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http://purl.uniprot.org/citations/29208687http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29208687http://www.w3.org/2000/01/rdf-schema#comment"Little is known about the molecular regulation of skeletal muscle protein turnover during exercise in field conditions where energy is intake inadequate. Here, 17 male and 7 female soldiers performed an 8 days long field-based military operation. Vastus lateralis muscle biopsies, in which autophagy, the ubiquitin-proteasome system, and the mTORC1 signaling pathway were studied, were collected before and after the operation. The 187 h long operation resulted in a 15% and 29% negative energy balance as well as a 4.1% and 4.6% loss of body mass in women and men, respectively. After the operation protein levels of ULK1 as well as the phosphorylation of ULK1Ser317 and ULK1Ser555 had increased by 11%, 39%, and 13%, respectively, and this was supported by a 17% increased phosphorylation of AMPKThr172 (< 0.05). The LC3b-I/II ratio was threefold higher after compared to before the operation (< 0.05), whereas protein levels of p62/SQSTM1 were unchanged. The β1, β2, and β5 activity of the proteasome and protein levels of MAFbx did not change, whereas levels of MuRF-1 were slightly reduced (6%, < 0.05). Protein levels and phosphorylation status of key components in the mTORC1 signaling pathway remained at basal levels after the operation. Muscle levels of glycogen decreased from 269 ± 12 to 181 ± 9 mmol·kg dry·muscle-1 after the exercise period (< 0.05). In conclusion, the 8 days of field-based exercise resulted in induction of autophagy without any increase in proteasome activity or protein ubiquitination. Simultaneously, the regulation of protein synthesis through the mTORC1 signaling pathway was maintained."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.org/dc/terms/identifier"doi:10.14814/phy2.13518"xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Jakobsson M."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Moberg M."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Ekblom B."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Ponten M."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Mattsson C.M."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Ekblom-Bak E."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Flockhart M."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Hendo G."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/author"Soderlund K."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/name"Physiol Rep"xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/title"Increased autophagy signaling but not proteasome activity in human skeletal muscle after prolonged low-intensity exercise with negative energy balance."xsd:string
http://purl.uniprot.org/citations/29208687http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/29208687http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29208687
http://purl.uniprot.org/citations/29208687http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29208687
http://purl.uniprot.org/uniprot/#_O75385-mappedCitation-29208687http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29208687
http://purl.uniprot.org/uniprot/O75385http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29208687