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The underlying mechanisms remain elusive.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Fed wild type (WT), 2\u2010day fasted WT, muscle\u2010specific insulin (INS) receptor (IR) knockout (M\u2010IR<jats:sup>\u2212\/\u2212<\/jats:sup>), and MKR mice were studied with regard to acute effects of the \u03b2<jats:sub>2<\/jats:sub>\u2010agonist formoterol (FOR) on protein metabolism and signalling events. MKR mice express a dominant negative IGF1 receptor, which blocks both INS\/IGF1 signalling. All received one injection of FOR (300\u00a0\u03bcg\u00a0kg<jats:sup>\u22121<\/jats:sup> subcutaneously) or saline. Skeletal muscles and serum samples were analysed from 30 to 240\u00a0min. For the study of chronic effects of FOR on muscle plasticity and function as well as intracellular signalling pathways, fed WT and MKR mice were treated with formoterol (300\u00a0\u03bcg\u00a0kg<jats:sup>\u22121<\/jats:sup>\u00a0day<jats:sup>\u22121<\/jats:sup>) for 30\u00a0days.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>In fed and fasted mice, one injection of FOR inhibited autophagosome formation (LC3\u2010II content, 65%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) that was paralleled by an increase in serum INS levels (4\u2010fold to 25\u2010fold, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) and the phosphorylation of Akt (4.4\u2010fold to 6.5\u2010fold, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) and ERK1\/2 (50% to two\u2010fold, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05). This led to the suppression (40\u201370%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) of the master regulators of atrophy, FoxOs, and the mRNA levels of their target genes. FOR enhanced (41%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) protein synthesis only in fed condition and stimulated (4.4\u2010fold to 35\u2010fold, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) the prosynthetic Akt\/mTOR\/p70S6K pathway in both fed and fasted states. FOR effects on Akt signalling during fasting were blunted in both M\u2010IR<jats:sup>\u2212\/\u2212<\/jats:sup> and MKR mice. Inhibition of proteolysis markers by FOR was prevented only in MKR mice. Blockade of PI3K\/Akt axis and mTORC1, but not ERK1\/2, in fasted mice also suppressed the acute FOR effects on proteolysis and autophagy. Chronic stimulation of \u03b2<jats:sub>2<\/jats:sub>\u2010adrenoceptors in fed WT mice increased body (11%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) and muscle (15%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) growth and downregulated atrophy\u2010related genes (30\u201340%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05), but these effects were abolished in MKR mice. Increases in muscle force caused by FOR (WT, 24%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) were only partially impaired in MKR mice (12%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05), and FOR\u2010induced slow\u2010to\u2010fast fibre type shift was not blocked at all in these animals. In MKR mice, FOR also restored the lower levels of muscle SDH activity to basal WT values and caused a marked reduction (57%, <jats:italic>P\u00a0\u2264<\/jats:italic>\u00a00.05) in the number of centrally nucleated fibers.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p>NS\/IGF1 signalling is necessary for the anti\u2010proteolytic and hypertrophic effects of <jats:italic>in vivo<\/jats:italic> \u03b2<jats:sub>2<\/jats:sub>\u2010adrenergic stimulation and appears to mediate FOR\u2010induced enhancement of protein synthesis. INS\/IGF1 signalling only partially contributes to gain in strength and does not mediate fibre type transition induced by FOR.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcsm.12395","type":"journal-article","created":{"date-parts":[[2019,4,1]],"date-time":"2019-04-01T11:35:53Z","timestamp":1554118553000},"page":"455-475","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Insulin\/IGF1 signalling mediates the effects of \u03b2<sub>2<\/sub>\u2010adrenergic agonist on muscle proteostasis and growth"],"prefix":"10.1002","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2621-3330","authenticated-orcid":false,"given":"Dawit A.","family":"Gon\u00e7alves","sequence":"first","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"},{"name":"Department of Biochemistry\/Immunology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"},{"name":"Department of Biomedical Sciences University of Padova  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6171-7940","authenticated-orcid":false,"given":"Wilian A.","family":"Silveira","sequence":"additional","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leandro H.","family":"Manfredi","sequence":"additional","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fl\u00e1via A.","family":"Gra\u00e7a","sequence":"additional","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Armani","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences University of Padova  Padova Italy"},{"name":"Venetian Institute of Molecular Medicine  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Enrico","family":"Bertaggia","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences University of Padova  Padova Italy"},{"name":"Venetian Institute of Molecular Medicine  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian T.","family":"O\u00b4Neill","sequence":"additional","affiliation":[{"name":"Section on Integrative Physiology and Metabolism, Joslin Diabetes Center Harvard Medical School  Boston MA USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Lautherbach","sequence":"additional","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliano","family":"Machado","sequence":"additional","affiliation":[{"name":"Department of Physiology Ribeir\u00e3o Preto Medical School\/University of S\u00e3o Paulo  Ribeir\u00e3o Preto SP Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leonardo","family":"Nogara","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences University of Padova  Padova Italy"},{"name":"Venetian Institute of Molecular Medicine  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo G.","family":"Pereira","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences University of Padova  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diletta","family":"Arcidiacono","sequence":"additional","affiliation":[{"name":"Digestive Endoscopy Unit Veneto Institute of Oncology IOV\u2010IRCCS  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Realdon","sequence":"additional","affiliation":[{"name":"Digestive Endoscopy Unit Veneto Institute of Oncology IOV\u2010IRCCS  Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. 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