
Lu, H., Huang, D., Ransohoff, R. M., & Zhou, L. (2011) · The FASEB Journal · doi:10.1096/fj.10-178939 · Cited by 264
Excitation‐transcription coupling in skeletal muscle: the molecular pathways of exercise
Gundersen, K. (2010) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2010.00161.x · Cited by 281
“Also transgenic mice overexpressing IGF-1 selectively in muscle cells display muscle hypertrophy (Coleman et al., 1995; Musaro et al., 2001).”
BackgroundSpangenburg, E. E., Roith, D. L., Ward, C. W., & Bodine, S. C. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.141507 · Cited by 259
“…of myotube diameters and a higher protein content (Rommel et al. 2001; Vyas et al. 2002), while the delivery of exogenous IGF-I either through osmotic pumps or genetic over-expression results in enhanced muscular mass in rodents (Adams & McCue, 1998; Musaro et al. 2001).”
BackgroundEffects of IGF-1 isoforms on muscle growth and sarcopenia
Ascenzi, F., Barberi, L., Dobrowolny, G., Villa Nova Bacurau, A., Nicoletti, C., Rizzuto, E., Rosenthal, N., Scicchitano, B. M., & Musarò, A. (2019) · Aging Cell · doi:10.1111/acel.12954 · Cited by 250
“In previous works, we demonstrated that localized IGF‐1Ea transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle (Musarò et al., 2001).”
BackgroundSelf-citationNeural control of aging skeletal muscle
Delbono, O. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00011.x · Cited by 248
“Acetylcholine binds to nicotinic acetylcholine receptors, leading to an increase in sodium and potassium conductance in the endplate membrane.”
BackgroundStem cell-mediated muscle regeneration is enhanced by local isoform of insulin-like growth factor 1
Musarò, A., Giacinti, C., Borsellino, G., Dobrowolny, G., Pelosi, L., Cairns, L., Ottolenghi, S., Cossu, G., Bernardi, G., Battistini, L., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0303792101 · Cited by 247
Self-citationPericytes at the intersection between tissue regeneration and pathology: Figure 1
Birbrair, A., Zhang, T., Wang, Z., Messi, M. L., Mintz, A., & Delbono, O. (2014) · Clinical Science · doi:10.1042/cs20140278 · Cited by 253
Blaauw, B., Canato, M., Agatea, L., Toniolo, L., Mammucari, C., Masiero, E., Abraham, R., Sandri, M., Schiaffino, S., & Reggiani, C. (2009) · The FASEB Journal · doi:10.1096/fj.09-131870 · Cited by 244
“It is worth noting that, in the present model of hypertrophy, the physiological assays were performed on a variety of muscles that in 3 wk had developed a hypertrophy of 50%, much greater than that observed ( 20%) in mice overexpressing IGF-1 all their life (1).”
BackgroundInfluentialPrevention and treatment of cancer cachexia: New insights into an old problem
Muscaritoli, M., Bossola, M., Aversa, Z., Bellantone, R. D. A., & Fanelli, F. R. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.07.026 · Cited by 241
“6) of skeletal muscle in an endocrine or paracrine/ autocrine fashion [104–107]; and that high and constant muscle levels of IGF-1 are able to induce muscle hypertrophy has been demonstrated in several studies where IGF-1 has been locally infused, introduced inmusclewith recombinant viruses, or locally hyperexpressed…”
BackgroundAutologous Transplantation of Muscle-Derived CD133+ Stem Cells in Duchenne Muscle Patients
Torrente, Y., Belicchi, M., Marchesi, C., D’Antona, G., Cogiamanian, F. M., Pisati, F., Gavina, M., Giordano, R., Tonlorenzi, R., Fagiolari, G., et al. (2007) · Cell Transplantation · doi:10.3727/000000007783465064 · Cited by 247
The hormonal action of IGF1 in postnatal mouse growth
Στρατικόπουλος, Η., Szabolcs, M. J., Dragatsis, I., Klinakis, A., & Efstratiadis, A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809223105 · Cited by 232
“We note that in two reports describing muscle-specific transgenic overexpression of Igf1 (26, 27) there was no change in serum IGF1, despite a 47-fold higher than normal level of the peptide in muscle extracts in one of the cases (26).”
BackgroundPeripheral Muscle Wasting in Chronic Obstructive Pulmonary Disease
Debigaré, R., Côt́e, C. H., & Maltais, F. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.164.9.2104035 · Cited by 230
Girgenrath, S., Song, K., & Whittemore, L.-A. (2004) · Muscle & Nerve · doi:10.1002/mus.20175 · Cited by 238
Owino, V., Yang, S. Y., & Goldspink, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02825-3 · Cited by 227
Metadata
- Authors
- Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., Barton, E. R., L Sweeney, H., & Rosenthal, N.
- Affiliations
- Massachusetts General Hospital (US)
- Sapienza University of Rome (IT)
- University of Pennsylvania (US)
- Corresponding author
- Rosenthal, Nadia
- ORCID
- Venue
- Nature Genetics
- Published
- 2001-02
- Volume
- 27
- Issue
- 2
- Pages
- 195-200
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W1562705858
- Cited by
- 1,137
- References
- 30
- Citations by year
- 2026: 17 · 2025: 19 · 2024: 27 · 2023: 22 · 2022: 21 · 2021: 27 · 2020: 29 · 2019: 35 · 2018: 38 · 2017: 28 · 2016: 34 · 2015: 60 · 2014: 52 · 2013: 59 · 2012: 71
- FWCI
- 17.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Genetics (clinical) › Neurogenetic and Muscular Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Physical Performance
- Keywords
- insulin-like growth factor I, skeletal muscle aging, muscle atrophy, myocyte hypertrophy, muscle regeneration, muscle fibrosis, GATA2, transgenic mouse model, muscle strength
- MeSH terms
- Animals, Cachexia, DNA-Binding Proteins, Hypertrophy, Insulin-Like Growth Factor I, Mice, Transgenic, Organ Size, Regeneration, Tissue Distribution, Transcription Factors, Cellular Senescence, Muscle, Skeletal, Neurodegenerative Diseases, Protein Isoforms, GATA2 Transcription Factor, Mice
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